Science topic

Milk - Science topic

Milk is the white liquid secreted by the mammary glands. It contains proteins, sugar, lipids, vitamins, and minerals.
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Milk and beef given the status quo clearly violate the 1.5 degrees Celsius limit - even in the near term.
As consumption patterns and cultural identifiers among middle class may be too sticky, how can the industry be demethanized?
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Changes in the diet of humans as well as cattle feed. Plus, converting animal and dairy wastes into bioenergy.
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define parameters of high milk yield and the nutritional requirements to achieve the high milk yield.
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This question has not a single answer.
Milk yield depends not only on nutritional regime but also on genetic merit, environmental conditions, body condition at the beginning of the lactation, etc. NRC and INRA give comprehensive methods to estimate requirements of dairy cows. The rationing would also depend on the ingredients (forages and concentrates) available for you.
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Lactoferrin is a natural antimicrobial in raw milk. I'm going to use this substance as food preservation.
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Surely, HPLC is better and more accurately
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Dear researchers,
We did the Gerber fat test for milk and sausage, after reacting with acid, the material turns brown and dark purple. What is the exact cause of this color change?
90% sulfuric acid is used for milk and Salvin reagent is used for sausage.
Is it because of antioxidants and nitrite or are proteins involved? Or is it a combination of these things?
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Dear Helia
In the Gerber test H2SO4 is used to increase specific gravity of milk serum which makes greater difference between milk serum and fat globules. It also destroys stickiness of milk by dissolving chemical bonds (hydrogen bounds first).
Adding sulfuric acid will denature the casein. As a result, the casein molecules are likely to stick to each other and form a centrifugable pellet that goes to t,he bottom of a centrifuge tube after spinning.
Sulfuric acid is very reactive and dissolves most metals, it is a concentrated acid that oxidizes, dehydrates, or sulfonates most organic compounds, often causes charring.
You can try out this one (think of personal safety and protection): take a lump of sugar and put 2-3 drops of 91% sulfuric acid and watch. The sulfuric acid is extracting all the water and leaving a black, charred residu.
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I'm trying to develop a milk fat quantitation method by spiking fats/fatty acids in skimmed cow milk to around 1.5% fat (w/w). Curious if anyone has experience in this regard. If you have ever used this approach and managed to dissolve fats/fatty acids in milk, what kind of additional sample prep have you used?
I am looking forward to hearing your suggestions.
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Milk is an oil-in water emulsion and thus, consists of both water and fatty acids (short-chained fatty acids, unsaturated, saturated, polyunsaturated etc.) The lipids are uniformly dispersed throughout the milk. Here, milk proteins (such as casein and whey) act as emulsifying agents that contributes to homogenize the lipid droplets in the milk.
One alternative to measure the milk fat content is to utilize the UV-spectrometry since milk fats are able to absorb UV-light, if I have understood your question correctly. You can read more about this by searching for milk fat content measurement using UV.
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I would like to know the software options for water footprint calculations. What are the advantages and disadvantages of each software?
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Hi Luis. I don’t know any good programs but beware of calculating a water footprint for milk, or any other animal product for that matter. For all of the examples I’ve seen the largest majority of water is used in the growing of the feed for the animals.
If you are in California or Mediterranean Europe then the source and cost of irrigation is a strong consideration. If you are in North East USA or Northern Europe, the water needed falls as rain so it is of less consequence.
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Dear friends;
What is the titratable acidity of plasma in butter?
How can I measure?
Thanks in advance.
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First you should determine fat content in butter. The rest is butter plasma. Example: fat content is 80% (butter plasma is 20%) and total acidity is 0.05%. The acidity of butter plasma is 100*0.05/20 = 0.25%
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I am trying to making eggless mayonnaise using skim milk powder with 40% oil. But I am facing separation problem of mayonnaise. What are the method to test the emulsion stability?
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You can use zeta potential and Particle size distribution or rheometer ( rheology methods). Also, you can use the oil off method.
What about the homogenization of the skim milk at the first step?
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camel milk
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Food categories means = fruit, vegetables, meat, fish, milk and milk products
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You might also look at the illustrated calculation in the Handbook of Food Engineering Practice
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Outcome depends on the type of food it takes right ? So if a cow consumes Genetically modified grass rather than normal will the quality of milk increase? And can we observe any changes in the behaviour ?
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One of the elements influencing the sensory qualities of milk and meat products is the kind of forages consumed by ruminants. The impact of the type of forages (corn silage, grass-based forages), the conservation strategy (hay versus silage), and the botanical composition of the grass on the sensory qualities of cheeses (colour, texture, flavour) are discussed for dairy products. There is no scientific evidence that genetically modified feed has an effect on milk output or composition. It is crucial to remember that cows consuming GM food do not modify an animal's (or a person's) DNA. Cow's milk has no GMOs. A contrast may be made to diabetics who use insulin; the individual does not become GMO. A dairy contrast is that a cow given chocolate does not produce the milk that comes from that animal.
Sravya Jasthi Hope this answer is relevant to your query.
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I have seen that many children with this habbit didnot get caries only those got whose mothers mixed sugar in it..and many have caries without use of feeding bottles...
so whats the main cause ??
