Science topic

Membranes - Science topic

Thin layers of tissue which cover parts of the body, separate adjacent cavities, or connect adjacent structures.
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Hello all, in DPPC/DOPC/cholesterol ternary system, we observe ld-lo phase separation. My question is why cholesterol prefers to stay with DPPC rather than DOPC. Thank you.
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How extensive was the separation? Was it published?
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For lateral flow test development, which membrane do you recommend most for conjugated pad? I currently use Whatman STANDARD 17 from Cytiva
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I really love Ahlstrom grade 8980 if you need a glass fiber, or Ahlstrom grade 6614 for a polyester material. Both are very robust.
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I have made TL reagent by mixing antibody in 1X PBS containing 0.25% sucrose for striping similarly the CL which is anti species of TL and prepared using the above composition. While running the LFA, I can see both TL and CL increases linearly with my analyte concentration which was strange.
I have found out with my investigation that my test line antibody move during the running of the lateral flow and the TL antibody gets captured at the CL and forms the sandwich with the analyte there and hence I see the linear correlation with the analyte.
I need to know how can I immobilize my antibody firmly to the nitrocellulose membrane, such that it does not move and interfere with CL antibody.
Thanks,
Yogita
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How high is your test line concentration? The nitrocellulose capacity for protein is finite, and you will get diminishing returns about 2 mg/mL. If it is higher than that, it can wash off and bind to the control line as you have seen. You also might have to cure the membrane by placing it at an elevated temperature for a day or two. This will better anchor the test line to the nitrocellulose, especially if you are using sucrose.
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I've been running a simulation of thermal expansion. Two parts are defined and conected via TIE. one of the parts is surrouneded by a fixed (ENCASTRE) membrane surface, and the two are defined in general contact as pairs.
During thermal expansion I found the following warning:
"Some nodes involved in general contact have penetrated their  tracked faces by more than 50.000 percent of the typical element dimension in the general contact domain."
The contact seemed to be ignored, as there is a deep penetration of the internal part through the outer membrane surface, despite the high density of the outer surface mesh.
The penetration is not only in the TIE area, but scatered all across.
Defining a Thickness surface to the parts in contact was impractical.
More info:
Abaqus version: 2017 Explicit.
TIE:
Hard contact
constraint enforcement method -
(Normal) Default. Allow separation after contact,
(Tangential) Fricttionless. 0;
Material properties:
Inner part:
*Material, name=RUBBER
*Density
1e-09,
*Hyperelastic, neo hooke, moduli=INSTANTANEOUS
200.,0.
*Viscoelastic, time=RELAXATION TEST DATA, nmax=5
*Shear Test Data, shrinf=0.3
1., 0.01
0.9, 0.4
0.82, 1.
0.72, 2.
0.56, 5.
0.44, 10.
0.38, 20.
0.3, 50.
*Expansion
0.001
Outer part:
*Material, name="Outer Shell"
*Density
1e-09,
*Elastic
9000, 0.29
How can I fix that?
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Were you were able to resolve it?
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I need to show the co-localization of my protein of interest in the membrane in HL60 round and small cells. So I took z-stack images to show the surface expression of the membrane marker that I used. But I don't know how to present my data for the paper.
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We usually use a proprietary software called MetaMorph. But either of the two you mentioned should work. I would start with Fiji.
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Regarding Egg membranes as model cell membranes for diffusion experiments.
which is better, the synthetic membranes or egg membrane
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Agreed.
C.A. (Kees) Kan Thank you for sharing the knowledge.
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Hi all,
I'm looking to conduct screening on a cell line of interest, using the Boyden Chamber Assay method, to identify migratory vs non-migratory phenotypes and then elucidate their matching genotypes.
I was wondering if anyone had any ideas of how to reliably separate the migrating cells on the lower transwell membrane, from the non-migratory cells suspended in the upper chamber?
Any ideas are appreciated...thanks!
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you can deploy Copilot Separating migratory and non-migratory cells in a Boyden Chamber Assay can be a bit tricky, but here are some steps and tips to help you out:
### Steps to Separate Migratory and Non-Migratory Cells
1. **Prepare the Boyden Chamber:**
- **Upper Chamber:** Place your cell suspension in the upper chamber.
- **Lower Chamber:** Fill the lower chamber with a medium containing chemoattractants to encourage cell migration.
2. **Incubation:**
- Allow the cells to incubate for the appropriate time to enable migration through the membrane.
3. **Collecting Migratory Cells:**
- **Remove the Upper Chamber:** Carefully remove the upper chamber without disturbing the lower chamber.
- **Wash the Membrane:** Gently wash the membrane to remove any non-migratory cells that might be loosely attached.
- **Scrape the Membrane:** Use a cell scraper to collect the migratory cells from the lower side of the membrane. Alternatively, you can use trypsin to detach the cells.
4. **Collecting Non-Migratory Cells:**
- **Upper Chamber Cells:** Collect the non-migratory cells that remain in the upper chamber by gently pipetting them out.
### Tips for Reliable Separation
- **Gentle Handling:** Be gentle when handling the cells to avoid disrupting the membrane or causing cell damage.
- **Optimal Pore Size:** Ensure that the pore size of the membrane is appropriate for your cell type. Typically, a pore size of 8 µm is suitable for most cell types.
- **Staining:** Stain the cells to differentiate between migratory and non-migratory cells. This can help in visualizing and counting the cells accurately.
- **Validation:** Use complementary techniques like flow cytometry or microscopy to validate the separation and ensure the purity of the collected cell populations.
### References
- **[Cell Migration and the Boyden Chamber](https://link.springer.com/protocol/10.1385/1-59259-137-X:047)**
- **[Discussion of Cell Migration Assay Formats](https://www.cellbiolabs.com/news/discussion-cell-migration-assay-formats)**
These steps and tips should help you effectively separate migratory and non-migratory cells in your Boyden Chamber Assay.
Good luck
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Is there any explanation for the strange curve feature at the beginning of the AFM tip contacting the sample membrane? Is it that there is some dust attaching the AFM tip or any other reason? How to avoid it?
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This is quite common when the tip adhere to cell membrane. See the reference:
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Hello, I have started working with Western blot recently and have difficulties getting the beta-actin band. I recently tried the steps for getting a beta-actin band from the intestinal sample of mice. I mentioned it here.
1- 10μl or a maximum of 20μl of protein into each well. Start at 100 V for 1-1:30 h.
2- Transfer protein from gel to membrane (make sandwich) 100V, 1:30h
• PDVF membrane; 1 min in methanol 100% for activating. However, I only get bands on the membrane after staining but no bands after the antibody-blocking steps.
I would be so happy if you could suggest me t how I can solve this problem.
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Hanieh Tajdozian Hi, Could you find the solution to this problem? I do have the same issue.
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Hi there. Have anybody noticed that the membrane time constant values in membrane test are in rage of micro-seconds (hundreds of microseconds but rarely more than few milliseconds). We are patching pyramidal neurons in neocortex, where the tau should be around 10-30 ms or more. The tau values based on on I-V tests in current clamp give us expected values around 30 ms. Can anybody explain why the tau values from membrane test (in VC) are so much off?
