Enzyme Trypsin Serine Lysine Protease Arginine Protease Recombinant
Trypsin can autocatalytically activate more trypsinogen to trypsin.
Trypsin consists of a single chain polypeptide of 223 amino acid
residues. This native form of trypsin is refered to as β-trypsin.
of β-trypsin (which is cleaved at Lys- Ser in the bovine sequence) results in α-trypsin which is held together
by disulfide bridges. Trypsin is a member of the serine protease S1
family. The active site
amino acid residues of trypsin include His and Ser
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 of
trypsin is pH 7 - 10. The
enzyme is inhibited by serine protease inhibitors, e.g. PMSF and by
metal chelating agents,
Recombinant Porcine 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.
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.
1) Recombinant porcine trypsin provides increased specific activity
and eliminates contaminating proteases activities found in
2) No other contaminating proteases such as chymotrypsin or
NLT 70% β-trysin, NMT 20% α-trypsin
No chymotrypsin, carboxypeptidase A, and other protease
One USP unit of trypsin activity will produce a Delta A253 of 0.003
per minute in a reaction volume of 3.0ml at pH7.6 and 25℃, with
BAEE as a substrate (1cm light path).
Prepare 1-10mg/ml recombinant trypsin with 1mM HCl.The ratio to
aimed protein is 1:50 to 1:1000 (w/w).The optimum pH is pH7-10.
Recombinant 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