Cathepsin B, Human Liver

Research area: Cell Signaling

Cathepsin B, Human Liver, is a native cathepsin B from human liver, purified by affinity chromatography. Cathepsin B is a lysosomal protease with endo/exopeptidase and a carboxydipeptidase activity. It is also known as cysteine cathepsin and belongs to the C1 family of papain-like enzymes. Cathepsin B like H, L, C, X, F, O and V is ubiquitously expressed in human tissues.

Optimal pH: 3.5-6.0.

Cathepsin B, Human Liver has been used to assess its linker cleavage or proteolytic activity using an LC/MS MRM-based quantitation method.

Cathepsin B facilitates non-specific, bulk proteolysis within the acidic conditions of the endosomal/lysosomal compartment. Here, they break down both intracellular and extracellular proteins. Upregulation and secretion of cathepsin B have been shown to occur in many types of tumors and to correlate positively with their invasive and metastatic capabilities. Cathepsin B is shown to facilitate tumor invasion by dissolving extracellular barriers.

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 Z-RR-βNA per min at 40°C, pH 6.0 in the presence of DTT.

In 50 mM sodium acetate buffer, 1 mM EDTA, pH 5.0.

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).

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