Recombinant Porcine Trypsin Peptide Fingerprinting Analysis Protein
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, e.g.EDTA.
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
Source: Porcine trypsin,expressed in E.coli.
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
≥3800 USP units/mg pro
NLT 70% β-trysin, NMT 20% α-trypsin
No chymotrypsin, carboxypeptidase A, and other protease
Unit Definition: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