EMS0006

Trypsin Protease

Hydrolyzes peptide bonds at the carboxyl side of arginine and lysine residues, suitable for mass spectrometry, recombinant, expressed in Pichia pastoris

• Synonym(s): Mass Spectrometry Trypsin, Proteomics grade Trypsin, rTrypsin
• UNSPSC Code: 12352204
• NACRES: NA.26
• Specific activity: ≥10,000 units/mg protein
• Recombinant: expressed in Pichia pastoris

Properties

• Product Name: Recombinant Trypsin, Proteomics Grade, lyophilized powder, recombinant, expressed in Pichia pastoris
• recombinant: expressed in Pichia pastoris
• Quality Segment: 200
• grade: Proteomics Grade
• form: lyophilized powder
• specific activity: ≥10,000 units/mg protein
• technique(s): protein mass spectrometry: suitable
• suitability: suitable for , suitable for mass spectrometry
• UniProt accession no.: P00761
• shipped in: wet ice
• storage temp.: 2-8°C

Description

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 Information

• Pictograms: GHS08,GHS05,GHS07,GHS09
• Signal Word: Danger
• Hazard Codes: H290,H314,H317,H334,H335,H411
• Precautionary Statements: P260 - P273 - P280 - P303 + P361 + P353 - P304 + P340 + P310 - P305 + P351 + P338
• 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: EUH071
• Storage Class: 8A - Combustible corrosive hazardous materials
• WGK: WGK 3
• Flash Point (°F): Not applicable
• Flash Point (°C): Not applicable