|Place of Origin:||China|
|Certification:||ISO 9001 2015|
|Minimum Order Quantity:||10mg|
|Packaging Details:||ice packaging|
|Delivery Time:||7 days|
|Supply Ability:||100000g per week|
|Product:||Recombinant Porcine Trypsin||Cat. No.:||RPT0201|
|Related Product:||Recombinant Carboxypeptidase B||White Lyophilized:||HPLC|
Serine Enzyme Recombinant Trypsin Lysine Protease or Arginine Protease
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 the preparation.
Trypsin will cleave peptides on the C-terminal side of lysine and arginine amino acid residues. The rate of hydrolysis is slower if an acidic residue is on either side of the cleavage site and no cleavage occurs if a proline residue is on the carboxyl side of the cleavage site.
Trypsin will hydrolyze ester and amide linkages of several synthetic substrates.
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.
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.
1) Recombinant porcine trypsin provides increased specific activity and eliminates contaminating proteases activities found in extracted enzymes.
2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A.
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 thawing.
≥3800 USP units/mg pro
NLT 70% β-trysin, NMT 20% α-trypsin
No chymotrypsin, carboxypeptidase A, and other protease contaminant.
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 trypsin with 1mM HCl.The ratio to aimed protein is 1:50 to 1:1000 (w/w).The optimum pH is 7-10.
Contact Person: Miss Eland