Package: Aluminum Foil Bag

Uses : Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues.

Product description: Sequencing Grade Trypsin Animal Origin Free CAS: 9002-07-7 EC: 3.4.21.4 SOURCE Expressed in E.Coli, purified by HPLC. DESCRIPTION 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 Trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There is no trace of contaminating enzyme activities such as carboxypeptidases and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparations. MAIN FEATURES Source E.Coli Purified by HPLC Physical form White or white-like lyophilized powder Specific activity NLT 4500 USP units/mg pro. No Contaminant activity No chymotrypsin, carboxypeptidase A, or other proteases contaminant. APPLICATION Protein digests for peptide mapping applications or protein identification by peptide mass fingerprinting or MS/MS spectral matching. It is suitable for digestion reactions in-solution or in-gel. RECOMMEND USAGE To prepare 1-10mg/ml with 1ml 1mM HCl, used within 2 days, or stored below -20℃ after repacked STORAGE AND STABILITY Recommend recombinant trypsin lyophilized powder stored under 2-8℃ in sealed container. It is stable within 24 months. After dissolved, it should be stored under -20℃, no activity lose after 10 times repeated freezing and thawing.