Trypsin from bovine pancreas(Modified,Sequencing Grade) (C09-1053-856)

Specificity:Trypsin cleaves peptides on the C-terminal side of lysine and arginine amino acid residues. If a proline residue is on the carboxyl side of the cleavage site, the cleavage will not occur. If an acidic residue is on either side of the cleavage site, the rate of hydrolysis has been shown to be slower.Protein Accession Number: P00760CATH Classification (v. 3.2.0): Class: Mainly BetaArchitecture: Beta BarrelTopology: Thrombin, subunit HMolecular Weight: 23.3 kDa (Theoretical)Optimal pH: 7.5-8.5 (Koutsopoulos et al. 2007)Isoelectric Point:Trypsinogen: pH 9.3 (Walsh and Neurath 1964)Trypsin: pH 10.5 (Cunningham 1954).Extinction Coefficient: Trypsinogen: 45,250 cm-1 M-1>Active Site Residues:Histidine (H63)Aspartic acid (D107)Serine (S200)Activators: The rate of trypsinogen conversion is enhanced by using lanthanide in place of calcium ions (Gomez et al. 1974).Inhibitors:Pancreatic-, soybean-, lima bean-, and egg white- trypsin inhibitors (see section on Trypsin Inhibitors)DFPAprotininAg+BenzamidineEDTA         (White and White 1997)Applications:Tissue dissociation, especially when combined with other enzymes such as collagenase, and elastaseCell harvesting by “trypsinization”Mitochondria isolationin vitro studies of proteinsRemoving monolayers of cells from plastic and glassVarious hemagglutination proceduresSample preparation for flow cytometric DNA analysisTryptic mappingFingerprinting and sequencing workEnvironmental monitoringReduction of cell density in tissue cultureSubculturing cellsCleavage fusion proteinsGenerating glycopeptides from purified glycoproteins (White and White 1997). Specification: ≥150 units/mg protein(at least 8,625 BAEE/2875 USP/NF units/mg protein) MDL Number: MFCD00082094 EC Number: 232-650-8