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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).

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What are pre-stained proteins?

Prestained proteins are proteins that are already stained permanently so they are visible while running the gel. This technique makes pre-stained protein ladder, that are useful to track the proteins running on the SDS-PAGE gels. In addition the marks or protein ladder can be transferred to blot membrane by western blotting.


Why p53 is run as 53 kda on sds page?

p53 is detected as approximately 53 kDa on SDS-PAGE because it is a 53 kilodalton (kDa) protein. SDS-PAGE separates proteins based on size, so the molecular weight of p53 corresponds to the band observed at 53 kDa on the gel.


Why to use dissolving gel in SDS-PAGE?

Dissolving gel in SDS-PAGE serves to separate proteins based on their size, allowing for effective analysis of protein samples. The gel matrix, composed of polyacrylamide, provides a porous environment that facilitates the migration of proteins when an electric current is applied. By using a dissolving gel, researchers can achieve higher resolution in protein separation and facilitate subsequent applications such as Western blotting or mass spectrometry for protein identification. Additionally, it ensures the proteins are denatured and uniformly charged, which is crucial for accurate size determination.


Is it possibile to see a double band on a SDS page. And why is that?

SDS page resolve the proteins in the sample based on their molecular mass and the negative charge(and shape). if your sample has two proteins sure you can see two bands. if they are degraded by a unspecific protease during sample preparation it shows more than two bands. Same applies when you run "n" proteins, you can detect "n" number of bands.


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..

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