*Molecular biology grade
Description & Application
Proteinase K is a highly reactive nonspecific serine protease. It cleaves at the carboxylic acid side of aliphatic, aromatic, or hydrophobic amino acids. This enzyme was designated proteinase K because of its ability to hydrolyze keratin. Proteinase K is active with or without the presence of SDS, urea, EDTA or various metal ions, but the activity of proteinase K can be increased by adding the denaturing agents and the structure of proteinase K can be stabilized by addition of Ca 2+. Proteinase K is inactivated by heating to 95°C for 10 minutes or using an inhibitor such as PMSF, AEBSF or DFP. Proteinase K is stable in a wide variety of detergents and buffer salts and at various temperatures and pH.
Proteinase K is capable of inactivating RNases and DNases and is used in the isolation or preparation of high molecular weight nucleic acids. Proteinase K is also useful for helping to characterize enzymes, due to its cleavage specificity.
MW: 28.5 kDa
Activity: ≥30 U/mg
Reconstitute in 50mM Tris-HCl (pH 8.0), 3mM CaCl2
Typically used at a concentration of 50-100 μg/ml
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