Signal Transduction - Science topic
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Questions related to Signal Transduction
I start this discussion so we can all share our favourites books on cell signaling or signal transduction. I am highly interested in GPCRs.
So I will start first.
"G Protein-Coupled Receptors: Structure, Signaling, and Physiology" by Sandra Siehler, Graeme Milligan is my favourite book so far.
Since the fetal bovine serum contains growth factors such as EGF，I am wondering whether the EGF induced signalings are continuously activated in cells cultured with serum- supplemented medium? For example，EGF activated PLC induced PIP2 hydrolysis. Does this mean that the PIP2 levels in membrane of cells cultured with serum are very low? Since PIP2 hydrolysis generates DAG and IP3, which in turn induces activation of PKC kinases, does this mean that PKC kinases are continuously activated in cells cultured with serum? In most articles, cells treated with EGF should be starved in serum-free medium before, however I did not observe PIP2 hydrolysis and PKC activation in normally cultured cells.
The Wnt signal transduction cascade controls myriad biological phenomena throughout the development and adult life of all animals.
I have seen many research works that have been used LiCl as a WNT activator but few research studies attempted to use it as an inhibitor.
Could anyone clarify, how LiCl would be used as a WNT inhibitor in developmental biology research?
Two signaling pathways can activate the host innate immunity against viral infection. One of the pathways utilizes members of the Toll-like receptor (TLR) family to detect viruses that enter the endosome through endocytosis. The TLR pathway induces interferon production through several signaling proteins that ultimately lead to the activation of the transcription factors NF-κB, IRF3 and IRF7. The other antiviral pathway uses the RNA helicase RIG-I as the receptor for intracellular viral double-stranded RNA. RIG-I activates NF-κB and IRFs through the recently identified adaptor protein MAVS, a CARD domain containing protein that resides in the mitochondrial membrane. MAVS is essential for antiviral innate immunity.
Is there any references that explain the involvement of RIG-I mediated antiviral innate immunity induced by Baculovirus?
I'm trying to prepare biological network pathways and signal transduction. Based on the requirement, please suggest online available tools to draw scientific figures.
I am trying to detect phosphorylated forms of Akt (Ser and Thr) in rat skin tissue. I have used p-Akt (S473) (587F11) Mouse mAb #4051 from Cell Signaling, and although this one works flawlessly in human, it does detect two bands in rat samples, and the upper one does not run at 60kDa, but more like at 50-55kDa). The similar is observed with Phospho-Akt (Ser473) (D9E) XP® Rabbit mAb #4060 and Phospho-Akt (Thr308) (C31E5E) Rabbit mAb #2965.
I include the sample of stimulated p-Akt in human cells versus one in rat tissue using the same Ab.
If you validated any p-Akt Ab that worked for your stimulated/unstimulated rat tissue, and does not detec the bottom band, please let me know, since it would save me a lot of time and $$$.
Plants acquire nutrients from soil but we also know that there is variability in soil fertility even within same field. However, the area where nitrogen availability is less plant always tend to spread its root towards the area where sufficient N is available. So my question is that what make plant roots to spread in search of N? How plant comes to know that N is available in that specific direction? is there any signal transduction by roots to find N rich area? if yes then kindly share its mechanism.
Is the introduction of labeling bad while detecting small molecules? If yes, what are the major disadvantages of using labels for signal amplification in the detection of small molecular weight ( <1 kDa ) compounds?
I want to study cell signaling. where the protein synthesized from signal transduction by cell A is secreted and is important for signal transduction pathway to cell B. Plz suggest such 2 cell lines, where I can track its live progress.
I went through papers in which people had carried out thymidine block followed by nocodazole block for synchronizing cells in the G2-M phase. However, after the thymidine block for 24 hrs,a 3 hr gap is maintained before the nocodzole tretment.
What would be the consequence if this 3 hr duration is not followed and instead cells are treated with nocodazole immediately after the 24 thymidine treatment?
I need an updated (published in the last 5 years) book clearly and extensively explaining the concepts underlying developmental processes (embryogenesis, flower, root, shoot and leaf development) in plants and how plant endogenous signals and environmental signals are perceived and integrated into the initiation, proceeding and control of developmental processes.
Thanks in advance
I'm currently having problems with Western blots using the following antibodies from Cell Signaling:
They seem to work very inconsistently, sometimes giving no signal at all. They used to work better for the first 6 months, giving the correct bands. It's not a technical issue - I'm regularly running multiple blots with ~30 different primary Abs, and they work consistently. Ponceau and GAPDH indicate the presence of protein. It's also not an issue of molecular weight - other 100-200 kDa proteins are detected without problems.
