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What else can I help you with?
What is the size in KDa of mouse IgG on western blot?
Running it on the SDS-PAGE and then immunoblotting (Western blotting) for it, you would get 2 bands: ~ 25 kDa band corresponding to the IgG light chain, and ~ 55 kDa band corresponding to the IgG heavy chain. If you don't use SDS-PAGE but rather a very weak detergent, you would most likely observe a band of 160 kDa, the size of the undentaured protein.
What type of gene is the p53 gene?
p53 (also known as protein 53 or tumor protein 53), is a tumor suppressor protein that in humans is encoded by the TP53gene. p53 is crucial in multicellular organisms, where it regulates the cell cycle and, thus, functions as a tumor suppressorthat is involved in preventing cancer. As such, p53 has been described as "the guardian of the genome" because of its role in conserving stability by preventing genome mutation.The name p53 is in reference to its apparent molecular mass: It runs as a 53-kilodalton (kDa) protein on SDS-PAGE. But, based on calculations from its amino acid residues, p53's mass is actually only 43.7 kDa. This difference is due to the high number of prolineresidues in the protein, which slows its migration on SDS-PAGE, thus making it appear heavier than it actually is. This effect is observed with p53 from a variety of species, including humans, rodents, frogs, and fish..
What is the molecular weight of cellulase?
it is depend on the purity of pectinase enzyme. to know exact value of mw you have to run SDS page for individual sample.
What is sds-page used for?
SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) is a common technique used to separate proteins based on their molecular weight. It denatures the proteins and binds a negative charge to them, allowing for separation solely based on size. It is often used in biochemistry and molecular biology research to analyze protein composition and purity.
What is the minimum amount of protein that can appear in SDS PAGE gel?
Although this would in part depend the size of the protein being separated and stained (for some staining methods), the largest factor that determines sensitivity of SDS-PAGE is the type of staining method used: - If staining is done with coomassie brilliant blue, the limit of detection claimed by most suppliers is 50 ng. In my experience, 100-1000 ng is more accurate for proteins of 20-30 kDa. - If staining is done with silver stain, the limit of detection is much lower (or higher sensitivity). Manufacturers usually claim that 5-50 ng of protein can be visualized, but in my experience 50 ng is the lower limit for average sized proteins (20-30 kDa). - If visualization is accomplished with an enzyme immunoassay, the limit of detection is lower still, as low as 0.1-1 ng (100-1000 pg). - If visualization is accomplished with radio immunoassay the limit of detection becomes much lower again, easily to the picogram level (0.001 ng).
What is the size in KDa of mouse IgG on western blot?
Running it on the SDS-PAGE and then immunoblotting (Western blotting) for it, you would get 2 bands: ~ 25 kDa band corresponding to the IgG light chain, and ~ 55 kDa band corresponding to the IgG heavy chain. If you don't use SDS-PAGE but rather a very weak detergent, you would most likely observe a band of 160 kDa, the size of the undentaured protein.
What type of gene is the p53 gene?
p53 (also known as protein 53 or tumor protein 53), is a tumor suppressor protein that in humans is encoded by the TP53gene. p53 is crucial in multicellular organisms, where it regulates the cell cycle and, thus, functions as a tumor suppressorthat is involved in preventing cancer. As such, p53 has been described as "the guardian of the genome" because of its role in conserving stability by preventing genome mutation.The name p53 is in reference to its apparent molecular mass: It runs as a 53-kilodalton (kDa) protein on SDS-PAGE. But, based on calculations from its amino acid residues, p53's mass is actually only 43.7 kDa. This difference is due to the high number of prolineresidues in the protein, which slows its migration on SDS-PAGE, thus making it appear heavier than it actually is. This effect is observed with p53 from a variety of species, including humans, rodents, frogs, and fish..
What is observed when run a sds-page using the pellet from serum collection?
SDS is a type of polyacrylamide gel in which bacteria can be grown. To see what can be observed, the collection and experiment should be done by the student.
Why is denaturing sds-page used for running sds-page electrophoresis of egg-white lysozyme and not non-denaturing page?
may be because of toomany disulfide linkages
What is the molecular weight of cellulase?
it is depend on the purity of pectinase enzyme. to know exact value of mw you have to run SDS page for individual sample.
What can SDS page tell you?
The size and charge of a protein (usually in kDa) The process involves loading a sample with different proteins and separating them out based on size and charge. The bands that will appear will be the monomer of the protein (1 subunit) as the buffers typically used will typically be ionic in character and compete with the different subunits for ionic binding, resulting in the appearance of only that 1 subunit. For example Hemoglobin is a 64 kDa tetramer protein with 4 subunits (2 alpha, 2 beta) we would expect to see 2 bands, one for each of the 2 different subunits.
What is sds-page used for?
SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) is a common technique used to separate proteins based on their molecular weight. It denatures the proteins and binds a negative charge to them, allowing for separation solely based on size. It is often used in biochemistry and molecular biology research to analyze protein composition and purity.
What are the differences between agarose gel electrophoresis and SDS-PAGE techniques for separating and analyzing biomolecules?
Agarose gel electrophoresis separates biomolecules based on size and charge, while SDS-PAGE separates based on size and mass. Agarose gel is used for larger molecules like DNA and RNA, while SDS-PAGE is used for proteins. Agarose gel uses a gel made from agarose, while SDS-PAGE uses a gel made from polyacrylamide.
What test has replaced the radial immunodiffusion test?
SDS-PAGE method
Who discovered SDS PAGE electrophoresis?
SDS-PAGE electrophoresis was developed by biochemist Ulrich K. Laemmli in 1970. It is a widely used technique for separating proteins based on their molecular weight.
What is difference between sds page and western blotting?
SDS-PAGE is a technique used to separate proteins based on their size, while western blotting is a technique used to detect specific proteins in a sample using antibodies. In SDS-PAGE, proteins are separated by gel electrophoresis, while in western blotting, proteins are transferred from a gel to a membrane for detection using antibodies.
What method could you use to further separate two bands from the same protein fraction after SDS-PAGE?
Electrophoresis is the method that could be used to further separate two bands from the same protein fraction after SDS-PAGE.
