Cathepsin H, Human Liver

Research area: Cell signaling

Native Cathepsin H, from the human liver, is the only cathepsin with mono-aminopeptidase activity.

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.

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.

Please refer to vial label for lot-specific concentration.

Toxicity: Standard Handling (A)

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.

In 100 mM NaCl, 20 mM sodium acetate buffer, 1 mM EDTA, pH 4.5.

Prepared from tissue of individuals that have been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Following initial thaw, aliquot and freeze (-70°C).

Note: 1 mU = 1 milliunit.

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