I would like to try out some new antibody clones, which ones would you recommend?
I have grown HepG2 cells for a couple of years, never had any problems serum starving and stimulating the cells (using pS473-Akt as a readout). But recently my cells stopped to respond: either pS473-Akt level is still high in starvation condition or still low after stimulation. I've changed media, serum, tested out different batches of cells I froze before which were definitely working back then but still can't solve the problem. One thing I want to mention is, once I changed to a new media and the cells became good but right after one split, they were bad again! Anyone has experienced the same thing?
We have compounds that have demonstrated innate immune stimulation in vivo, however are unclear on the mechanism of action/specific receptor involved. We had thought they stimulated TLR9, however upon analysis using a TLR9-specific reporter cell line, we found this not to be the case. Since we don't know where exactly to look next and creating/buying receptor-specific cell lines is time-consuming/costly, we are trying to devise a cheap and quick method.
We believe it isn’t any of the other TLRs, so I devised a quick way to rule this out involving measuring MyD88 & TRIF levels in stimulated cell lysates via western blot, as I believe one out of these two molecules is always required for TLR signal transduction – no increase in signal over the negative control in each would therefore show that the compounds are operating via a TLR-independent mechanism. However, I am unaware whether stimulation of the associated TLR causes increased expression of these molecules, or simply localisation to the receptor site, and cannot find any examples of this technique used to measure TLR stimulation in the literature. Essentially – do you think this would work before I order in antibodies? Or if not, are there any other cheap, quick methods for measuring stimulation of all TLRs?
I am using calcium channel blockers to reduce intracellular calcium level.
Based on previous reference we informed that intracellular calcium amout is 100nM.
So after treatment of CCBs which percentage inhibition of calcium level disrupt calcium homeostasis as well as which percentage of calcium inhibition can effect on intracellular signal transductions?
Thanks in advance.
What is the simplest, quickest, and/or cheapest way of finding out whether a molecule is involved in a novel quorum sensing / cell-cell signaling / signal transduction pathway?
Most literature explains assays that build on systems that have already been established, involving AHLs, AI-2, DKPs, DSFs, HAQs, etc., but our suspected signal molecule is not similar to those. It might be involved in cessation of cell growth, and we sort of have growth curves at different concentrations of the compound.
Outside of forward and reverse genetics, which would be especially difficult for our organism, an Archaeal methanogen, I’ve seen the most plausible options in this paper:
Affinity chromatography and photo-affinity labeling don’t seem simple or quick or cheap, though.
I’d appreciate any suggestions.
bistability is about the switching between two states from one state to another state. it correlates with Michaelis-Menten equation that explain enzyme kinetic activity. Anyway, there are some theoretical studies showed that it can be applied in phosphorylation. Could it possible to applied to other signal transductions? Thank for your help
I would like to know the difference between newborn and adult cardiac fibroblasts inculdes characters and signal transduction. Who can suggest some references? Thank you.
Steroid hormones are usually transported in the blood stream by carrier proteins. At their target cells they are released and can then either bind to surface receptors or diffuse through the plasma membrane due to their lipophilic nature. In the cell they are bound to receptors that enter the nucleus and influence gene expression. Some aspects of this model are not clear to me:
1.) How do carrier proteins in the bloodstream "know" when to release the hormones? How are target cells recognized? The ability of steroid hormones to directly pass the plasma membrane makes specificity somewhat difficult to achieve.
2.) So most steroids can pass through the plasma membrane because they are lipophilic. But then they have to travel through the hydrophilic cytoplasm to reach their destination. Are steroid hormones amphiphilic? Or are they immediately bound to a receptor protein once they pass the plasma membrane?
3.) If steroid hormones are capable to pass the plasma membrane they should also be able to pass the nuclear membrane without being bound to a receptor protein, yet this does not seem to be the case. The lipid composition of plasma and nuclear membrane is different, but can this explain the differential diffusion behaviour of steroid hormones?
4.) How are steroid hormones that have served their purpose removed from the cell? Are there deactivating enzymes? If yes, how are these regulated? Or can the steroid hormones, once released from their receptors, simply diffuse out of the cell? If this is the case, how is a "re-binding" of the hormone to another receptor protein prevented?