-dissolved sugar
-plain milk
-feeding bottle
-poor nutrition
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Baby Bottle Tooth Decay can occur when babies are put to bed with a bottle, when a bottle is used as a pacifier, or if a baby uses a bottle or sippy cup for extended periods of time.
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Hi all,
We are working on nanozymes using TMB substrate. The oxidized TMB turned an unexpected green color when the presence of melamine in milk was analyzed. Does anyone have any ideas for this observation?
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Green color is perhaps due to the presence of both semi-oxidized (blue) and completely oxidized (yellow) form of TMB. We observed green color when oxidized TMB by nanozymes in a buffer with ph lower than 4.
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So, the problem happening here is when I am doing blots to check GFP in my cell lysates, bands are occuring at higher molecular weight then the actual GFP protein has i.e bands are developing above 55KDa but the mol weight of GFP is around 25KDa. This is the case when I am using 5% milk buffer in TBST for blocking.
But when I used 3% BSA in 1XPBS for blocking bands developed at 2 sites- one is around 25KDa and other is above it around 35/40KDa. But the blots are not looking clear when I am using BSA.
Anyone can tell why is this happening?
Is there protein interaction happens when you use GFP with milk buffer?
And how can I troubleshoot this issue?
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Hi,
you mean you have two bands within one sample when using BSA? One at around 25kDa and one at 35/40kDa? Or in different samples?
In my experience BSA leads to more unspecific binding than blocking with milk.
In case it is within one sample then I would trust the BSA more with the band around 25 kDa and the one above is possibly a non-specific signal. Do a proper control without GFP transfection and maybe also try blotting with secondary antibody only without primary antibody detecting GFP, because secondary antibodies can lead to unspecific signals as well.
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I need the new data of Food Standards Australia New Zealand (FSANZ)/ Joint FAO/WHO Expert Committee on Food Additives (JECFA) or other regulations.Thanks.
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Also, kindly check the following link that may be useful:
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If the cow is bitten by rabid dog is it safe to consume its milk (If there are any specific literature available kindly share).
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Not safe if the dog is infected with zoonotic diseases like PPR
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I want to detect HO-1 proteins in TIG cell lines and this cell line is a new cell line that I work on. I want to know your ideas on my WB protocol to detect HO-1 by western blotting because my results are not consistent and also on top of that my bands have tailing effect even after so many trials.
1. Lysis buffer – I use RIPA lysis buffer with PMSF at the final concentration of 1mM. I use only PMSF as a protease inhibitor. But I wonder if I have to add a phosphatase inhibitor.
Following is how I prepare my cell lysates.
Cells in 6 well plates, CM removed and wash x3 with PBS
Centrifuge 2600 rpm/ 7 minutes/ 4C
RIPA lysis buffer 60 µl added to each pellet and suspended x20 times
On ICE for 30 minutes
Centrifuge at 14000 rpm for 20 minutes
Sup collected and protein concentration measurement with BCA protein Assay.
Add x4 SDS sample buffer at 1:1 ratio and boil 100C for 5 minutes
2. Gel electrophoresis – I use 10% gels and plan to load the samples 30/20/20/5/3 µg per lane. In my previous experiments I understand that I have to load at least 30 µg/lane to detect positive bands even after stimulation of HO-1 with ALA/SFC. Do you have any suggestion on the minimum protein amount per lane to load to detect HO-1? I use Ab82585 anti rabbit first Ab at x1000 dilution O/N, followed by second Ab incubation x2000 for 1 hr.
3. Quality of the bands- My bands always have tailing effect and do not come as sharp bands. I tried electrophoresis 50 V for 30 mins followed by 150V for 1 hr and then changed to 50 V 30 mins followed by 120 V for 120 minutes on crushed ice bath. But the effect is still there. Do you have suggestions to improve it?
4. I want to know your suggestion on WB procedure that I use.
Blocking- 3% skim milk for 1 hr
Washing- 0.1% PBST x5 times
First Ab- Dilution in 3 % skim milk
Second Ab – Dilution in 3 % skim milk
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your protocol looks fine to me but I would advice you to check your buffers even though tailing effect of your bands might be probably for the dye you are using or the protease inhibitor
it would be helpful if you show some pictures.. how is your ladder separating in the gel? is it fine and well separated?
what is your housekeeping antibody, do you have a picture for that?
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Hi all,
I recently developed a nitrocellulose membrane using the Li-cor western blot system. However, I wanted to strip it and probe it again for the ECL system to see if there was a difference in band quality. I was planning on stripping the Li-cor system membrane, blocking with milk, followed by re-probing for ECL. Has anyone tried this before? I have seen comments that have used ECL membranes for Li-cor, but not many discussing the opposite.
Thank you!
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In my experience (and others I know as well), membranes probed with the NIR LiCor secondary antibodies do not strip well at all, especially at if any point in your process the membrane dried. LiCor sells a stripping buffer that is supposed to work for their antibodies, but I have never tried it myself.
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Why do we use non-fat or skim milk in blocking during ELISA and WESTERN BLOT, why it is only normal milk? what is the science behind "non-fat"?
