Chymotrypsin C Protein (His Tag) (recombinant human)

Activity: Measured by its ability to cleave the fluorogenic peptide substrate, SUC­Ala­Ala­Pro­Phe­AMC.The specific activity is >300 pmol/min/µg. Protein Construction: A DNA sequence encoding the human CTRC (Q99895) (Met 1-Leu 268) was fused with a polyhistidine tag at the C-terminus. Sequence: Met 1-Leu 268. Fusion tag: C-His Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method. Apparent Molecular Mass: 36 kDa. Protein function: Chymotrypsin C (abbreviated for CTRC), also known as caldecrin or elastase4, is a digestive enzyme of the peptidase S1 family. This enzyme is synthesized as an inactivate chymotrypsinogen. On cleavage by trypsin into two parts that activate each other by removing two small peptides in a trans-proteolysis, chymotrypsin C produced. N-linked glycosylation of human CTRC is required for efficient folding and secretion, however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding. It has been proposed that CTRC is a key regulator of digestive zymogen activation and a physiological co-activator of digestive carboxypeptidases proCPA1 and proCPA2. Mutations that abolish activity or secretion of CTRC increase the risk for chronic pancreatitis. It's speculated that CTRC might regulate pancreatic cancer cell migration in relation to cytokeratin 18 expression. The pancreatic cancer cell migration ability was downregulated in pancreatic cancer Aspc-1 cells that overexpressed CTRC, whereas the cell Protein function: Regulates activation and degradation of trypsinogens and procarboxypeptidases by targeting specific cleavage sites within their zymogen precursors. Has chymotrypsin-type protease activity and hypocalcemic activity. [The UniProt Consortium]