I would appreciate if somebody could help me with these questions and/or point me to literature that explains these processes in more detail.
It is generally accepted that KRAS mutations shortcut the signal transductions which physiologically tranfer extracellular signals into nucleus. The mutated KRAS forms a blocking configuration at GTP-binding site, and becomes constitutively active. However, there are also some literatures reporting that KRAS mutated cells do not completely bypass upstream receptors. For example, in NSCLC EGFR knockdown inhibited cell proliferation in KRAS mutated cells-in a degree much more than it affected KRAS wild type cells. (BMC Med, 2012, 10: 28) There are several other papers indicating that KRAS mutated cells still need receptor tyrosine kinases to transduce signals. Does anyone have any idea about this contradiction? Is there any clinical evidence regarding this issue?
I'm having a hard time finding a broad and in-depth review or book chapter that covers PDGF signaling pathway focusing on its relationship to ROS generation during signaling transduction in mammalian cells. Any suggestions?
Studies I have found that use this tried and true technique (radioactive ligand binding assay) use cell culture preps or dissociated tissue. Do the cells need to be treated a certain way after FACS? Do you recommend membrane prep v intact cells? Thanks!
For example, protein-protein/nucleic acid/lipid interaction pattern, signal transduction pathway they may participate, or some other else.
As the question says, I am looking into the PathScan Antibody Array Kit from Cell Signaling and would like some opinions on it. Is the protocol difficult/confusing, are there better alternatives, and also if anyone has done it with tissue samples.
I have been getting great support from RG members.
Today, i want to ask about phosphorylation.
LATS1, which is known to be a critical component of Hippo pathway,
regulates YAP. As far as i know negative regulators of Hippo pathway
enhances nucleus localization of YAP by inhibiting LATS1.
Here is my question : LATS1 has phosphorylation sites.(S909 and T1079)
I studied that increased phosphorylation at such sites indicates elevated activity of LATS1, affecting loclization of YAP inside cells.
Is there any critical difference between the affect of dephosphorylation of
S909 and T1079 of LATS1? I have heard that phosphorylation or dephosphorylation at different sites in one same molecule can have different effects, which makes related research quite tricky and complex.
I want to know whether such differences exists in LATS1, as i just described above.(ex) Same YAP nucleus translocation but different target gene expression, etc.)
Thank you for your interst and hope for your great achivements in your research
(I will say my genes of interest as A,B and C)
Based on the results so far, A seems to induce translocation of B into nucleus from cytoplasm. As for B, B is already known as a transcriptional regulator of C.
For me, i hypothesized that A enhances nucleus localization of B, which finally upregulates mRNA level of C and finally protein level of C.
Here is my dilemma. I am doing experiments described above under high cell confluency, but I cannot see positive regulation of C by B under such condition. (B localization depends on cell confluency, so B is mainly located in cytoplasm in dense cell condition while it is mainly found in nucleus when cells are cultured under sparse confluency)
I think that because transcription activity of B is very low in dense cell condition, it is difficult for me to confirm positive correlation between B and C expression. The positive side is that i could confirm the outcomes which support that B upregulates C
in sparse condition.
i want to ask whether i can make a research story like this
: I got results which indicate that A acts as positive upstream molecule of B, which increases C expression so A regulates C under high cell confluency.
However, because transcription activity of B is very low under such dense cell density which makes demonstrating increased C expression by B very difficult, i induced enhanced transcription activity of B by seeding cells sparsely, and i could see that B really promotes C expression. A seems to regulate C not only via B but also other factors in high cell confluecy.
For me my idea flow seems quite reasonable but i am concerned about my
quite subjective view. So I want to get some opinions from others.
Thank you for reading so long question!
We would like to be able to screen multiple signaling pathways at once with primary cells after stimulating with whatever stimulus we choose. Doing tons of western blots is not possible so hoping someone can provide an answer to what they have used to look at for example JAK/STAT, MAPK, PI3K, NFkB, etc all at once. So far I've seen R&D has a phosho-kinase array but do need some feedback for what has worked well for primary cells. Phosphorylation flow cytometry is also a possibility but would rather do a broad screen first to give us a clue of what pathways to study further. Thanks!
MYH9(NM-IIA) is known for regulating cell migration. It can express both on cytoplasmic and membrane. If I can down-regulate MYH9 expression on cell membrane, will it effect its function?
In my experiment using C3H10T1/2 cells I found phosphorylation of PKA substrates at band size of In-between 75-100 and 100-150 and also at 150 position. What might be those target proteins?