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The fat globules are known to block measurements in milk because they have a large volume in the liquid and sometimes cover other elements of the milk.
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I have a concern regarding the transfer of monosodium glutamate via milk through breastfeeding. The only research paper I can find regarding this topic is from the 1970’s and by Stegink, and I’m wondering if there has been any further research to confirm their data? Their overall conclusion was that MSG is not passed into breastmilk in significant levels. I have a hard time trusting data that has not been replicated in more recent studies by other researchers, but perhaps I’m just having difficulty finding data to confirm the results.
I appreciate thoughtful input. Thank you ahead of time for your expertise.
Sincerely,
A concerned mother
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My immediate thought was whether MSG has been shown to be a substrate for BCRP (Breast Cancer Resistance Protein) that is known to excrete drugs into breast milk. I've not looked at the literature to bolster or refute this possibility.
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for western blot analysis
the buffer in which the antibody already is, written in the datasheet, or should I use already the bsa or milk solution that I use for final diluition?
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As a postdoc back in the late 1980's and early 90's, the lab protocol was to dilute the commercial antibodies in 1X PBS at a 1:10 dilution and store them at -80 or -20 in 20 ul aliquots. The antibodies lasted mostly for years. Its a practice that I have kept using. I just got a new shipment and I am open to change.
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hi,
im doing CHD4/Mi-2ß Western Blots. First lane is WT, second lane monoallelic knockout.
As you see, the second lane has one band at around 260kDa which should be CHD4.
First lane has one big band at the top. What could that be? Any suggestions?
There is some smearing in lane 1 too.
Ive loaded 60ug protein per lane, 7,5ul 5x laemmli buffer, 10min at 75°C.
Blocking with 5% milk in TBST for 2,5h, primary AB over night, secondary AB for 1h at RT.
The lysates were made in the absolute same way.
Any suggestions?
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60ug is a lot of protein. I have the same question about reducing agent. I would reduce the amount of protein you load as that is likely contributing to the smearing you see. Does CDH4 have a lot of post translational modifications? That could retard the migration on an SDS-PAGE.
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Dear Colleagues,
I need a protocol to analyze cortisol in the milk (animals or humans) using HPLC.
Could somebody help me out?
Thank you
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Dear Marc,
Thank you for your kind reply. We would like to set up the HPLC method for analyzing milk cortisol but seems that HPLC-FLD is required (we don't have it). Also, we don't have LC-MS equipment at the moment. However, I appreciate it if we can communicate via email to further discuss this. Would you please provide your email address or send me an email to: jalilgh@konkuk.ac.kr either more convenient for you.
Thank you
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Milk fermentation increased my samples' L* and whiteness index (WI) values.
I want to write a discussion sentence about it. I have found some papers which give the whiteness values of milk and fermented milk, but I couldn't see any technical description.
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I didn't explore exopolysaccharides' possible effect on whiteness in the literature. Thank you for your interpretive answer. I will search and think about this perspective.
Thanks and Best Regards,
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We keep our membranes in cold 1X TBS buffer, and block with nonfat milk. However, the milk curdled during the blocking process, and when we went to image it, there was no result, including the ladder. Is there a way to prevent the curdling of the milk when blocking?
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Hi Samvit
We use non-fat milk to block our membranes but do so in TBST (TBS + 0.1% tewwn-20). The detergent helps to keep the milk suspension stable and can help to avoid it from precipitating out (forming lumps that stick to membrane).
We block for 1h at RT. Moving between 4C and RT often or not allowing buffers to calibrate to ambient temperatures can also accelerate precipitation.
Hope this helps
Aparajita
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Hi everyone,
I wanna know if there is a robust method of measuring the iodine content in the cow milk. For plant samples usually the lab I been working uses Tetramethyl amonium hydroxide (TMAH) to extract iodine from plant samples and measurement is done by ICP-MS (Inductively Coupled Plasma – Mass Spectrometer). But we want to know how we can do it with milk.
Thanks.
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These publications also probably refer to analytics
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Can I use casein instead of skim milk powder for blocking Western blotting?
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The role of the blocking buffer is to saturate the remaining sites on the polystyrene wells (ELISA) or nitrocellulose membranes (WB). It is used in a variable percentage from 1 to 5% of a some protein such as BSA, ovalbumin, casein, or powdered milk, or for example fetal calf serum that you are not going to use in cell cultures. It exists also commercial blocking buffers from several providers. For each type of immunoassay, the ideal blocking agent should be found, as well as in what % to use it. I hope it works for you
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One of my yeast isolate got from fermented milk was identified as Candida kefyr using API CAUX20 biomeriuex kit. I have send the sample for molecular identification and they are telling the sample matches Fusarium (ITS 1 and ITS4 primers used). But I am getting good quality fermented milk from this isolate. Can it be possible?
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API certainly has limitations, but you report a major disconnect. Appears the molecular ID may have been on a contaminant. Suggest you ensure pure culture and resubmit.
fyi - the The perfect form of C. kyfir is Kluyveromyces marxianus
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I want to know about the limits and value of white side test for mastitis detection such as leukocytes/ml for 1+/2+/3+/4+ reaction.
any suggestion for rapid counting methods of epithelial cells in milk at farm level?
