Trypsin is a serine protease that cleaves peptides on C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7.0-8.0. Trypsin is inhibited by serine protease inhibitors including TLCK (N-p-tosyl-L-lysine chloromethyl ketone), PMSF (phenylmethanesulfonyl fluoride), benzamidine, soybean trypsin inhibitor, and ovomucoid
Trypsin (Human, Recombinant) is genetically engineered human trypsin expressed in E. coli and purified by high pressure liquid chromatography. It has animal free source of origin, so is virus free and also it has no other contaminating proteases such as chymotrypsin and carboxypeptidase. No protease inhibitor such as PMSF involved in its preparation.
Trypsin (Human, Recombinant) can be used to make cell-dissociation reagent. It can be used for digestion of peptide and proteins for sequencing.
Features
- Animal free source of origin: Recombinant human trypsin expressed in E. coli. Free from contaminating proteases such as chymotrypsin and carboxypeptidase A and viruses.
- High purity: ≥ 95% ; purified by high pressure liquid chromatography
- Specific activity: ≥2500 USP u/mg
- Unit definition: One USP unit of trypsin will produce a change of absorbance 253 nm of 0.003 per minute at pH 7.6 and at temperature 25°C when the reaction volume is 3 ml and BAEE (benzoyl L-arginine ethyl ester) is used as substrate.
Applications:
- Trypsin (Human, Recombinant) can be used to make cell-dissociation reagents
- It can be used for digestion of peptide and proteins for sequencing.