Description
Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The optimum pH is pH 7.0 - 8.0. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA.
Recombinant human trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.
Form
White or White-like lyophilized powder
Enzyme Commission Number
EC 3.4.21.4
Activity
>2500 USP u/mg protein
Unit Definition
One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.0ml at pH7.6 and 25°C, with BAEE as a substrate (1cm light path).
Storage
Recombinant human trypsin lyophilized should be stored under 2° C-8° C in sealed container. It is stable within 24 months. After dissolved, it should be stored under -20° C. It is stable within 24 months and above 90% activity remained after 10 times repeated freezing and thawing.
Synonyms
α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin
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