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CMT is rapid test for detection subclinical cases of mastitis depending on cellular protein(WBC) which detected by using Alkely_Arylsulphonate.
For limits and values depends on degree of mastitis e.g Subclincal,clinical ,chronic ,so degree evaluations according to number of inflamatory cells and kind of aetiology
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Exopolysaccharide Production
Qualitative screening of test cultures Lact. plantarum BBC32A, BBC32B, BBC33, and BIF43 to produce exopolysaccharides (EPS) was determined by streaking actively growing cells and cultured in MRS broth at 37 °C for 16 h, onto modified Ruthenium red milk agar [20] and MRS-lac agar [25], respectively. Ruthenium red milk agar was prepared by adding 0.08 g/L ruthenium red, 1.0 g/L yeast extract, and 1.0 g/L sucrose 100 ml pre-boiled skim milk (10%, w/v, milk powder in distilled water, boiled at 100 °C for 10 min). MRSlac agar was prepared by replacing glucose with lactose (2%, w/v). Plates were incubated at 37 °C for 24–36 h. Strains that produced EPS formed white ropy colonies on ruthenium red milk agar, whereas non-EPSproducing colonies were pink. Ropiness was further confirmed multiple times by the formation of a sticky filament when colonies were touched with a loop ., thanks
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I am not exactly sure what is happening here. However, unlike many stains, which can be stored for prolonged time periods (in amber viles), Ruthenium Red will only stay good, once mixed, for a couple of days in amber viles. Your problem “may“ be due to stain that is not made fresh.
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Want to know about the effect of sodium azide and sodium benzoate on the functional properties (antioxidant and total phenol content)during storage of walnut milk.
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Wazir ali Hangu, I wonder about the purposefulness of such research with the use of sodium azide and sodium benzoate. After all, when storing food products, such compounds must not be used. However, if you insist on such study, preliminary tests (with different concentrations) will be necessary to determine the effects of these compounds on the components of the walnut milk, here antioxidants.
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milk, baby formula has an expiration date beyond which it is unfit for human consumption. Manufacturers, who must discard millions of pounds of outdated formula annually
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Yes, harnessing that as an ingredient in formulation of animal fed is possible. You only have to follow the principles of feed formulation including purpose, nutrient requirement of animal, inclusion rates, among others. Very importantly you need to ensure the quality and safety of the that ingredient before its use.
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Hi, am new to metabolomics, can i use GC-MS to characterize volatile of milk? or there is a better methodology.
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Heritability for milk yield <0.10
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In the case of high inbreeding, which results in a genetic similarity of the clan to a large degree, in this case the difference resulting from the environment, as the quantitative traits are affected by both genetic and environmental factors
To avoid this, out-breeding of the herd must be brought about through mating (crossbreeding)
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Hello, after following all of the instructions for gel preparation and getting the apparatus up and running, Unfortunately I am facing the following issue.
I have an antibody (MW: 17-22 KDa) that I'd want to test across several cancer cell lines. The image below shows the expression across several cell lines. The arrow highlights the distinct protein bands. The protein bands are not. separated to each other. the bands for B actin from the same gel are well separated.
1. I prepared two types of lower gel (12% and 15%), and loaded 6ul protein samples.
2. The protein was transferred using a PVDF membrane (Time: 90 minutes; I: 300).
3. To block the membrane, use 5% skimmed milk.
4. The antibody dilution is made with 5% milk. The membrane is incubated at 4 C overnight. then for two hours at room temperature with the secondary antibody.
(Note: The same process is repeated when the primary antibody dilution is made in 3% BSA and the membrane is blocked in 3% BSA.)
Your valuable suggestions are requested.
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From the attached image and your content, it seems that issue could be related to either with the sample preparation or the sample buffer itself. The beta actin control indicates that the protein has not been equated in your sample as the beta actin bands are of varied intensity. So protein equation is also concern with the image.
Recheck whether you have used appropriate enzyme (proteinases) inhibitors in your sample buffer and the samples are prepared as per the established protocol.
Best
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Thanks in advance to anyone who will answer. I am trying to precipitate caseins in raw skim milk without using isoelectric precipitation. My goal is in fact to obtain caseins in their native structures. I have already tried centrifugation at 30000 x g for 1 h and it seems to work pretty well. However, the centrifuged pellet seems to be in e gel-like form, so I'm afraid the present proteins are highly denatured. Do you have any suggestion?
Thanks again.
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The usual first step is to centrifuge the milk to remove the fat and precipitate the casein micelles with low pH or precipitating agents. ... If the majority of the product protein associates with either the fat or micelles, this can be used to advantage. https://pubmed.ncbi.nlm.nih.gov/1429861/
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Hi everyone,
I am trying to detect mono-ubiquitilated proteins in a whole cell lysate and I expected to see a smear on the western blot or maybe a band for free ubiquitin. But instead I see no signal at all.