Thanks
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I noticed this discrepancy long time ago and I think it should be addressed by Axon ASAP. The membrane test in pClamp is performed in Voltage Clamp and the time constant is calculated by method described in Axon manual yet, it is obviously not just exponential fitting typically performed on initial segment of the pulse in Current Clam clamp (that returns those higher values for tau). Unfortunately I don't really know how to compare both or how to address this discrepancy (Axon/Molecular Probes should). I typically go with fitting performed on traces in CC performed with .ab files by software like Neuroexpress (by Dr. A. Szucs). I hope this helps...
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When dealing with the fabrication of Ceramic membrane using Fly Ash & Clay or Kaolin, using sodium silicate as binding agent it breaks & turns into powder at room temperature after sintering at 800°C. Which binding agent is suitable to avoid the turning of membrane into powder form after sintering?
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Exactly, that's what we have not covered. As the calcination also helps in greater binding strength later on along with impurities removal. Thank you Sir for providing valuable answer & filling on my gap..
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For unknown reasons I started to notice that after sometimes (0.5-1.0 hr) of operating crossflow filtration system, the flux increases steadily with corresponding decrease of rejection of the monitored ions (SO4 and Cl-). several types of membranes were tested with the same problem including NF270, BW30, NF, NFS, etc.
initially we thought something wrong with the cell so we changed it and used brand new Sterlitech cell. We also thought that some needle like pracipitates may have formed, we cleaned the whole system using 4 % cetric acid by circulation for 30 min then thoughly circulating UPW.
The cell we are using is Sepa CF Med/High Foulant System, 316 SS, 75 Mil with an active area of 140 cm2.
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The increase in flux with a corresponding decrease in ion rejection during wastewater filtration with NF membranes could stem from several factors. Membrane compaction or relaxation under high pressure may initially alter pore structures, increasing flux but reducing ion selectivity. Temperature effects are also relevant, as even slight increases in feed water temperature lower viscosity, enhancing flux while decreasing rejection. Another potential factor is concentration polarization, where solute buildup near the membrane surface alters local osmotic pressure, reducing ion rejection and pushing flux upward. Membrane fouling could further complicate this issue, as loose fouling layers might dissolve or change over time, impacting filtration performance despite your cleaning with citric acid. Finally, surface degradation from ions or feed contaminants may contribute to increased permeability and reduced rejection. Monitoring system temperature, adjusting shear rates, or analyzing membrane surfaces post-filtration could provide insights into these challenges.
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we are tried all different concentrations of polymer (Polysulfone) and solvents (NMP & DMF) to synthesis FO membrane. but unfortunately every time polymer penetration occurs across the fabric that results in poor water flux in FO testing.
kindly guide a way through which we can avoid penetration of solvent across the support fabric.
thank you
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First of all, sorry for late response.
In our work, we applied different types of polymeric hydrogels, and we did not noticed any penetration of the particles.
According to our experimental work and our readings, this issue does not exist in the application of hydrogels as draw agents because it is a solid dry material, which swells with water without dissolution.
The phenomenon of reverse diffusion of solutes occurs when solutions are applied as draw agents, and it is called reverse solute flux. This issue is widely discussed in previous studies.
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Hello,
I obtain western blot bands at desired region on the membrane but there is no space between the bands (attaching image for reference), may i know what could be the reason?
TIA
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The bands on the gel are not continuous. You still see the boundaries between the 6 samples, they have just migrated closely together. This is a normal effect of SDS-PAGE, since the differences in salt concentartions and pH between the gel and the samples lead to a broadening of the samples (electric current pulling the proteins not only downwards, but also sidewards at the edges), which is usually stooped when the sample from the neighboring well interferes with sidewards movement. If you need to have free space beween the samples, leave one lane free (or better fill it with empty loading buffer) between the samples.
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Hello, we have been struggling with the lots of background in our wb membranes probed with an anti-Streptavidin-HRP from Thermofisher (Pierce 21134). Samples contained biotinilated proteins. Every time there is some blobs somewhere and so much background that it is hard so see our biotinilated proteins. I attached the same pic with different contrast. Did anyone face the same problem?
All stepts have been performed with PBS 1X and here the protocol:
  • After transfer, rinse off membrane for 5 min in PBS
  • Block with BSA blocking buffer (1% filtered BSA and 0.2% Triton x-100 in PBS) for 30 min
  • incubation with streptavidin antibody 1:2000 dilution ON at 4C
  • Rinse off with PBS three times and do ABS blocking (10% adult bovin serum and 1% triton x-100 in PBS) for 5 min
  • Rinse off with PBS three times and incubate with PBS for 5 min
  • Develop with ECL for 5 min and acquire
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@Jasminebaby I also do my WB without ABS but for streptavidin-HRP i noticed that ABS incubation is critical to remove background :( but you can try without and see what happen! You might have a good surprise :)!!
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I made 2 membrane samples of 91% CuO and 93% CuO using the sol-gel method. The SEM image of the grain is obtained evenly but the surface is slightly rough
📷
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Sarada K Gopinathan , thanks, i will sent for you
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A similar ADC HKT288 that used a DM4 payload with anti-CDH6 monoclonal was discontinued over inflammatory and neurological adverse events. Would the adverse events be tied to targeting CDH6 or to payload toxicities?
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The adverse events associated with the discontinuation of the ADC HKT288, which used a DM4 payload and targeted CDH6 (cadherin-6), could potentially be linked to either CDH6 targeting or the DM4 payload itself.
CDH6 is also expressed in normal cells, especially in neural tissue, it may cause drugs to attack not only tumor cells but also normal cells, leading to inflammation and neurological damage.
DM4 is a maytansinoid, a microtubule-disrupting agent. It works by inhibiting microtubule polymerization, leading to cell death, and is a highly potent cytotoxic drug. The neurological toxicity seen with DM4 payloads can arise because microtubules are critical for neuronal function, including intracellular transport, which makes neurons highly susceptible to microtubule inhibitors like DM4. This could explain the neurological side effects (e.g., peripheral neuropathy) observed in patients treated with HKT288.
Inflammatory effects could also be tied to DM4 toxicity, as the drug can affect dividing cells in healthy tissues and provoke inflammatory responses, especially in tissues where microtubules play a critical role (e.g., gut, liver, immune cells).
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I recently found an old bottle of opened chloroform (2.5L) in our lab, we would like to use it for RNA extraction, but not sure if it has been used for other experiments and would be exposed to RNase as there is no marking on it.
I have thought of filtering it but we only have 0.2um filter with PES membrane which is not compatible with chloroform.
I have also searched on the internet to find an answer but nothing appeared.
Has anyone experienced the same before?
please kindly help, thanks!
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Chloroform is cheap, experiments are expensive. Just get a small clean bottle and be safe.
It is likely that the DNase is denatured but RNase can readily refold when back in an aqueous environment, which is why it is hard to get rid of RNase. If it were me, I would not risk it.
Also 0.2um filter would remove cells but not most proteins. Even phages and viruses would pass through.
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Hi guys. I was wondering if you guys have any suggestions on staining live cells for long time (ideally at least 5 hours)? I want to at least define where the cell boundary is, and hopefully it should be a red dye so it will have less crosstalk with my another green dye. I have tried several dyes but none of them satisfies me:
  1. Plasma membrane dye like CellMask and DiD: these dyes can visualize membrane well but just cannot retain too long (up to 1 hour for DiD and 4 hours for cellmask). They will be internalized into cells and can barely be seen on the membrane.
  2. SYTO 61 and 62. These dyes are for staining nucleic acid, but are actually good for seeing membrane cause it will also stain cytoplasm. The bad thing is that they make my cells super bright on green fluorescence due to unknown reason (probably cell stress) and just cannot be used for my purpose.
