|Place of Origin:||China, Shanghai|
|Certification:||NQA ISO 9001:2015|
|Minimum Order Quantity:||10mg|
|Packaging Details:||ice packaging, carton|
|Delivery Time:||7 working days after confirming payment|
|Supply Ability:||1000g per year|
|Product Name:||Recombinant Trypsin||Size Of Panel:||10mg，100mg，1g Or Bulk|
|Source:||E. Coli||Purified By:||HPLC|
|Specific Activity:||≥3800 USP Units/mg Pro||Protein Content:||Refer To COA|
cell culture trypsin
For Enzymatic Hydrolysis of Protein, CAS 9002-07-7, Recombinant Trypsin
Enzyme Commission (EC) Number: 18.104.22.168
Molecular Weight: 23.3 kDa (bovine & porcine)
Extinction Coefficient: E1% = 12.9 - 15.4 (280 nm)
pI: 10.1 - 10.5
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.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.
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.
The activity of most preparations is determined by a continuous rate spectrophotometric assay
and expressed in BAEE units.
Unit Definition: One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25 °C using BAEE
as substrate. Reaction volume = 3.2 mL (1 cm 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 thawing.
Contact Person: Miss Eland