Recombinant chymotrypsin is a serine endopeptidase that is expressed in E. Coli expression system and purified by HPL. Its amino acid sequence is the same as that of human chymotrypsin. Recombinant chymotrypsin can selectively hydrolyze the peptide bonds formed by the C-terminus of aromatic amino acids such as tyrosine, phenylalanine and tryptophan. It can also hydrolyze the peptide bonds formed by leucine and methionine at a slower rate., Can also act on esters formed by sensitive amino acids. the optimum pH of chymotrypsin is 7.0--9.0. Recombinant production, no foreign virus contamination, such as swine flu virus, porcine parvovirus, etc. No contamination by other miscellaneous enzymes: No other side reactions in the digestion reaction. Freeze-dried powder, easy to store and transport; mass production, stable product quality. Used alone, or together with other  to digest protein, or other special purposes, such as organic synthesis, etc.

Product advantages
No animal origin: recombinant production, no foreign virus contamination, such as swine flu virus, porcine parvovirus, etc.
High purity: no other miscellaneous enzyme pollution: no other side reactions in the digestion reaction
High specific activity: not less than 1000 u/mg pro.
Stable: freeze-dried powder, easy to store and transport; mass production, stable product quality
Product Features
Recombinant chymotrypsin can selectively hydrolyze the peptide bonds formed by the C-terminus of aromatic amino acids such as tyrosine, phenylalanine and tryptophan. the peptide bond formed by leucine and methionine can also be hydrolyzed slowly at a slower rate. It can also act on esters formed by sensitive amino acids.
Product Usage
1. Used alone or together with other  to digest proteins for peptide mapping, peptide fingerprinting or protein sequence analysis.
2. for the digestion of protein or peptide, the recommended ratio is 1:60 (mass ratio, chymotrypsin: protein), and the recommended solution is: 100mM Tris-HCl, 10mM CaCl2 pH7.8, 30C, temperature higher than 37°C may cause the enzyme itself to undergo self-degradation. A known peptide such as melittin can be used as an experimental control.
Purification:HPL
Product status:
White or almost white freeze-dried powder
Activity:  ≥1000 unit/mg pro
Purity:> 95%