Description
Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.
Abbr
Trypsin, Recombinant (Bovine)
Applications
Trypsin has been used in a study to assess the use of animal protein-free products for passaging adherent human adipose-derived stromal/stem cells. TrypZean has also been used in a study to compare a recombinant trypsin with the porcine pancreatic extract on sperm used for the in vitro production of bovine embryos.
Product Overview
Trypsin eliminates the introduction of animal source contaminants found in traditional bovine and porcine trypsins.
Enzyme Commission Number
EC 3.4.21.4
Activity
> 3650 units/mg solid (USP)
Warnings
Manufactured utilizing ProdiGene′s proprietary transgenic plant protein expression system.
Pathway
Activation of Matrix Metalloproteinases, organism-specific biosystem; Defective AMN causes hereditary megaloblastic anemia 1, organism-specific biosystem; Defective CUBN causes hereditary megaloblastic anemia 1, organism-specific biosystem
Function
calcium ion binding; serine-type endopeptidase activity
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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