Trypsin from bovine pancreas(Modified,Sequencing Grade) - ≥150 units/mg protein(at least 8,625 BAEE/2875 USP/NF units/mg protein), high purity , CAS No.9002-07-7
Trypsin from bovine pancreas(Modified,Sequencing Grade) - ≥150 units/mg protein(at least 8,625 BAEE/2875 USP/NF units/mg protein), high purity , CAS No.9002-07-7
EnzymoPure™
≥150 units/mg protein(at least 8,625 BAEE/2875 USP/NF units/mg protein)
≥150 units/mg protein(at least 8,625 BAEE/2875 USP/NF units/mg protein)
Biochemical and Physiological Mechanisms
Trypsin cleaves peptide chains, amides and esters mainly at the carboxyl side of the amino acids lysine or arginine. Trypsin originates in the pancreas in the form of the zymogen trypsinogen.
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: P00760 CATH Classification (v. 3.2.0): Class: Mainly Beta Architecture: Beta Barrel Topology: Thrombin, subunit H Molecular 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) DFP Aprotinin Ag+ Benzamidine EDTA (White and White 1997) Applications: Tissue dissociation, especially when combined with other enzymes such as collagenase, and elastase Cell harvesting by “trypsinization” Mitochondria isolation in vitro studies of proteins Removing monolayers of cells from plastic and glass Various hemagglutination procedures Sample preparation for flow cytometric DNA analysis Tryptic mapping Fingerprinting and sequencing work Environmental monitoring Reduction of cell density in tissue culture Subculturing cells Cleavage fusion proteins Generating glycopeptides from purified glycoproteins (White and White 1997)
Names and Identifiers
Enzyme Commission Number
3.4.21.4
WGK Germany
1
RTECS
YN5075000
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