I used CST antibody 'Phospho-PKA Substrate (RRXS*/T*) (100G7E) Rabbit mAb #9624'
I would like model the synergistic effect of two ligands (one with high affinity and the second with low) onto the same receptor. Both are activators of the receptor. Do anyone have experience with that?
I am looking to test various cdk inhibitors in cell lines and would like to be able to measure relative effects by following levels of phosphorylated target proteins. For example, the retinoblastoma protein phosphorylated at T821 is often used as an in vitro measure of CDK2 activity. Could anyone help me with a analogous target for CDK1- preferably one that is specific for CDK1 activity (ie not typically phosphorylated by other kinases). Many thanks for any help
I want to proof that my protein promotes the activity of PCNA. The interaction of my protein with PCNA and the subunit p50 of polymerase delta is known. After knockdown of my protein the proliferation is decreased. Therefore, I want to show that the absence of my protein reduce the activity of PCNA. Have someone an idea for an assay?
I have a mitochondrial uncoupler that inhibits viral infection. I want to show that this inhibition is due to a lack of ATP. However, the respiratory chain is blocked. I know that ATP in medium is cytotoxic and has difficulties to enter in cells.
In what form should I add ATP to the cells so that it comes in and can be consumed directly without going through the mitochondrial chain? (consumed directly by kinases)
How can one study chronic activation of a receptor (G-protein) with a short half life at the cell surface/high turnover to reduce over-activation? Does increasing the dose of agonist with time improve receptor recycling?
I am doing anti diabetic activity via insulin receptor activation pathway.
I have acess to NIT-1, 3T3-L1 and C2C12 cell lines. what are the method could I use for the checking activity?
I want some literature regarding AKT phosphorylation for insulin receptor activation
How can we do it?
on Which cell lines we can perform AKT phosphorylation.?
I am new to performing MAP kinase and other signalling pathways, please can anyone help me with the drug incubation time I should start with when performing my western blot analysis? I like to know what times are ideal to consider during phosphorylation.
I want to know a gene strongly altered by 17 beta estradiol in human brain endothelial cells, so that i can take that gene as a control for the system.
I know that the LY294002 inhibit the activation of AKT by supressing its upstream key molecule PI3K. But how about perifosine? It is an alkyl-phospholipid. Does it inhibit the activation of AKT partially by directly binding to AKT? I have got a molecule which could totally reverse the inhitition of phosphorylation of AKT by perifosine but not LY294002. I was wondering the underlying mechanism.
I would like to treat my cells with TSA to test effect on the mobility of nuclear protein. As a readout of TSA treatment, what should I check to confirm TSA worked?
Like silenced c-met and ron will lead to inhibition of cell migration and invasion by p42/44mapk phosphorylation and reduce stat 3 activation in cancer cell line. With this pathway, can I apply it in diabetic cell line if I spot there is reduced activation of stat 3 and mapk then link it to less expression of ron?
Can I use it to explain the reduction of wound closure on cell proliferation and cell migration based on an assumption basis or as an indicator of what can that pathway leads to? Or even, what can the receptor do relate to cell migration?
I am confused by the role of cAMP on adipogenesis and lipolysis. I know that when cAMP is high, it activates PKA and thus phosphorylates HSL and perilipin A to facilitate lipolysis, and when cAMP, insulin, and glucocorticoid present together, the "cocktail" can induce adipogenesis. But if both procedure require high cAMP concentration, how does the cell decide which way to go? It does not make sense that the cell differentiates and breakdown lipid simultaneously. Also, insulin is supposed to inhibit cAMP production through PI3K pathway, how come that these two show together in the body to stimulate adipocyte differentiation?
If there are any figures that help illustrate this problem, it is more than welcomed.
i have a jmy protein and akt phosphorylates it but at what sequence site
i wish to compare the diffrent akt phosphyrlation site of jmy on diffrent species
please dont just provide a link give me some depth also as i am stupid.
can you please provide me with the human jmy akt region to which akt phosphorylates then i can do the rest
JMY protein is phosphorylated by AKT i know AKT1 and 2 are anti apoptotic and AKT1 decreases cell motility whereas AKT2 increases motility but what does this mean for when these phosphorylate JMY how do they effect apoptosis, cell motility and autophagy e.g.
i know phosphrylation of a protein affects its function but what does JMY phosphorylaion by akt1 or akt2 do in this context?
any help is appreciated, as i am not very bright could you explain your answer please in some depth
hi there could you please tell me to what sequence on JMY does AKT kinase bind too i have checked on pathwaynet and JMY is indeed phosphorylated by AKT but what exact region in the sequence does it bind too?
any help would be appreciated
could you explain your answer in laymans terms as im not very bright and provide the website to which you found this infomation .
