For Enzymatic Hydrolysis of Protein, CAS No: 9002-07-7, Recombinant Trypsin

For Enzymatic Hydrolysis of Protein, CAS 9002-07-7, Recombinant Trypsin

Recombinant Trypsin

Description

Trypsin

Enzyme Commission (EC) Number: 3.4.21.4

Molecular Weight: 23.3 kDa (bovine & porcine)

Extinction Coefficient: E^1% = 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.

Assay Method

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).

Recommend Usage

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.

Storage Instructions

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.