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EMS0006 Sigma-Aldrich

Recombinant Trypsin

Proteomics Grade, lyophilized powder, recombinant, expressed in Pichia pastoris

Synonym: Mass Spectrometry Trypsin

  •  NACRES NA.26



General description

Trypsin is a major proteolytic enzyme, synthesized as a preproenzyme by pancreas and is stored as proenzyme trypsinogen in secretory granules. Trypsin belongs to the family of serine proteases that are characterized by the catalytic triad His57, Asp102 and Ser195. Trypsin is routinely used in proteomics research for peptide mapping and protein sequence work due to its highly specific cleavage resulting in a limited number of tryptic peptides. Trypsin is a pancreatic serine endoprotease which hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues. The rate of hydrolysis is slower if an acidic residue is on either side of the cleavage site and cleavage may not occur if a proline residue is on the carboxyl side. The enzyme also exhibits esterase and amidase activities. Trypsin has an average molecular mass of 23.29 kDa and a pH optimum near 8.0. This product is prepared from recombinant trypsin, porcine sequence. It is naturally devoid of chymotryptic activity. This high-quality trypsin is suitable for proteomics use.

Biochem/physiol Actions

Trypsin plays an important role in the digestion of consumed protein and contributes to the activation of other proteolytic enzymes like chemotrypsin and elastase.

Safety & Documentation

Safety Information

Signal word 
Hazard statements 
Target organs 
Respiratory system
UN 1789 8 / PGIII
WGK Germany 
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable


Certificate of Analysis (COA)

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