Human Trypsin, Cleave C-terminal Peptide Bond of Lysine and Arginine

Human Trypsin, Cleave C-terminal Peptide Bond of Lysine and Arginine

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.

Advantages

Animal origin free:The use of recombinant Human Trypsin eliminates the risk of virus presence, and of any other potential adventitious agents found in animal pancreas-derived trypsin. YaxinBio Recombinant Human Trypsin belongs to the AOF level 3.

Recombinant human trypsin:The amino acid sequence is the same as the Human Trypsin 2.

Stable:A sterile recombinant human trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss in the process of transport and storage.

High purity:

1) Recombinant human trypsin provides increased specificity and eliminates contaminating activities found in lower purity enzymes.

2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A.

3) Purity is more than 95% by HPLC.

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).

RECOMMEND USAGE

Prepare 1-10mg/ml recombinant human trypsin with 1mM HCl.The ratio to aimed protein is 1:50 to 1:1000 (w/w).The optimum pH is pH7.0-11.0.