I am thinking, maybe the ubiquitin in the milk I'm using for blocking and dissolving the antibody could be the problem. Does anyone have experience with this and suggestions around? Maybe a BSA-based blocking recipe and recipe for making up the antibody stock?
Thanks!
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Yes, that worked for me
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I would like to do the fractionation of a medicated milk to do the activity study.
Milk will act like a solvent in the preparation of this medicine.
But because of the milk content I am facing some problems in the selection of fractionation method. so please provide suggestions...
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Fat corrected milk (FCM) Kg contains 0.4 (kg milk)+15 (kg fat)
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Dear all,
We are trying to quantify different proteins in 6 dpf zebrafish larvae. After exposure we collect the larvae in PBS which is then replaced by RIPA buffer containing PMSF and a cocktail of inhibitors. Following homogeneization and centrifugation, we quantify protein by BCA method and apply 50 ug in a 4/12% SDS gel. After running the gel and performing the transfer, we proceed with the common blocking (5% milk), primary antibody incubation (in 5% BSA) overnight at 4 ºC, secondary antibody incubation (in 5% milk) and proceed with the detection using a chromogenic substrate. Yet, and after deeply optimize every step in the western blot procedure, we are still not getting protein signals except for the GAPDH antibody.
We have tried this same procedure with adult zebrafish brain and we get bands for some of the antibodies that we're testing but the larvae do not show any band (an example can be found attached).
Does anybody have a possible explanation for not getting any signal from larval samples? Is this possibly related to antibodies specificity for each organ?
Thanks in advance
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Dear @Elisabeth E LeClair
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By which chemical does milk need to be stored for RNA extraction except for RNAlater?
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thank you for answers. TRIzol is an expensive chemical so I'm looking for a cheaper chemical.
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How much impact does it have on milk and meat production?
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mastitis & foot & mouth diseases well as Rift valley fever are common now due to winter season
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I am looking for ways to activate DREADDs in pups and was wondering if anyone could share experience/thoughts on whether CNO can be transmitted through maternal milk ? Thanks!
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Hi Rajae, I'm not aware of any publications specifically looking at transmission of CNO through maternal milk. But there is recent paper regarding administration of CNO to 8-10 week old mice pups that might be of use:
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I am studying the histology of mammary glands of lactating Wistar rats. I need to differentiate glands with higher milk secretion from the glands with lesser or no milk secretion. What are the fundamental differences in gland's histology in this case?
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لا اعلم يمكن مراجعة المختصين
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Using supermarket skim milk
in screening of protease
and SDS PAGE
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5% skimmed milk for a membrane blocking during western blot
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Want to know about the hazards free chemicals preservatives for walnut milk preparation. Kindly recommend me any articles related to the above mentioned problems
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Dear Wazir ali Hangu as an inorganic chemist I'm absolutely not a specialist in this discipline. However, I just came across the following potentially useful article which might help you in your analysis:
Natural tropical and chemical preservatives effects on shelf-life and hedonic acceptability of tiger- nut milk and soymilk under storage conditions: A review
The good thing about this article is that it is freely available as public full text on RG. Thus you can freely download it as pdf file.
Good luck with your work!
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Hello everyone, I am trying to detect pIRF3 protein in MDA-MB-231 and BT-549 cells, but have been unsuccessful for a while now. I am able to detect other proteins such as pSTAT1 and pSTAT3, but pIRF3 just doesn't seem to work even after stimulation of the cells. Has anyone tried to detect this protein in these cell lines? If so, what are the protocols and antibodies used?
My protocol:
- After transferring proteins onto nitrocellulose membrane, block in 5% milk/ TBST for 45mins
- Incubate with primary antibody in 5% milk/TBST or 5% BSA overnight (Antibody from Cell Sig Tech #4947s, 1:500)
- Incubate with anti-rabbit antibody (1:2000) in 5% milk/TBST for 2h before proceeding with detection using Super signal West Femto
Thank you.
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Hi,
Did you include phosphatase inhibitors in your lysis buffer? In addition, you may enrich the protein by IP and then do western blot. Good luck for your experiments :^)
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During the household survey, we profiled lactating cows;
lactation length,
month and year of the last calving,
average milk production per day, milk production at calving, peak, yesterday and late lactation.
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Joseph -
I noticed in this question thread that among your questions you asked for the "average milk production per day." Would that be for the entire farm/household so that you could obtain a total volume by household farm? If not, if you had that for each cow at the household, you would have that value. If you now wanted to know total milk production for the current population, you might use these data, total previous milk production per household farm, as predictor (independent variable) data, if you have this for every household in the population of interest, and a relatively small current sample of the largest cases, i.e. farm households, plus perhaps a small systematic sample of the rest of the current population, for the response data. Thus you might relatively quickly obtain an estimate (actually a "prediction," not a forecast, since Y is a random variable) of the total milk production for your current population.
I promoted this model-based approach for finding total energy production, for various categories, at the US Energy Information Administration, and realized this could be applied elsewhere, whenever there is a census followed by a sample or samples, say an annual census survey and 12 monthly samples. The systematic sampling part of the sample here would make it possible to check that the regression coefficient estimated here is good enough for the entire population, or to perhaps stratify otherwise (as in the Karmel and Jain reference found in the first paper to follow). I know that systematic sampling is chapter 8 of both the 1st and 3rd editions of Cochran's Sampling Techniques, Wiley, but the estimation here would instead be by a model-based (prediction) method.
