Due to many proline residues it migrates slower on sds page and appears heavier than it is.
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..
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.
SDS - PAGE is apparently used to seperate proteins. The proteins are by nature different sizes. SDS works as a stabilizer by separating proteins according to similar forms.
it is depend on the purity of pectinase enzyme. to know exact value of mw you have to run SDS page for individual sample.
It is the gel of choice for SDS PAGE
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..
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.
SDS - PAGE is apparently used to seperate proteins. The proteins are by nature different sizes. SDS works as a stabilizer by separating proteins according to similar forms.
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.
may be because of toomany disulfide linkages
glycine molecular weight high so mobility also high so using in SDS PAGE
it is depend on the purity of pectinase enzyme. to know exact value of mw you have to run SDS page for individual sample.
The major drawback is that treatment with SDS denatures the protein, meaning you are not looking at it in its natural state.
It is the gel of choice for SDS PAGE
Laemmli U. K.
SDS-PAGE method
Glycine increases the mobility of the gel.