  3. SiR actin for staining the F-actin of cells. These are great in background and won't be internalized fast like PM dyes. However, my cells are probably not fully covered by F-actin and there are always space that is not stained by SiR actin but clearly is a part of cells.
I am running out of ideas now. The only option left is expressing fluorescent proteins tagged to other membrane proteins. CellBrite steady looks like another great choice since it is expected to retain signal at the PM for more than 24 hours. It might work but just could take too much time. Would appreciate it if anyone have experience on this topic ;)
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I would suggest CellTracker in the version CellTracker™ Red CMTPX if it should be a dye or if you would like to stain only the membranes you might want to try CellLight™ Plasma Membrane-RFP, BacMam 2.0 both from Thermo Fisher. I have used the later with different tags and it worked great for me.
The CellTrackers are really good, the CMAC, CMFDA and CMTPX are all great and should last for days.
Best wishes
Soenke
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Hi all,
Thank you in advance.
I labelled my membrane receptor (a GPCR 41 kDa; approx 80 kDa with SNAP at N-terminus and nLuc at C-terminus) with SNAP-AlexaFluor-488 (surface/non-permeable) and SNAP-647-SiR (permeable to the membrane). Lysed cells, collected total protein (stored on ice), stored at -20 dC for a week. Ran 10 uL supernatant on mPAGE™ 4-12% Bis-Tris Precast Gel, 10x8 cm. Electrophoresed first at 60V for 6 min (for protein to enter the gel) and then at 200 V for 33 min at room temperature in MOPS running buffer. Post-electrophoresis washed gel with tap water three times for 5 minutes. Scanned on Amersham Typhoon gel scanner using filter Cy2 (488 nm), Cy5 (635 nm), and Cy3 (532 nm). I see no problem with the Cy2 channel, but with the other two channels the images are weird - the gel appears granular, with white patches.
Note: while setting up the tank (just before loading the samples and filling the running buffer) I think I first slightly overtightened to create a seal but stopped and loosened it.
Please find the attached images
Please let me know if you need more information from my end.
Thank you once again.
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Hello Bhardwaj,
I couldn't give a definitive answer but I could give 1 potential answer for this. It could be due to incomplete dissolving of agarose. Would recommend looking at a similar post that was made on research gate on Dec 14, 2016. Posted by Lorenz Kempeneers.
Hope you the best,
Nicolas
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Hi, I performed western blotting for the 8 times. In two of them I used wet-transfer and the rest of them assayed with semi-dry transfer. I checked my buffers, systems, gels and everything. I used two different primary antibodies which one of them is surely working. In the first 5 assay, I observed signal from the antibody that we know it is working. after we took images, I stained the membrane and observed protein bands on it. but now I can not observe any signal neither of them. and there is any protein bands on membrane. what could go wrong?
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If you do not detect any protein on your membrane after the staining procedure (I guess for your experiment, using ponceau S), it is most probably the transfer issue you are facing...Putting aside the antibody verification, if there is not any protein on your blot but you have them on your gel after SDS-PAGE, this must be investigated during the transfer process. How about your ladder, can you see them on your PVDF membrane? Your PVDF membrane conditioning (pre-wetted with MeOH) protocol has been performed properly?... Applied voltages and transfer protocols are valid and buffers are prepared fresh?... Do you observe this in both semi and wet-transfer platforms?
After blotting has been completed, you may check the gel again and put a secondary PVDF membrane during transfer to see if any protein either passes through the membrane or remains in the gel...This will clarify if this is a transfer issue...
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How does membrane selectivity impact CH4 recovery and CO2 removal efficiency in biogas upgradation?
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Taisir K. Abbas Yes for sure and many people have already tried this along with double and single systems
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I observed GFP-KrasG12D localization in the nucleus by immunostaining, instead of at the membrane where it is typically found. Could this be an artefact, or has anyone else observed this as well?"
best
marianne
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Hi Marianne,
The localization of KrasG12D in the nucleus, as observed with GFP-tagged KrasG12D and immunostaining, can indeed raise some intriguing questions. Here’s how to interpret this finding:
1. Potential Artefact
  • Tag Effects: The GFP tag might influence the protein's localization. Fusion proteins can sometimes exhibit altered localization patterns due to the tag itself.
  • Overexpression: High levels of overexpression might overwhelm normal cellular processes, leading to mislocalization. Ensure that the observed nuclear localization is not due to excessive expression levels.
2. Biological Relevance
  • Nuclear Function: There are precedents for Ras proteins (including Kras) being involved in nuclear processes. For example, Ras can interact with nuclear import machinery or nuclear factors, suggesting that nuclear localization might be functionally relevant in certain contexts.
  • Pathological Context: KrasG12D is a mutant form of Kras associated with oncogenesis. In some cancer contexts, Ras proteins can exhibit aberrant localization patterns, which might reflect altered regulatory mechanisms.
3. Verification
  • Repeat Experiments: Confirm your findings with additional experiments, such as using different tags or methods (e.g., different fixation protocols) to rule out technical artefacts.
  • Colocalization Studies: Perform colocalization studies with known nuclear markers to verify if KrasG12D is truly localized in the nucleus or if the observed pattern is an artefact.
4. Literature Review
  • Existing Studies: Review the literature to see if other studies have reported similar findings. Some research might have documented unconventional localization patterns for Kras mutants, especially in cancer models.
5. Alternative Explanations
  • Cell Type Specificity: The observed nuclear localization might be specific to the cell type or experimental conditions used. Different cell types or stress conditions can influence protein localization.
Summary
While the nuclear localization of KrasG12D might initially seem unexpected, it could be either an artefact of the experimental conditions or a biologically relevant finding. Verification through repeat experiments, literature review, and additional controls will help clarify the nature of this observation.
Best of luck with your research!
Marianne
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I'm looking for protocols/sources that provide information about how to maximize the isolation of membrane bound proteins and general protein yield of unstimulated primary CD4+ T-cells. I have used RIPA and other ThermoScientific specialized protein lysis products and I have not succeeded.
These cells are isolated from fresh PBMCs.
My ultimate goal is to use Western Blot and ELISA as my protein assays.
Any suggestion is welcome. Thanks!
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Maria,
The Mem-PER™ Plus Membrane Protein Extraction Kit from Thermo Fisher utilizes CHAPS as a detergent in its membrane solubilizing mixture (verified in its SDS documentation). So, I guess, to isolate membrane-bound proteins, you can first lyse the cells using a mild detergent to solubilize cytosolic proteins, and then add a buffer based on CAPS to extract the membrane proteins effectively.
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What is the optimal membrane material and configuration for efficient CO2 removal in biogas degradation? About membrane degradation units
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You can prepare to apply the mesoporous honeycomb like 2D void microstructured biopolymeric nanosorbents which also possess a quite number of active binding sites for the effective capturing of CO2.
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What are the common fouling mechanisms in membrane biogas upgradation, and how can they be mitigated? Let us collectively list these down
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Aside from membrane fouling issues from the raw biogas such as by siloxanes and colloids as well as from metal dust particles resulting from gas compression, the major membrane challenges in biogas purification are accelerated aging and plasticization due to the high differential pressures required for separating gas molecules.
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How do operating conditions like pressure, temperature, and flow rate impact membrane performance in biogas purification?
