Description
General description
Research area: Cell signaling
Native Cathepsin H, from the human liver, is the only cathepsin with mono-aminopeptidase activity.
Application
Cathepsin H has been used to determine the potential of aziridinyl peptides to act as inhibitors of this protein and potentially explore their therapeutic applications.
Biochem/physiol Actions
Cathepsin H, derived from human liver, serves dual functions as both an aminopeptidase and an endopeptidase. It plays a significant role in the catabolism of proteins within lysosomes. Cathepsin H is classified as an endoaminopeptidase because it can hydrolyze proteins, N-terminal substituted proteins, amino acid derivatives, and peptides with different chain lengths and N-terminal free amino acid derivatives. This protein is also observed to exhibit amidase and esterase activity.
Packaging
Please refer to vial label for lot-specific concentration.
Physical form
In 100 mM NaCl, 20 mM sodium acetate buffer, 1 mM EDTA, pH 4.5.
Preparation Note
Following initial thaw, aliquot and freeze (-70°C).
Prepared from tissue of individuals that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Other Notes
Note: 1 mU = 1 milliunit.
One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol H-Arg-βNA per min at 40°C, pH 6.8.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)