EMS0006
Recombinant Trypsin
Proteomics Grade, lyophilized powder, recombinant, expressed in Pichia pastoris
Synonym(s):
Mass Spectrometry Trypsin, Proteomics grade Trypsin, rTrypsin
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.26
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General description
Trypsin is a major proteolytic enzyme, synthesized as a preproenzyme by pancreas and is stored as proenzyme trypsinogen in secretory granules.[1] Trypsin belongs to the family of serine proteases that are characterized by the catalytic triad His57, Asp102 and Ser195.[2] 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.[3] 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.[1]
signalword
Danger
Hazard Classifications
Aquatic Chronic 2 - Eye Dam. 1 - Met. Corr. 1 - Resp. Sens. 1 - Skin Corr. 1A - Skin Sens. 1 - STOT SE 3
target_organs
Respiratory system
supp_hazards
Storage Class
8A - Combustible corrosive hazardous materials
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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