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- The operating pressure plays a crucial role in establishing a pressure gradient between the internal region, where gas flows, and the external region, where permeate gas is collected. Elevated pressures may lead to an expansion of intermolecular spaces (organic membranes) or pores (inorganic membranes), potentially damaging the membrane, particularly if it is composed of organic materials. Conversely, reduced pressures can diminish the pressure gradient, thereby hindering the effective separation of gases.
- Temperature significantly affects the thermodynamic aspects of the process. Increased temperatures enhance molecular diffusion through the membrane; however, this may be detrimental as it can decrease the concentration of the permeate gas by enlarging the intermolecular spaces or pores within the membrane, especially in organic types. In certain scenarios, elevated temperatures can also inhibit gas solubilization within the membrane. At lower temperatures, gas solubilization is favored, yet this can adversely impact gas permeability by constricting the intermolecular spaces or pores.
- The flow rate is intrinsically linked to the residence time of gas within the membrane. A lower gas residence time results in prolonged contact between the gas and the membrane, while a higher residence time leads to reduced contact duration. Increased flow rates may diminish the volume of permeated gas, whereas decreased flow rates can enhance permeation, but more than one membranes are required.
-Inorganic membranes exhibit superior performance in high-pressure (>10 bar) and elevated temperature (>50ºC) environments due to their rigid structural composition. Nevertheless, their production is costly and complex. Conversely, polymeric membranes are better suited for lower pressure (<5 bar) and ambient temperature (<30ºC) applications, although they are prone to quicker degradation over extended use.
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I am getting extra peaks in my XRD graph of essential oil mediated zno nanoparticle which supposed to be of zinc hydroxy nitrates from the literature review. Would this sharp zinc hydroxy nitrate peak has any impact on the membrane stabilizing activity and antimicrobial activity.
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I am not an expert in this field, but I am very interested and have researched to find an answer. I received some assistance from tlooto.com for this response. Could you please review the response below to see if it is correct?
The presence of zinc hydroxy nitrate in ZnO nanoparticle synthesis can affect both membrane stabilizing and antimicrobial activities. Zinc hydroxy nitrate itself exhibits antimicrobial properties [3][4], potentially enhancing the overall efficacy of ZnO nanoparticles. The sharp peaks in your XRD graph indicate a significant presence of zinc hydroxy nitrate, which might alter the interaction of the nanoparticles with microbial membranes, thus enhancing their stabilizing activity [5]. However, the exact impact depends on the concentration and specific microbial strains involved. Further experimental validation is crucial to ascertain these effects [1][2].
Reference
[1] Tiwari, V., Mishra, N., Gadani, K., Solanki, P., Shah, N., & Tiwari, M. (2018). Mechanism of Anti-bacterial Activity of Zinc Oxide Nanoparticle Against Carbapenem-Resistant Acinetobacter baumannii. Frontiers in Microbiology, 9.
[2] Pezzuto, J., Reddy, L. S., Nisha, M., Joice, M., & Shilpa, P. (2014). Antimicrobial activity of zinc oxide (ZnO) nanoparticle against Klebsiella pneumoniae. Pharmaceutical Biology, 52, 1388 - 1397.
[3] Kaur, T., Putatunda, C., Vyas, A., & Kumar, G. (2020). Zinc oxide nanoparticles inhibit bacterial biofilm formation via altering cell membrane permeability. Preparative Biochemistry & Biotechnology, 51, 309 - 319.
[4] Shahbazi, Y., & Shavisi, N. (2018). Chitosan Coatings Containing Mentha spicata Essential Oil and Zinc Oxide Nanoparticle for Shelf Life Extension of Rainbow Trout Fillets. Journal of Aquatic Food Product Technology, 27, 986 - 997.
[5] Hamza, Z. S. (2020). Antibacterial activity of Zinc Oxide Nanoparticle (ZnONP) Biosynthesis by Lactobacillus plantarium aganist pathogenic Bacteria. Indian Journal of Forensic Medicine & Toxicology.
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Hello!
I am preparing liposomes using a membrane extruder.
The procedure is well-known and descibed extensively in the literature:
1. I start with a solution of the lipid in chloroform, then evaporate the chloroform. At this stage I know the mass of the lipid M.
2. I add buffer (volume V) and make several freeze-thaw cycles with vortexing.
3. The resulting mixture goes to extruder and becomes transparent upon several extrusion cycles.
What it the resulting concentration of the lipid? It should be lower than M/V due to adsorption of the lipid onto the membrane and the inner surface if the glass syringes. But what is the typical concentraion loss? Is it 10-15% of M/V?
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Hello,
A phosphate assay measures the concentration of phosphate ions in a sample. Since phospholipids contain phosphate groups, this type of assay can be used to indirectly quantify lipid levels.
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What kind of material can I use as a membrane?
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Dear Ademario,
Thank you for your prompt and thorough response to my question. Your explanation was clear and insightful, and the references you provided will be extremely helpful.
I appreciate your time and expertise.
Best regards,
Rouz
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How does Membrane Scrubbing Technology remove impurities like CO2, H2S, and H2O from raw biogas to produce high-quality BioCNG (>97% CH4) while minimizing methane slip?
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We have no loss of methane with our proven biogas purification strategy and technologies as explained on https://www.researchgate.net/post/Ow_does_Membrane_Scrubbing_Technology_compare_to_other_biogas_upgrading_methods
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After extraction and separation of humic acid and fulvic acid, I need to purify them before characterization. What should be the size of dialysis membranes?
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For purifying soil organic matter, specifically humic and fulvic acids, use dialysis membranes with a Molecular Weight Cut-Off (MWCO) of 1000 to 3500 Daltons. For humic acids, membranes with 3000-3500 Da MWCO are suitable, while for fulvic acids, use membranes with 1000-2000 Da MWCO. This range effectively removes smaller inorganic ions while retaining the larger organic compounds of interest, with the smaller pore size for fulvic acids accounting for their lower molecular weight compared to humic acids.
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I have overexpressed my protein of interest (a single pass transmembrane protein) in C41 (DE3) E.coli cells. Currently, I am trying to solubilise the protein from the membrane using detergents. I have used DDM, OG, CHAPSO, LDAO, and LMNG, but nothing works. Has anyone faced a similar issue? Could someone possibly suggest a solution?
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You may add to your construct a solubility enhancer tag such as MBP or GST...
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I have primary breast cells embedded in the hydrogel. When stained with EpCAM without the hydrogel, the staining was correctly localized to the membrane as expected! However, after embedding in hydrogel and using the same protocol for immunofluorescent, we are now seeing nuclear staining. Have you encountered this issue? Any recommendations on how to resolve it?
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Are you sure that this is an artefact? If the antibody epitope is on the intracellular domain it may be genuine signal.
This paper talks about its translocation:
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Hello,
I am currently working with Malaria Pf/Pan nitrocellulose membranes coated for malaria detection. After drying the coated membranes in an Incubator (overnight at 37°C), I've noticed that they tend to release moisture with time approximately within 15 days. Additionally, the (silica) desiccant turns pink, indicating the presence of moisture. This is causing issues with the stability and performance of the membranes.
Has anyone encountered similar problems or have suggestions on how to resolve this issue? Specifically:
- Is there a more effective drying method or a different drying temperature that could prevent the release of moisture?
- Are there alternative storage conditions or desiccants that could help maintain the dryness of the membranes?
- Does presence of moisture also affects the migration of blood sample from gold conjugate pad?
