Stable Recombinant Human Trypsin Enzyme, Expressed in E.Coli, Purified by HPLC

Stable Recombinant Human Trypsin Enzyme, Expressed in E.Coli, Purified by HPLC

Human Trypsin

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 - 10. 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.

Human Trypsin 1, encoded by the PRSS1 gene, is also known as cationic trypsinogen . Constituting approximately two-thirds of the total trypsin content in normal pancreatic juice, it is the most abundant trypsin isoform produced by the pancreas. It contains a signal peptide (residues 1‑15), a pro region (residues 16‑23), and a mature chain (residues 24‑247). Trypsin 1 is synthesized in the pancreas

and secreted into the duodenum lumen, where it is activated by enterokinase. Its major physiologic function is to digest food and to activate other pro-enzymes . Mutations in the PRSS1 gene can

cause hereditary pancreatitis

Main Features

Unit Definition

One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in

a reaction volume of 3.2ml at pH7.6 and 25℃, with BAEE as a substrate (1cm light path).

Storage Instructions

Recombinant human trypsin lyophilized should be stored under 2℃-8℃ in sealed container. It is

stable within 24 months.After dissolved, it should be stored under -20℃. It is stable within 24 months

and above 90% activity remained after 10 times repeated freezing and thawing.