Human Trypsin, Cleave C-terminal Peptide Bond of Lysine and
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
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.
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
3) Purity is more than 95% by HPLC.
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).
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