I am working on mRNA dopamine receptor to see the changes of gene expression of these receptor in rat brain in 3 different area
Do we have some webbased tool to do this? Or we just download each pathway gene list to find this? Because common signaling pathway could initiated by different receptors, maybe they want say something similar, does it possible for us to find tools to find this common targets?
I'm looking for an inhibitor of Pi(5)P kinase, publications didn't help me a lot, maybe plumbagin but i'm not sure. I found many inhibitors for Pi3K and Pi4K but not for Pi5K and I need it to inhibit kinases and see effects on bacterial replication in eukaryotic cells. Thank you if you know what molecule can be used.
What are the cell lines I can use it for the experimental studies related to Aquaporin-2 and Vasopressin receptor, which is found in renal cells of the human?
I have seen in Wikipedia that HEK 293 cells should not be used as an in vitro model of typical kidney cells.
Is there such a case that certain antibodies have limited access to the intra-cellular domain of its receptor and this results in a negative staining?
I have been struggling trying to detect signals associated with the intra-cellular β-subunits of the insulin-like growth factor receptor (IGF-1R). Using exactly the same protocol however, I got very good results showing a positive staining of extracellular α-subunits of IGF-1R.
I have tried all the commercially available antibodies against IGF-1R beta-subunit which are applicable for immunohistochemistry, so I was wondering why this is the case.
Also, if my IHC results showed positive staining of α-subunits, can I conclude that the whole receptor is present, rather than saying only the α-subunits of the receptor are present?
I want to induce blockade with DPCPX and SH58261 (Selective A1 and A2A adenosine receptor inhibitors, respectively) in cultured L6 rat skeletal muscle cells as a part of an inhibitory assay. Both inhibitors are insoluble in water and therefore, the solubility is given in DMSO (Dimethyl Sulfoxide). I just wanna know the best DMSO percentage (100% DMSO or a dilution such as 0.5% DMSO) efficient in preparing the inhibitory solutions in required concentration.
Ezrin is a FERM domain cytoskeletal protein that in the inactive state assumes a conformation by which the N-terminal domain binds the c-terminal actin binding tail. I know phosphorylation leads to protein to open up and bind to actin filaments. How can I design a biosensor to detect activation state of Ezrin? what are the positive and negative control constructs?
The bands of WB suggesting the natural compound inhibited the phosphorylation of both Stat5 and Stat3. The extent of reduction of p-Stat3 and p-Stat5 is different, the level of p-Stat5 reduced more remarkable.
So, the questions is, can we just assume that the target of this compound is more likely to be Stat5 or the upstream of Stat5. Or in other words, this compound is more easily combine with Stat5 or the upstream protein of Stat5? If so, I want to know what methods we can use to further prove my assumption.
Meaning, is there a loss of PTEN and/or an increase in upstream signaling to PI3K/Akt that would lead to above average phospho-Akt levels, as compared to other cell lines? Thanks y'all!
I want to check role of Wnt signaling during differentiation of cardiosphere derived cells to cardiomyocytes. Wnt acts in time-dependent manner during differentiation. So, I want to add Wnt inhibitor at different time points of differentiation induction. Is IC50 value to be considered ? or have to check the expression of markers at different time periods of differentiation with different concentrations of inhibitor.
Kindly provide with proper protocol to determine the concentration
In my view the concentration of the ligand is transmitted as the frequency of collision on the receptor. The higher is the concentration of the ligand the number of ligands hitting the receptor per second is higher. But more importantly the receptor should transmit the frequency of ligand collision as a frequency signal onto the next element of the signal transduction pathway, too. This is not as evident as we might think. The collision of the ligand impacts receptor structure, which should be repaired before the next collision. If this does not happen then the receptor will not be aware of the next ligand collision and will be unable to transmit the correct frequency and thus the correct concentration of the ligand. I note, that the information of the concentration is not transmitted, independently whether the receptor is still in its active state (that is continuously activates further elements of the signal transduction pathway) or it is blocked (and does not activate further processes) when the next collision arrives. Do you agree with this visualisation of receptor function? Please give your opinion
I have a bit of headache to find good downstream target gene to track for NFkB and Myc pathway activity.
