Chymotrypsin from human pancreas
SIGMA/SRP6509 - ≥95% (SDS-PAGE)
Synonym: CLCR; CTRC; CTRC_HUMAN; Caldecrin; Chymotrypsin C; Chymotrypsin-C; ELA 4; Elastase 4; Elastase IV; Serum calcium decreasing factor
EC Number: 232-671-2
Product Type: Chemical
assay | ≥95% (SDS-PAGE) |
biological source | human |
form | lyophilized |
mol wt | 25 kDa |
packaging | pkg of 100 μg |
shipped in | wet ice |
storage temp. | −20°C |
UniProt accession no. | Q99895 |
Biochem/physiol Actions: | Chymotrypsin from human pancreas selectively hydrolyzes peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan and leucine. Loss-of-function mutations in this gene have been associated with increased risk of chronic pancreatitis. It has high activity toward leucyl peptide bonds. The enzyme acts as a co-activator of procarboxypeptidases A1 and A2. |
General description: | Chymotrypsin from human pancreas is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. It is secreted by the pancreas as inactive chymotrypsinogen C. Molecular weight of this enzyme is found to be 25kDa. The pI is 8.75. |
Physical form: | Lyophilized as a salt-free solid. |
Symbol | GHS07,GHS08 |
Signal word | Danger |
Hazard statements | H315 - H319 - H334 - H335 |
Precautionary statements | P261 - P280 - P284 - P304 + P340 + P312 - P337 + P313 - P342 + P311 |
RIDADR | NONH for all modes of transport |
WGK Germany | WGK 1 |
Flash Point(F) | Not applicable |
Flash Point(C) | Not applicable |
Purity | ≥95% (SDS-PAGE) |
Storage Temp. | −20°C |
UNSPSC | 12352200 |