So, if the possibility of relatively fast and relatively inexpensive predicted/estimated total milk production would be of interest to you, here is a guide:
Here is a way to estimate sample size needs with a model I think may be appropriate for you:
This presentation may have some practical advice:
and this was an invited presentation for mathematical statisticians at the US Energy Information Administration:   
I have a project on this topic, as follows:
Cheers - Jim
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I performed an indirect ELISA and I used BSA and skimmed milk with different concentration for blocking separately but the result didn‘t change and negative control change color. Also I test different dilution of the antigen, primary antibidy and secondary antibody. But there were no difference between the positive and negative control. I hope some experts can give me a solution.
Looking forward to your reply.
Zahra
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If either the positive or negative control does not produce the expected result, it indicates that the investigator should reconsider his or her experimental procedure. Zahra Rezaei
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commercial ELISA kits for estimation of beta hydroxybutyric acid (BHB) cost approx. Rs.50000/- which is very costly. Is there any alternative method for quantitative determination of BHB in blood/ urine/ milk
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Specimen type: β-hydroxybutyrate levels can be measured in serum. Point-of-care devices that can measure β-hydroxybutyrate levels in a single drop of blood within 30 seconds have been developed Sudhakar Goud Karpurapu
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We used tumor and normal tissue lysate and an equal amount of 30 ug of protein was loaded to each well. The lysate was stored in -80 degree. After mixing the dye it was stored in -20 degree. Also we observed a high non-specific background along with intense multiple bands below 55 kDa. We blocked the membrane with 5% Skimmed milk in TBST and also 5% BSA in TBST the next time. The background issue is still not solved. Other proteins show crisp bands with very light background. Should we change another loading control?
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Was it native WB or denatured WB? If it was denatured one how did you prepare you sample?
-20 isn't ideal for sample storage, -80 is (for fresh frozen sample). If you are doing a denatured WB and when you say "mix the dye" means "mix the lysate with sample buffer and cook for denaturation", then you can keep the denatured sample in 4 celsius fig for a couple of weeks for no problem.
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Fouling is one of the major problems in milk heating. What will be the probability of fouling of milk in a magnetic induction-based heating system? What are the precautions to be taken in order to reduce/avoid fouling in a magnetic induction-based heating unit for milk?
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Litterature seems to be poor in LCA references or other environmental indicators concerning non-milk beverages.
I'm interested in beverages from almonds, soy, oat, rice and coco, comparing to animal milk and dairy products.
The aim is to know more about the strengths and weaknesses of each, in a multicriteria perspective.
Do you know any publication, report or team working on this topic?
A great thank in advance.
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Dear Armelle,
I hope the reference below might help.
1. From popular press:
2. The scientific publication that the popular pressed was based on:
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I repeated my western blot 5 times with 5 different samples, trying to detect phospho-IRF3, phospho-STAT1 and phospho-STAT3. Sadly, all 5 of them had totally no bands present for all 3 proteins (but GAPDH signal was really strong, so I know my proteins have transferred). Any tips?
I use 5% milk to block my membrane for 30mins at room temperature, and 5% milk to dilute my phospho antibodies and incubate them overnight at 4°C. Will it be better to use BSA? And if so, how do I prepare them with BSA?
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Hello,
Yes, it is better to use BSA.
You should never use milk while detecting phospho protein by Western Blot. Milk contains casein, a phosphoprotein that will bind to anti-phospho antibodies causing non-specific binding and high background. Milk may mask some antigens if they are present in low abundance which would result in faint bands.
For detection of phospho protein by Western Blot you should use 5% BSA in TBST for blocking, primary antibody in 3% BSA in TBST and secondary antibody in 3% BSA in TBST.
Also, you need to add Phosphatase inhibitors like sodium orthovanadate and sodium fluoride in the lysis buffer to prevent dephosphorylation of phosphorylated proteins.
Best Wishes.
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I have a freeze dried dairy probiotic mix that contains 2 bacterial species that i want to isolate to use in my research, I'm planning to seperate them on blood agar but what do you recommend i do prior to that? Is mixing in distilled water or nutrient broth sufficient? I have 2 other pure ATCC bacteriums I'm using that method for but I'm not sure if it's different for milk based cultures
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check the article below may help you Nadeen Al-Otaiby
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In bacterial counts, sometimes for the specific bacterial count, such as Enterobactericeace/ Staph. aureus count from milk samples, the count number is null/Zero for some samples. Then what we can do for log transformation of the value. As the log-transformed value of 0 becomes infinitive? And if we remove the samples from the count, perhaps the mean will be changed as the number of observations will be reduced? Would you please correct me or suggest your opinions?
Thanks in advance
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I explain these type of issues in the attached paper...have a look
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#research #biotechnology #spectroscopy
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Molecular fluorescence spectroscopy is one of the most sensitive and highly selective spectroscopic methods, which can detect extremely low amounts of chemical substances. In the milk industry, it is used for the determination of vitamins, fatty acids, residual amounts of antibiotics, and the identification of different milk species in dairy products.