What I did was treating A549 cell with inhibitors of NFkB (BAY 11-7082) and Myc (10058-F4) for 24 hours and then tracking the downstream gene expression through first generating cDNA (qScript cDNA SuperMix) and real time PCR (Fast SYBR Green Master Mix).
I have tried following list of known NFkB and Myc downstream genes but they show no differences (compare to GAPDH control) or even induction by the inhibitors even though the amplification looks good.
Myc: CEBPB, TERT, CCND2, PTEN, PCNA, TP53, RPL19, E2F1, EIF4A1, EIF4B, EIF4E
NFkB: AGT, CFB, CSF2, CSF3, IFNA1, IFNB1, TNF, LTA, IL6, IL8, ICAM1
I don't know what I did wrong so I get this weird result!
Any suggestion of good downstream targets and possible way for me to fix the experiment would be most appreciated!
please provide me any study related to the activation of phosphorylation of estrogen receptor alpha at serine 167 have any direct or indirect relationship with induction of apoptosis
I am trying to visualize calcium release in primary cells in culture over long periods of time. basically we give a treatment at time 0 and want to do time lapse imaging of calcium release from the ER and its accumulation in the cytosol over a 24 hour period for example.
Does anyone have any suggestions of how to accomplish this. we tried using fura and oregon-green bapta-am, but they seem to be good only for acute calcium release.
I found out that HEK293 cells are not useful for examining PI3-kinase mediated signaling, as they typically display constitutively active Akt, but no reference is cited. Does anybody know where can I find a reference for that source?
Thanks in advance!
I've been using TOPFlash luciferase assays to measure Wnt signalling in HEK293T cells, in order to study the effect of transfecting a protein of interest (a transcription factor) on Wnt signalling. The assay uses a TOPFlash luciferase reporter, which has binding sites for Wnt transcription factor TCF and is expressed when the Wnt pathway is active, and a second (control) reporter, Renilla luciferase, which is expressed constitutively and is used to normalise data to correct for transfection efficiency and sample handling. The issue I'm having is, when I co-transfect my protein of interest alongside the two reporters, I get an increase not only in the TOPFlash reporter signal but also in the Renilla control reporter signal. Others have reported seeing a modulation of Renilla expression by experimental factors (first link below), which it is suggested could be due to factors interacting with regulatory elements in the TK (or other) promoter, and it was suggested that using a promoterless Renilla (pRL-Null) could overcome this problem (1st/2nd link). However, I have tried using the promoterless Renilla plasmid and found I still have the same problem.
So my questions are these:
1) Why might my Renilla signal be increasing when I transfect my protein of interest (NB. Total protein levels in the cell, measured by BCA assay, do not appear to be increased in concert with the increase in reporter signal)
and, related to this
2) How is transcription initiated when there is no promoter? I can't seem to find anything on this, but transcription must be happening, because I'm seeing a substantial amount of signal with the Renilla construct.
The completion of genome sequences from human and mice suggested a regulatory role of space (Chorobiology) in controlling biological phenomena and activities. Consequently fundamental constants of mathematics such as π, the ratio of a circle's circumference to its diameter, should have a role in describing properties and establishing control in biology.
The Greek mathematician Archimedes who found π, developed a rigorous approach to approximating π. Archimedes observed that polygons drawn inside and outside a circle would have perimeters somewhat close to the circumference of the circle.
While π is an infinite number (never ending No), it relates to a symmetric geometrical image, the circle, but intriguingly Archimedes used polygons to measure the circumference of the circle.
What could be the meaning or the role of π in the control of signal transduction? And why π is an infinite number?
Hi Everyone I am looking for antibodies for ER pathways that works in INS-1 cells or any other cells. There are lots of paper out there but I want to know if anybody have tried these antibodies in INS-1 cells and that has worked perfectly. The antibodies I am interested are as follows:
spliced-XBP1. p-PERK, PERK, p-IRE1 alpha, Total-IRE1 alpha, ATF4, ATF6 active.
Any information will be highly appreciated. Thanks in advance.
I want to test antioxidant drug in spontaneous colorectal cancer mouse model. By knocking down NLRP3 inflammasome, mice which already having spontaneous colitis develops tumor in proximal colon at age 12, without giving any carcinogen. I am wondering whether my antioxidant will work on this model or not? I want to inhibit the ROS level in order to ameliorate the progression of colitis to cancer.