Product Name

Cathepsin C from bovine spleen

Synonym

Dipeptidyl aminopeptidase, Dipeptidyl peptidase I

CAS Number

9032-68-2

MDL number

MFCD00081490

Suitability

BioReagent

l Physical and Chemical Information

Appearance

lyophilized powder

Physical form

Lyophilized from a 1 M sodium chloride solution.

l Biological Information

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.

Application

Cathepsin C has been used in a study that demonstrated the potential of a proteomics approach to identify novel proteins expressed by extravillous trophoblast and to uncover the mechanisms leading to disease states in pregnancy. Cathepsin C has also been used in a study to evaluate biodegradable thermogels.

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.

Caution

Unstable. Keep frozen.

Unit Definition

One unit will produce 1 μmole of Gly-Phe-NHOH from Gly-Phe-NH² and hydroxylamine per min at pH 6.8 at 37 °C using DL-phenylalanine hydroxamic acid as the standard. In addition to its hydrolytic properties, cathepsin C catalyzes the polymerization of dipeptide amides.

l Storage

Storage temp.

-20°C

l Precautions and Disclaimer

This product is for R&D use only, not for drug, household, or other uses.

l References

1. http://www.drugbank.ca

2. https://ncit.nci.nih.gov

3. https://www.ncbi.nlm.nih.gov