Trypsin specifically hydrolyzes peptide bonds at the carboxyl side of lysine and arginine residues. Recombinant trypsin is free of any other proteases activities, and TPCK is unnecessary and not contained. Unmodified trypsin is subject to auto-proteolysis, generating fragments that can interfere with protein sequencing or HPLC/MS peptides analysis. YaxinBio’s sequencing grade modified trypsin is recombinant porcine trypsin modified by reductive methylation, rendering it resistant to proteolytic digestion. R141080: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 pH optimum 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.Animal origin free:The use of recombinant Porcine Trypsin eliminates the risk of virus presence, and other potential adventitious agents found in animalderived trypsin. YaxinBio Recombinant Porcine Trypsin belongs to the AOF level 3.Stablility:A sterile recombinant trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss in the process of transport and storage.High purity: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.
Names and Identifiers
Enzyme Commission Number
3.4.21.4
WGK Germany
1
RTECS
YN5075000
Certificates
Certificate of Analysis(COA)
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