Cathepsin D from bovine spleen

Research area: Cell Signaling

Cathepsin D is a soluble endosomal-lysosomal aspartic protease and is synthesized in the rough endoplasmic reticulum as preprocathepsin D. It is encoded by the CTSD gene located in the 11p15.5 region.

Cathepsin D from bovine spleen has been used:

• in in vitro dose-dependent fluorometric activity assays.
• in in vitro myelin oligodendrocyte glycoprotein (MOG) digestion to study the uptake of malondialdehyde (MDA)-modified MOG and its implications in central nervous system autoimmunity.
• for enzymatic digestion of the proteoglycan moiety of the articular cartilage in order to determine its dynamic elastic modulus at two different levels of tissue organization.
• in cathepsin D activity assay.

Cathepsin D is an endosomal-lysosomal aspartic protease implicated in breast cancer metastasis and Alzheimer′s disease. Lysosomal release of cathepsin D has been found to precede cytochrome c release and loss of membrane potential in apoptotic human foreskin fibroblasts. Cathepsin D levels in PC12 cells increase 12 to 24 hours after apoptosis is induced.

Endosomal-lysosomal aspartic protease implicated in breast cancer metastasis and Alzheimer′s disease. Lysosomal release of cathepsin D has been found to precede cytochrome c release and loss of membrane potential in apoptotic human foreskin fibroblasts.

Lyophilized powder containing citrate buffer salts

One unit will produce an increase in A₂₈₀ of 1.0 per min per mL at pH 3.0 at 37 °C measured as TCA-soluble products using hemoglobin as substrate (1 cm light path).