Note:
- Silica is activated properly.
- Incubator in not placed in DH
Any insights or recommendations would be greatly appreciated.
Thank you!
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Malaria-coated nitrocellulose membranes in rapid diagnostic tests often suffer from moisture-related issues, degrading antibodies or antigens and causing clumping, noise, and damage. To mitigate this, store membranes in dry environments with desiccants, vacuum seal, control temperature and humidity, and use moisture-barrier packaging. Implement rigorous quality control and strict handling protocols to maintain test reliability and integrity.
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I am trying to coat my micelles and PLGA based nanoparticles with cell membrane using an Avanti mini extruder according to literature . I use 200nm membrane but my particles end up to be 400nm And high PDI. Anyone has experience using extruder for this purpose?
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You should have samples of micelles and cell membranes (extracted from cells). Remember that micelles and cell membranes need to be in water, as they self-assemble in water through hydrophobic interactions. The resulting mixture of micelles and membranes (two suspensions) is then extruded 10-20 times through a porous polycarbonate membrane of 400 nm thickness using an Avanti mini-extruder. Such mechanical force created by extrusion facilitates the fusion (self-assembly) of nanoparticles (micelles) with membranes. The consultant gets the impression that you are trying to put the extruder membrane on the micelles.
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Does it exist some special technique for cutting ceramic membranes for Cross-sectional FESEM or SEM images?
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You con use an Ion Milling System to cut the sample out of the SEM and then insert your cross section into the microscope.
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Is there an established protocol to measure the permeability of bacterial membranes?
Thank you
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I also found this assay:
"Microbial adhesion to solvents: a novel method to determine the electron-donor/electron-acceptor or Lewis acid-base properties of microbial cells" (
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Why?
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Yasmine Mabed Replacing Na2O and CaO with Li2O and BaO in glass membrane electrodes extends the pH range to levels greater than 12 due to the following reasons:
1. Increased basicity: Li2O and BaO are more basic than Na2O and CaO, which allows the glass to withstand higher pH levels without dissolving or degrading.
2. Improved durability: The substitution increases the glass's resistance to alkali attack, reducing the risk of damage or degradation at high pH levels.
3. Enhanced stability: Li2O and BaO help maintain the glass's structural stability, even in highly alkaline environments, ensuring consistent electrode performance.
4. Reduced sodium error: Li2O reduces the sodium error, which is a common issue in glass electrodes at high pH levels, allowing for more accurate measurements.
5. Increased lithium ion mobility: Li2O increases the mobility of lithium ions within the glass, facilitating faster and more accurate pH measurements.
By replacing Na2O and CaO with Li2O and BaO, the glass membrane electrode's pH range is extended to levels greater than 12, making it suitable for applications in highly alkaline environments, such as in certain industrial processes or wastewater treatment.
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I am trying to scale up a transwell migration assay for PBMCs and I have preliminary data from 96 well plate format, that shows that my cells migrate towards my attractant through a 5 µm polycarbonate membrane.
No I am trying to establish the same in the 24 well format and am having issues with this. With the same chemoattractant concentration, I see less than 30% of my migratory effect in the 24 well format when compared to the 96 well plate effect I observed so frequently.
The TC-treated inserts I use in the 24 well plate also have 5 µm pores, however membranes are made from PET (polyethylene terephthalate).
Could it be that my cells stick to the PET membrane more and fail to migrate to the lower compartment? Are there any other ways the membrane material could impact migration of PBMCs in this setup?
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Dear Sofya,
I wish you Good Luck for your experiments!
Regards,
Malcolm
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we have a nafion 117 membrane and we want to know if it has the properties claimed by the sellers. what are the tests available ?
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I'm not familiar with this particular membrane, what properties are being claimed? I've tested several membranes by running a comparison between a raw sample and the same sample passed through the membrane. Find a test for what property you are testing and run that before and after.
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I recently got new secondary antibodies but didn't realize they needed to reconstituted prior to use (first time getting fresh ones myself) until after I had finished washing my membrane with TBS-t. How long can my membrane sit in TBS-t? There is 30 minutes between end of last wash and when the secondary antibodies will be ready to use. Should I place the membrane in TBS while I wait?
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Mohammad Baquir Thank you!!
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I want to make sure that the culture medium contains membrane vesicles.
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Takuma Yoshida The key markers of Staphylococcus aureus membrane vesicles (MVs) are:
  • Immunostimulatory DNA, RNA, and peptidoglycan that activate innate immune receptors like Toll-like receptors (TLR2, TLR7, TLR8, TLR9) and NOD2
  • Small RNAs (sRNAs) detected in the RNA content of S. aureus MVs.
  • Variable protein cargo composition, with 131 proteins identified in MVs from S. aureus grown in Luria-Bertani broth and 617 proteins in MVs from brain-heart infusion broth.
  • The number, morphology, and cargo composition of S. aureus MVs can vary depending on the bacterial strain and growth conditions.
To ensure your culture medium contains S. aureus MVs, you should:
1. Use either Luria-Bertani broth or brain-heart infusion broth as the growth medium.
2. Analyze the culture supernatant for the presence of spherical nanovesicles by electron microscopy.
3. Detect the immunostimulatory nucleic acids (DNA, RNA) and peptidoglycan in the vesicle fraction using PCR and immunoassays.
4. Identify the variable protein cargo composition by mass spectrometry proteomics.
The presence of these markers will confirm that your S. aureus culture is producing membrane vesicles that can modulate host immune responses and bacterial pathogenesis.
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I prepared drug loaded HPBCD inclusion complex in two different ways.
1. In the first case, both were mixed under stirring till solvent evaporated and dried
2. In another case, the mixture was filtered using 0.45 micrometer membrane filter and the filtrate was was lyophilized to get the particles.
3. In the other case, both the drug and HPBCD were mixed in closed container using incubator shaker and filtered using 0.45 micrometer membrane filter and the filtrate was was lyophilized to get the particles.
It was observed that the loading efficiency was least in 3 followed by 2 (a little higher than 3) & then 1 (drastically high). Please help me with the possible reasons.
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Bably Khatun The filtrate particles typically have lower loading and encapsulation efficiency compared to the precipitate for the following reasons:
1. Particle size: Smaller particles tend to have higher surface area to volume ratios, allowing for more efficient encapsulation of the drug. The filtrate contains smaller particles that pass through the filter, resulting in lower encapsulation efficiency.
2. Drug distribution: During the precipitation process, the drug is distributed throughout the polymer matrix. However, some drug may remain in the solvent and be lost in the filtrate, leading to lower overall drug loading.
3. Polymer concentration: The filtrate has a lower polymer concentration compared to the precipitate, as some polymer is retained on the filter. Lower polymer content results in less efficient encapsulation and drug loading.
4. Particle morphology: The precipitation process can produce particles with a core-shell structure, where the drug is concentrated in the core. The filtrate may contain particles with less defined core-shell morphology, leading to lower encapsulation efficiency.
In summary, the filtrate particles have lower loading and encapsulation efficiency due to their smaller size, less efficient drug distribution, lower polymer concentration, and potentially less favorable particle morphology compared to the precipitate.
Based on the information provided, it seems that the loading efficiency of the drug-loaded HPBCD inclusion complex was highest in method 1 (direct mixing and drying), followed by method 2 (mixing, filtering, and lyophilizing), and lowest in method 3 (mixing in a closed container, filtering, and lyophilizing).