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Need some research articles related to the preparation and stability of walnut milk .
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I want to administer tamoxifen to P9 neonate mice. Does anyone have any experience injecting tamoxifen in the nursing mother in order to administer tamoxifen to her pups? If so, what is the recommended dosing strategy and how long does it take for the pups to be exposed to tamoxifen? Thanks!
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It has not been answered definitively. Yet, there are obvious effects in postnatal mice that were exposed to lactating mothers that in turn received TAM for certain time periods. It is not certain that TAM is passed through breast milk as it is in order to activate the CreERT2 system in neonates. My guess is that it should work.
Prolonged TAM administration will seize lactation in those mums.
Y
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Hello,
I'm trying to select among different peptones from different sources such as potatoes, meat, milk solids etc. for C. Elegans growth medium. What difference do they make? Any suggestions about which one I should choose.
Thanks.
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I have been using a nonfat dry milk solution (100 g/L) for Salmonella pre-enrichment on samples of cocoa products. This solution is recommend by ISO 6887-4, instead of Buffered Peptone Water, since cocoa has antimicrobial compounds, and milk casein can avoid this activity. The ISO standard recommends, but does not explain the preparation instructions:
- The sterilization procedure is the main issue because the 10% skim milk solution always caramelizes when trying to sterilizate it on autoclave (already tried: 121°C for 5 min; 115°C for 10 min; 110°C for 15 min). Considering that I only have this equipment for sterilization, how can I avoid the caramelization? Does the caramelization affects Salmonella growth??).
Notes:
- Also tried a sterilization cycle of 20 min at 106°C. These were the only conditions that do not caramelized the solution.
- I don't have 0.22 µm filters.
- I have tried many diferent autoclavation cycles based on this question: https://www.researchgate.net/post/How-can-I-sterilize-skim-milk-and-avoid-caramelization
- A 1% (w/v) Brilliant Green solution was prepared. Is it safe to aplly on the milk solution without inhibiting Salmonella growth? The reason that I have not been using Brilliant Green is because our cocoa samples don't usually have high bacterial counts (100-1000 x 10³ CFU/g).
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Hi everyone! I have had good luck asking questions before so I thought I should ask this. Has anyone else ever noticed that fat globules surrounding secretory tissue seem to prevent cells from emerging from the tissue? These are plated secretory tissue from bovine mammary glands. Fibroblasts and mammary epithelial cells emerge from tissue but I've noticed that there are none where there is a sort of "halo" of milk fat globules. Not sure if this is just a coincidence or maybe I just don't notice them as much when there are cells there.
I have the milk fat "halo" pictured and then a picture of emerging cells on another piece of tissue. Thank you.
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Unfortunately, I do not have information in this field and I think that you can obtain information in your field of specialization by searching in scientific sites interested in this field. I wish you success and success.
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If I have a milk sample and isolation of exosomes by ultracentrifugation and measure the size of exosomes by zeta sizer, the problem is that the mean size is high, about 373nm; what can I do to get a size less than 200nm?
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Hello guys,
I need some help with my WB troubleshooting.
I'm investigating Lung tissue of mice for different Cytokines.
In all my Westernblots from different samples I got strong non-specific bands , one between 150-100 kDa and on at 75 kDa and a faint one at 25kDA, which is not optimal because some of my Cytokines are in the same kDa range.
I have already done an WB only with the secondary antibody and apparently it's the cause of these non-specific bands, because I have got the same non-specific Bands like in my other WB. Even after I have changed to a different secondary Ab I have got the same results.
I did the block (1h 30min) with Milk 5% and I also tried BSA 5%.
All the first antibodies are incubated at 4 degree over night and the host is rabbit.
The secondary antibody (goat anti rabbit igG) was diluted in 5%Milk (TBS+ 0,1% Tween) 1:10000 and incubated for 1h.
Do you guys have any explanation for these non-specific bands.
The picture is from a WB which was only incubated with my secondary antibody. (I cut the Membran in to pieces)
Thank you guys for your help.
Kind regards
Marco
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Hello
You need to optimize the secondary antibody concentration. May be 1:10000 is too high. You can further dilute the secondary antibody, and you can go upto 1:20000.
Also, use affinity purified secondary antibody.
Good Luck.
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Dear Expert, I am trying to detect two proteins ( MW 37 kDa and 10 kDa) by Western Blot. I can easily detect the first protein (37 kDa but I have a problem detecting the second protein (10 kDa). I followed these protocols and it worked for me several times. Suddenly it is now working
1. Loaded 20 ug protein from cell lysate (denatured after mixing BME, LDS)
2. Loaded to NuPage 4-12% bis tris with MES buffer (run 35 min)
3. Transfer to PVDF membrane for 1-2 H (wet)
4. Washed using TBST
5. Blocked with 5% Milk
6. Blotted with First Ab (1:1000, cell signaling), incubated ON
7.Washed (TBST) > blotted with Secondary Ab (1 H, 1:2000, cell signaling) with 5% Milk
8. Washed 20 mL x 5 times x 5 min > developed with Thermo Scientific™ Pierce™ ECL Western Blotting Substrate
9. Visualized and detected first protein (37 kDa)
10. Washed > blocked again with 5% Milk (1 H)
11. Blotted with primary Ab (1:1000) for another protein (10 kDa), incubated ON
12. Copied protocol steps 7-9
This time I could not see any protein band, only a WHITE SCREEN. I used this protocol 10+ times and it worked, Suddenly it is not working!
