Recombinant Trypsin E.coli Animal Components Free Trypsin
Enzyme Commission (EC) Number: 184.108.40.206
Molecular Weight: 23.3 kDa (porcine)
Extinction Coefficient: E1% = 12.9 - 15.4 (280 nm)
pI: 10.1 - 10.5(porcine)
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 pH optimum of trypsin is pH 7.0 - 9.0. The enzyme is
inhibited by serine protease inhibitors, e.g. PMSF, aprotinin,
soybean trypsin inhibitor and by metal chelating agents, e.g.,
Recombinant Porcine Trypsin is a genetically engineered protein
expressed in E.coli and purified by
high pressure liquid chromatography. There are no any other
contaminating enzyme activities. No protease inhibitors such as
PMSF are contained in the preparation.
Molecular Weight: 24 kDa5 (porcine)
Extinction Coefficient: E1% = 14.4 (280 nm)
pI: 9.32 (porcine)
Trypsinogen, the proenzyme (zymogen) form of trypsin, is produced
in the acinar exocrine cells of the pancreas. Three isoforms are
excreted from the human pancreas. The cationic and anionic forms
are the predominant human isoforms. The inhibitor-resistant
mesotrypsinogen is found only in trace amounts.The proenzyme is activated only after it reaches the lumen of the
small intestine. Enterokinase activates pancreatic trypsinogen to
trypsin by the hydrolysis of a hexapeptide(for bovine trypsin at
the Lys - Ile peptide bond) from the NH2 terminus.
Animal origin free:The use of recombinant porcine trypsin
eliminates the risk of virus presence, and other potential
adventitious agents found in animal-derived trypsin. YaxinBio
Recombinant Porcine Trypsin belongs to the AOF level 3.
Stablility: A sterile recombinant trypsin lyophilized powder
eliminates the contamination risks and decreases the chance of
activity loss in the process of transport and storage.
High purity:Recombinant porcine trypsin provides increased specific
activity and eliminates contaminating proteases activities found in
extracted enzymes.No other contaminating proteases such as
chymotrypsin or carboxypeptidase A.