Here are the possible reasons for the observed differences in loading efficiency:
1. Direct mixing and drying (method 1):
- The direct mixing of the drug and HPBCD under stirring allows for efficient interaction and complexation between the two components.
- The slow evaporation of the solvent during drying promotes the formation of the inclusion complex, leading to higher drug loading.
- The absence of filtration minimizes the loss of drug-loaded complexes, resulting in the highest loading efficiency among the three methods.
2. Mixing, filtering, and lyophilizing (method 2):
- The filtration step using a 0.45 μm membrane filter may remove some of the drug-loaded complexes, leading to a slight decrease in loading efficiency compared to method 1.
- The lyophilization process helps preserve the drug-loaded complexes, but some loss may occur during filtration.
3. Mixing in a closed container, filtering, and lyophilizing (method 3):
- The mixing in a closed container using an incubator shaker may not provide sufficient interaction between the drug and HPBCD, resulting in less efficient complexation.
- The filtration step using a 0.45 μm membrane filter leads to the loss of some drug-loaded complexes, further reducing the loading efficiency.
- The lyophilization process helps preserve the drug-loaded complexes, but the cumulative effect of less efficient complexation and filtration loss results in the lowest loading efficiency among the three methods.
It is important to note that the specific reasons may depend on the nature of the drug, HPBCD, and the solvent system used. Additionally, the particle size distribution and morphology of the final product may also influence the loading efficiency.
To improve the loading efficiency in methods 2 and 3, you can consider optimizing the mixing conditions, such as increasing the mixing time or using a more efficient mixing technique, to enhance the complexation between the drug and HPBCD. Additionally, exploring alternative filtration methods or using a larger pore size membrane filter may help minimize the loss of drug-loaded complexes during filtration.
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NA
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To wash capsule filters with a Poly Ether Sulfone (PES) membrane and a pore size of 0.2 μm or 0.45 μm, it is generally recommended to use a mild detergent solution. Sodium hydroxide (NaOH) should not be used for washing these filters due to its potential to damage the membrane and affect its performance. Avoid using NaOH or other strong chemicals, as they can degrade the PES membrane and compromise its integrity and performance.
Instead, follow these steps to clean the filters:
1. Mild Detergent Solution: Use a mild detergent solution, such as a 0.1% to 0.5% solution of a non-ionic detergent.
2. Rinse with Water: Thoroughly rinse the filters with deionized or distilled water to remove any remaining detergent.
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I have this problem with my western blot for the ABCG2 antibody on nitrocellulose membrane. Help please
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Echoing others, what am I looking at? I see some sporadic dots on a membrane and one that appears to be completely black. Is this correct? Echoing the first two, the black membrane hasn't been adequately blocked, if at all. You'll want to use a solution of 5% milk in PBS with 0.1% Tween-20. Block AT LEAST 40 minutes. Longer for whole cell lysates and you'll want to just spike your primary into the blocking too. My personal experience is that this does help cut down on nonspecific binding.
As for the membrane that looks like it doesn't have any dots/bands (I think there is a membrane there), this could be caused by multiple things:
1.) Your primary antibody may be bad/old. Not all clones work for WBs. Check the manufacturer's website and make sure the one you're using is validated for WB use. Although the standard dilution for primary is 1:1000, you may need to do a titration to find if you need a higher or lower dilution to get a clean looking WB image.
2.) You did not incubate the membrane in primary long enough. Overnight at 4 C is what I've always done, although sometimes you can get away with RT for 2 hours.
3.) You used the wrong secondary antibody. If for example, if the host for your primary is mouse, make sure the 2nd antibody is anti-mouse.
4.) You may have reacted all the luminol (if you imaged for a while) and there is no more chemiluminescence for the imager to collect.
I hope this helps you! Good luck!
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I am performing in vitro drug release studies using franz diffusion cells. my drug is soluble in the release medium (3mg/mL) and for the duration of my studies. I have used 1 mL of 1 mg/mL of drug in aqueous solution in donor compartment and is also stable in it for the duration of studies. I have tried different membranes, and it doesnot seem to be problem either.. but still the cumulative release at 24 hours is not 100%.. i have also filtered my release media before use.. what could be the issue? I guess, I do not need to use any solubilizers as the release media volume is 12 mL and should be enough to dissolve 100% of drug from donor compartment if released
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The incomplete recovery is likely not due to solubility limitations, but rather a combination of factors like adsorption, incomplete mixing, potential degradation, and partitioning issues. Optimizing the experimental setup and analytical method can help improve the drug recovery. However, 100% recovery is not always achievable, and the focus should be on developing a robust, reproducible in vitro release method.
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Several times by placing a restriction on the upper part of the membrane with the aim of preventing the drug from being added from this side, we tried to keep the drug at the top of the leaf, but the drug was added again from this side. Thank you for your advice.
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It depends on the physicochemical characteristics (e.g., solubility) and size of the bioactive molecule.
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I have prepared curcumin-loaded biopolymer nanoparticles and wanted to know how to check the drug release from the nanoparticles. The literature suggests nylon pouches, dialysis membrane, centrifugal ultrafiltration membrane, etc. Please let me know the best one for my work and the specifications to buy the appropriate one as soon as possible.
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To check drug release from polymer nanoparticles, a dialysis membrane is often used due to its ability to mimic physiological conditions and provide a controlled environment for the diffusion of drugs. Here are some key points:
Ideal Characteristics of Dialysis Membrane:
  • Molecular Weight Cut-Off (MWCO): Select an appropriate MWCO based on the size of the drug to ensure it can pass through while retaining the nanoparticles.
  • Biocompatibility: Ensure the membrane material does not interact with the drug or nanoparticles.
  • Chemical Stability: The membrane should be stable in the release medium.
Commonly Used Materials:
  • Cellulose Acetate: Widely used due to its biocompatibility and availability in various MWCOs.
  • Polyethersulfone (PES): Known for its mechanical strength and chemical resistance.
  • Regenerated Cellulose: Offers high purity and minimal nonspecific binding.
Protocol Overview:
  1. Preparation: Load the nanoparticle-drug solution into the dialysis bag or cassette.
  2. Immersion: Place the bag in a release medium (e.g., phosphate-buffered saline) and maintain under controlled conditions (e.g., temperature, agitation).
  3. Sampling: At predetermined intervals, sample the medium outside the dialysis bag to measure drug concentration using appropriate analytical techniques (e.g., HPLC, UV-Vis spectroscopy).
By choosing the right membrane and carefully designing the release study, you can effectively evaluate the release profile of drugs from polymer nanoparticles.
4o
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I am trying to insert cholesterol inside the DPPC membrane by using gmx insert_molecules -replace. But number of DPPC molecules replaced is much higher than the number of cholesterol inserted? Please suggest me a way to build the system by replacing desired number of DPPC.
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You can play around with gmx insert-molecules flags for example by scaling (-scale) the vdw radii for insertion or having larger number or tries (-try). Take a look at the manual page (https://manual.gromacs.org/current/onlinehelp/gmx-insert-molecules.html).
