ChemicalBook--->CAS DataBase List--->9032-68-2

9032-68-2

9032-68-2 Structure

9032-68-2 Structure
IdentificationBack Directory
[Name]

EC 3.4.14.1
[CAS]

9032-68-2
[Synonyms]

DPP1
EC 3.4.14.1
CATHEPSIN C
E.C. 3.4.4.9
CATHEPSIN C TYPE X
CATHEPSIN C, BOVINE
Dipeptidyl transferase
DIPEPTIDYL PEPTIDASE I
Dipeptide arylamidase I
DIPEPTIDYL AMINOPEPTIDASE
Native Bovine Cathepsin C
DIPEPTIDYLPEPTIDE HYDROLASE
cathepsin c from bovine spleen
cathepsin C type X: from bovine spleen
CATHEPSIN C, SOLUTION, FROM BOVINE SPLEEN
Dipeptidyl aminopeptidase, Dipeptidyl peptidaseI
[EINECS(EC#)]

232-881-4
[MDL Number]

MFCD00081490
Chemical PropertiesBack Directory
[storage temp. ]

-20°C
[form ]

lyophilized powder
Safety DataBack Directory
[WGK Germany ]

3
Hazard InformationBack Directory
[Uses]

The enzyme from Sigma has been used in the activation of granzyme k (Gzmk) precursor from E. coli. Granzymes are granule-stored lymphocyte serine proteases that are implicated in T- and natural killer cell-mediated cytotoxic defense reactions.
[Biochem/physiol Actions]

Cathespin C is a dipeptidyl aminopeptidase that can sequentially remove dipeptides from a peptide chain with an unsubstituted N-terminus. The enzyme exhibits a preference for glycine and proline as N-terminal aminoacids. Substrates that have an N-terminal lysyl or arginyl residue, or a penultimate proryl residue are not targeted by this enzyme. The endopeptidase activity requires the presence of halide ions and sulfydryl activators.
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