|Place of Origin:||China|
|Certification:||ISO 9001 2015|
|Minimum Order Quantity:||10mg|
|Packaging Details:||dry ice|
|Delivery Time:||7 work days|
|Supply Ability:||1000g per week|
|Source:||E. Coli||Purified By:||HPLC|
|Physical Form:||White Or White-like Lyophilized Powder||Additives:||Carbohydrates|
|Protein Content:||35% ～ 70%||Related Product:||Recombinant Trypsin Solution|
Alkaline Protease Recombinant Enzyme Trypsin Trpsin
Molecular Weight: 24 kDa
Extinction Coefficient: E1% = 14.4 (280 nm)
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. Bovine trypsinogen consists of a single polypeptide chain of 229 amino acids and is cross linked by six disulfide bridges. 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. Autolysis 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, 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.
≥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 3.0ml 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.
Contact Person: Miss Eland