My feeling however is that you wont get rid of the problem. You are trying to insert a bulky molecule such as cholesterol in a equilibrated DPPC membrane. This means that, even if the average area per lipid for a DPPC molecule may not be very far from that of a mixed chol/DPPC membrane, every DPPC lipid molecule alone is going to be disordered and you will have to remove more than one for having enough volume to put a cholesterol molecule, especially if you are in a liquid-like regime (temperature). And then you will have to re-equilibrate the system. Also, can you respect the symmetry of the bilayer, that is, insert the cholesterol molecules with the polar head group at the right depth? You will also have to try to substitute roughly the same number of lipid molecules per side as otherwise you will lose the leaflets symmetry.
Why do you want to substitute the molecules? My advice would be to start with a new membrane simulation where your content of cholesterol is already correct.
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Hello, I've just attempted a wet transfer of a western, and had set up the cassette and tank, and run @ 100V and set it to 90 mins. I had pre-chilled the transfer buffer - but didn't put the chamber in an ice bucket/add ice-packs (this is my first time attempting a wet transfer, I'm used to using semi-dry). When I walked in after 30 mins, the tank was genuinely steaming and boiling to touch. I switched it off and took out the gel/membrane, and am now blocking the membrane in some vain hope that there's something on it (but doubt it with the overheating and the fact it was only transferring for 30 mins). Has anyone had any experience of this - and it worked? And is there anything else you'd suggest other than setting the chamber up in an ice bucket?
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you need to bring the temperature down as the wattage used in wet transfer generates a lot of heat. place the rig and power pack in a cold room or refrigerator and put a top a stir plate to circulate the buffer.
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Hi, I am preparing a porous Carboxymethyl cellulose membrane by adding DMF as non solvant. After addition of DMF into CMC, I stirred it at 70 degree for 4 hours and then put into glass petri dish to dry in a oven at 80 degrees. When all the water evaporates, then it starts to break. I cannot get a membrane. Also membrane is very fragile, it breaks just by touching it. Can you please let me know how I can resolve this issue?
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Can I use inert atmosphere for drying?
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I am working on an acetyltransferase that is highly unstable. Its pI is 6.65, and its molecular weight is around 18 kDa. The protein elutes at 1M imidazole and begins to precipitate immediately after elution. After testing various pH levels and salt concentrations, I have been able to stabilize it in MES buffer at pH 5.5 with 1M salt and 5% glycerol, by immediately diluting it after collection. The highest concentration I achieved was approximately 6.67 mg/mL, which was only possible by adding 50 mM EDTA post-elution. This addition seemed to stabilize the protein, but I am uncertain if this approach is optimal, and replicating the results has been challenging.
However, when I try to concentrate it using a concentrator, its concentration rapidly decreases after buffer exchange. I have tested the flow-through, and the protein is not present there. I have also tried flushing the concentrator membrane with buffer, but there is no protein stuck to the membrane either. Only a negligible amount is precipitated. I am unable to determine what is happening to the protein. My eventual goal is to crystallize the protein.
Thank you.
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Have you tried including a substrate during and after the purification to help with stability? Keeping the protein concentration as low as practical should help reduce precipitation. For crystallization, it may not be necessary to have the concentration very high, since the protein seems to be prone to self-associate.
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Hello everyone!
I am working on PVDF-based membranes for dye rejection and have encountered a recurring problem: after each rejection cycle, the membrane flux increases rather than decreases, although the membrane's separation efficiency decreased from 99.8% to 91% up to the 14th cycle. What could be causing this, and how can it be addressed?
I am looking forward to help from experts in the relevant field regarding this problem!
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Repeated cycles can lead to cracks or enlarged pores which decrease rejection and increases flux. adding some plasticizers or blending could help
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I am working with snake venom, specifically targeting toxins around the 15 kDa range. I need to remove higher molecular weight toxins (above 20 kDa). Would it be advisable to use a 20 kDa MWCO membrane to separate proteins above 20 kDa and then use a 10 kDa MWCO filter to concentrate the lower molecular weight toxins around 15 kDa which is of my interest?
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Dear Kishore Srinivasan, I think in your situation the use of dialysis bags is a tedious task. You have to read about fractionation of proteins techniques. At the momoent I suggest to play on their differential solubility and precipitation at the isoelectric point, by pH adjustment. My Regards
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Hi all,
Can I please ask, how can I calculate the pure water flux without knowing the surface area? I am using the NF membrane and I have the cross-sectional area but don't know the surface area.
I want to know the effect of TMP on the permeate flux.
Thanks
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How will you do that if you don't know the membrane cutting factor = porosity? Doing your own calibration (with different markers/proteins) will take a lot of time
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Hi,
I have a question regarding western blot. I performed total protein statin after trasfering membrane. The result was totally fine before (Figure 1). However, there were strange bubble-like spots over the membrane every time since last month (Figure 2). I have tried more than 10 times and switched the gel, PVDF membrane, buffers and the results were the same. I transferred the membrane under 200mA for 3 hours. Every one in our lab use the same transfer condition and share the tank for transfer. Their results were totally normal. I was wondering what is the problem?
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Hi Chien-SWei,
difficult problem. I first thought about air bubbles, but I don't think you did everything correct. Then I thought about a high content of membran proteins and lipoproteins. Especially multi-spanning membrane protein can fragment and precipitate when heated in Laemmli buffer at 95°C. Or that a high amount of lipoprotein precipitate during the running.
I would suggest not to heat the sample (and use a relativly low protein concentration) in the Laemmli sample buffer, just a 10 min incubation at ambient temperature.
But that is a difficult problem, I have never seen such a effect in a gel.
Best,
Carsten
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Is PAMPA an effective option? what membranes can be used to evaluate the same? are there options available in cell culture using SHSY5Y cell lines?
Any comments are appreciated!
Thank you.
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Unfortunately, none of the cultured human brain EC models are tight enough to simulate in vivo flux of a small molecule. Use the permeability coefficient from one of the standard cell (MDCK, Caco-2) monolayer models. It is also important to determine whether the compound is a P-glycoprotein substrate and how bound the compound is in plasma. Ideally, measuring a 'calculated free' brain conc. after oral dosing is the best guesstimate.
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i was preparing gelmA by already reported method. but im unabke to seperate side product methacrylic acid and unreacted methacrylic anhydride. we donot have dialysing membrane facility nor we have lyophilization technique. kindly tell there alternatives
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I have 2 proteins-one is 19KD and other is 5KD. I tried detecting both of them through western blot using 20% SDS gel. I transferred them into 0.45 PDVF membrane for 100mins, I could detect the 19KD protein but I couldn't get the 5KD protein.
Any suggestions will be appreciated.
Thanks in advance
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Thanks, I will try following this method
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Hi all!
I would like to know if there is a method to polymerize low MW cellulose triacetate (e.g. re-engaging in acetylation). Or this is not possible and the MW of my cellulose source should be high?
Thanks.
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Dear Polo Jerome Daquipil, please check the following publication and the references theirin. It seems very possible to conduct acetylation further. My Regards
10.3390/molecules27041434
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I am having an issue with the western blot transfer from last week, I see imprints of cassette on my membrane.
I am making a 14% gel and I run transfer for 2hr at 100V, after the transfer I see imprints of cassettes on the membrane.
I thought it could be because of the cassette was too tight or because of the temperature. So I keep in check for the cassette and temperature (1hr 45min) and repeated the western I see the same problem.
I used fresh buffers both the times.
Any suggestions how can I improve?
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Hello Thamizhiniyan, I used more blotting paper. I used 3 paper up and 3 down to make a western blot sandwich and also I kept cold ice packs in the transfer tank during the transfer process. I hope it helps.