Does anyone know what could be the reasons?
Thanks
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You could try to spot-blot your lysate onto a membrane (just 1 µL placed onto the membrane and given a minute to bind) and then develop like a western. This will tell you whether the lysate contains anything that reacts with the primary antibody, irrespective of molecular mass.
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We want detect mycobacterium avium subspecies paratuberculosis from raw milk and feces.
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there are about 30 FAO recommended microsatellite markers for genetic characterization of animal genetic resources so how i can identify which marker is concern with diversity or milk traits. in NCBI when i search via accession no of markers it only shows sequence. so please suggest how to identify
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Any paper or PDF report references on camels - dromedaries in Libya and Tunisia ?
- breed types, local name of different breeds
- management ( meat, milk, wool-hair, etc)
- diseases
- general info ?
Thank you
Regards
Gus Gintzburger
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Kindly check the following RG link:
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I have to quantify milk whey protein by RP-HPLC using a 300 Å PLRP-S column. Milk whey was obtained by precipitating caseins by adding 10 % HAc, followed by 10 % NaAc to buffer the system. Can I run these samples through that column using the following gradient and eluents?
Eluent A: 0.1 % TFA in H2O
Eluent B: 0.1 % TFA in Acetonitrile
Gradient:
8 min: 75% A; 25% B
2 min: 65% A; 35% B
7 min: 64-36
6 min: 63-38
0.5 min: 0% A; 100% B
1.5 min: 75% A; 25% B
Thanks in advance
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I've separated total lipids from the milk and intended to make liposomes out of it, can anyone guide me on which of the method is the most appropriate for total milk lipid liposomes preparation.
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I have analysed infant milk powder with Raman microscopy. However, the Raman shift (cm-1) is very high and it's not what I was looking for. Usually the Raman shifts of milk powder is between 400 cm-1 and 4000 cm-1 and this is beyond those number. What went wrong? I am also sure that the unit is cm-1 and not something else.
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I am doing physico-chemical analysis (nutrional profiling) of different raw milk and milk byproduct using a Lactostar Funker Gerber machine. This require to use a mucasol reagent which is not accessible in our region (RDCongo). So is there any other product that can be used and give reliable results?
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Can you explain more for the purpose of help, thank you
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COVID-19 greatly affect the animal production sector in Bangladesh. Due to lockdown, farmers are not able to sell their farm products like egg, milk. Marketing chain is also affected. In the upcoming Eid, there's a chance to huge loss in beef production due to this pandemic in Bangladesh.
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COVID-19 greatly affects life in general. As for the animal production sector, it causes great losses due to the inability of farmers to sell their agricultural products such as eggs and milk, as well as its impact on farmers, their work and management of fields and farms, and thus the deterioration of production
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I've been having issues visualizing blots when probing for the Myc tag in HEK cells. I'll list my basic step outline that I follow, maybe that will be informative in picking out something I'm doing wrong:
Gel electrophoresis, transfer -> Either block membrane in 5% milk in 1x TBST at 4 degrees overnight or block at room temperature for an hour -> Incubate overnight with primary antibody (Mouse Myc antibody) at 4 degrees; 1:1000 in 5% milk in 1x TBST -> Wash membrane 3x for 15 minutes in 1x TBST -> Incubate in secondary antibody (donkey α mouse) at 4 degrees; 1:5000 in 5% milk in 1x TBST -> Wash membrane 3x for 15 minutes in 1x TBST -> Drip on HRP, wait 3 or so minutes, remove excess HRP and put an extra film on top of the membrane so it doesn't dry out -> Visualize in chemidoc -> See nothing.
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I am performing an in-house ELISA using BSA for the blocking buffer and Skim Milk to dilute the samples and the conjugate.
Also, is it advisable to centrifuge the skim milk with PBS before use?
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An identical blocking agent must be included in both blocking and sample dilution buffers. Immune recognition of contaminants in antigen preparations by antibodies present in test sera: e.g. Anti-BSA antibodies present in human sera react with minor contaminants such as BSA in insulin preparations https://www.sciencedirect.com/science/article/pii/S2215016117300122
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Hi all, anyone knows whether oxytocin can be reliably detected in milk of dairy cows (not injected with exogenous oxytocin). What I've read so far is that there is none or only very small quantities in milk, which makes it difficult to detect/use reliably. Thank you !
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This hormone is a protein in nature. It transport through blood from the site of release to the site of action. Physiologically Oxytocin hormone is important for milking. It causes contraction of smooth muscle cells surrounding the milk producing cells. However, the level of oxytocin in milk is too low to trace. Boiling milk before consumption is a good way to minimize traces of oxytocin in milk.