9032-68-2

Basic information

• Product Name: EC 3.4.14.1
• Synonyms: DIPEPTIDYLPEPTIDE HYDROLASE;DIPEPTIDYL AMINOPEPTIDASE;DIPEPTIDYL PEPTIDASE I;EC 3.4.14.1;CATHEPSIN C;CATHEPSIN C, BOVINE;CATHEPSIN C TYPE X;cathepsin C type X: from bovine spleen
• CAS NO: 9032-68-2
• Molecular Weight: 0
• EINECS: 232-881-4
• Mol File: 9032-68-2.mol
• Article Data: 0

Chemical Properties

• Appearance: /
• Storage Temp.: −20°C
• CAS DataBase Reference: EC 3.4.14.1(CAS DataBase Reference)
• NIST Chemistry Reference: EC 3.4.14.1(9032-68-2)
• EPA Substance Registry System: EC 3.4.14.1(9032-68-2)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 9032-68-2(Hazardous Substances Data)

Usage

Description

EC 3.4.14.1 is an enzyme that plays a crucial role in the activation of granzyme K (Gzmk) precursor from E. coli. Granzymes are granule-stored lymphocyte serine proteases that are involved in Tand natural killer cell-mediated cytotoxic defense reactions. This enzyme is essential for the proper functioning of the immune system and has potential applications in various fields.

Uses

Used in Pharmaceutical Industry:
EC 3.4.14.1 is used as a therapeutic agent for enhancing the immune response against infections and diseases. Its role in activating granzyme K precursor makes it a promising candidate for the development of new drugs and therapies to boost the immune system and combat various health conditions.
Used in Research and Development:
EC 3.4.14.1 is used as a research tool for studying the mechanisms of Tand natural killer cell-mediated cytotoxic defense reactions. Understanding the role of this enzyme in the immune system can help scientists develop new strategies for treating diseases and improving overall health.
Used in Diagnostics:
EC 3.4.14.1 can be used as a diagnostic marker to assess the immune system's functionality and identify potential deficiencies or abnormalities. This can help in early detection of diseases and the development of personalized treatment plans for patients.

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.