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Problem 1: In my research, I encountered an issue with my wet transblot procedure: despite using 8-10ug of RNA sample and applying a voltage of 10 v for 2 hours in TBE transfer buffer, I observed incomplete transfer of the top band from the UREA gel (8M) to the nylon membrane upon examination.
Problem 2: for northern blot, I conducted prehybridization at temperatures ranging from 55°C, 60 °C, and 65°C, followed by membrane washing with SSC buffer and blocking with blocking solution. Subsequently, I proceeded wash the membrane in wash buffer and soak in detection buffer and applied CDP-Star on top of the membrane. The entire membrane exhibited fluorescence (is it normal?), later the resulting X-ray film exposure did not reveal the desired bands. Background noise quite bad. I would appreciate any professional guidance or suggestions to address this discrepancy."
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problem in northern blotting is often sample degradation by RNases (both endogenous to the sample and through environmental contamination), which can be avoided by proper sterilization of glassware and the use of RNase inhibitors such as DEPC (diethylpyrocarbonate)
Northern blots are used to detect the presence of specific mRNA molecules. To do a northern blot, RNA is loaded into the wells of a gel, and separated according to size by electrophoresis. The RNA is then transferred to a membrane filter in a process called blotting.
Northern Blots: 0.05 fmol detection limit with near-IR RNA Probes.
To disrupt the secondary structure of RNA, either formaldehyde or glyoxal/DMSO (dimethyl sulfoxide) is commonly used as a denaturing reagent. Formaldehyde is simply added to the samples and gels, so that the method using formaldehyde is easier to run the gels than that using glyoxal/DMSO.
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I would like to run an invitro drug release experiment for chitosan nanoparticles (600nm) loaded with herbal extract using dialysis membrane method. However since its not easy to ascertain the molecular weight of the herbal extract because its mixture of different compounds. therefore I am not sure which is the best MWCO for dialysis membrane that I can use. I used 5Kda but nothing went through in 24hrs.
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oh, thanks so much. I have used 14kda let me see how the results come out.
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NF membranes sit between Reverse Osmosis (RO) and Ultrafiltration (UF) in terms of pore size. This allows them to remove a wider range of contaminants than UF but not as much as RO. However, current NF membranes aren't perfect at selectively removing certain contaminants while allowing desirable minerals to pass through. In optimizing NF membrane selectivity, could machine learning algorithms be used to design or predict ideal pore structures or surface functionalities for NF membranes?
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@ Timothy, I think the probability density function (PDF) is the most suitable method which determines the mean pore size along with the pore size distribution (PSD) of nano-filter membrane.
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For treatment of water (river), what is the life of ceramic membrane? For example, 5 years or 50 years? MF or UF?
Operation of ceramic membrane after usage: should be kept under water like polymeric membranes?
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Hey, the question is not clear: which membrane, what type, thickness, porosity, how much pressure is applied to it... etc.
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Aslamo alikom/ Greetings everyone,
I'm conducting a western blot experiment (8% SDS gel) and I wanna test 2 proteins, one is 95 KDa, and another is 35KDa. The antibodies I've for both are mouse Abs used at 1:1000 dilution and I use secondary HRP-conjugated at 1:2000 dilutions.
Ideally, I use to test them sequentially, but I'm wondering if it's possible to add the 2 antibodies to the incubation buffer (BSA/milk) and test for both in one go?
I would highly appreciate an answer for this. Also, if someone has done it before, I would appreciate the feedback/tips if any.
Thank you
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Dear Mariam,
It is advisable not to mix two primary antibodies even if they have requirement for same secondary antibody. Cutting the blot based on the molecular weight is one approach and the second one is to follow sequential incubation.
Good luck with your blots.
Best,
Sheethal Galande
PhD Fellow
AHF
AIG Hospitals
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Method of fixing exosomes on a slide, assuming that the membrane is negatively charged, the positive slide attracts exosomes
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Exosomes are mostly negatively charged. Like all materials, exosomes spontaneously acquire surface electrical charge when brought into contact with a polar medium, such as a hydrophilic buffer. Therefore, the exosome surface will generally be negatively charged in such buffers.
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I want to study CO2 capture simulation on activated carbin filters in a duct how can I find the amount of CO2 adsorb by membrane?
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Quantifying the quantity of CO2 adsorbed by the membrane requires multiple processes, which are important to examine CO2 capture simulation on activated carbon filters in a duct. First, employing activated carbon filters, an experimental setup or simulation model must be created to mimic the CO2 capture conditions inside the duct. To ascertain the activated carbon's relevant characteristics for CO2 adsorption, such as surface area, pore size distribution, and functional groups, characterization is essential. The relationship between the concentration of CO2 in the gas phase and the amount adsorbed by the filters is then determined via adsorption isotherm tests or simulations.
The amount of CO2 adsorbed is then determined by mass balance calculations that take into account the gas flow rate, adsorption capacity, and concentrations at the input and output. In addition, CO2 adsorption behavior under various operating conditions can be predicted using mathematical models or computational simulations; the quality of these predictions is ensured by confirmation against experimental data. This scientific methodology allows for the development of CO2 capture applications for increased efficiency by providing data on the CO2 capture performance of activated carbon filters in ducts.
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I'm not sure how to interpret or fix the sample so that it creates a normal band. I used Percoll Gradient with density gradients to generate the questionable band. It's supposed to represent basolateral membrane fraction, and most people mentioned that the sample preparation is not good enough, but I'm not sure how I can make it "good enough".
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Here are some concise tips to improve the quality of bands in your Percoll gradient:
1. Optimize Percoll Concentration: Experiment with different concentrations to find the optimal gradient for separating the basolateral membrane fraction.
2.Sample Preparation: Use effective techniques like homogenization or sonication to isolate the membranes efficiently.
3.Starting Material Quality: Ensure high-quality cells or tissue free from contamination.
4.Centrifugation Parameters: Adjust speed and duration to optimize separation.
5.Marker Proteins: Include specific markers to confirm the presence and purity of the fraction.
6.Gradient Fractionation: Collect and analyze fractions separately to locate the basolateral membrane fraction.
7.Quality Control: Use assays to confirm membrane protein presence and fraction purity.
8.Consult Literature: Look for optimized protocols and techniques in relevant research papers.
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I prepared a membrane for use as a dielectric material using the electrospinning method. their index is as follows: one shows 0.9 under 9 GHz and another 0.83 under 8.5 GHz but one shows 1.03 and another 1.09 under 10 GHz. After that, doubting the result, I re-examined and the same result is repeated. So can anyone give me any advice on this matter?
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Mr. Kaushik Shandilya, first of all, thank you very much for your advice and for taking the time to reply.
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I am establishing a polarized gastric-epithelial monolayer culture on transwell system for bacterial infection studies. I use NCI-N87 cells and I culture them by replacing medium on every alternative day for 21 days. Later, I confirmed the expression of ZO-1 on 100% methanol (-20C) fixed cells. However, I face the following issues during this process.
1. How to avoid membrane curling while I cut off the membrane from the insert to mount on glass slide?
2. When I used 4% formaldehyde as a fixative to stain cell surface proteins, I found few cells or small cell clusters lying over the tight monolayer.
3. Is it necessary to use 21 days grown cells for bacterial infection studies? Because I see many highly cited papers also have used lesser days grown cells.
How to overcome these technicalities?
Any help is highly appreciated.
Thank you in advance.
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Thank you Sasikala!!