Cathepsin D is a protein that in humans is encoded by the CTSD gene. It is an estrogen-regulated, lysosomal acidic protease associated with tissue breakdown. This gene encodes a lysosomal aspartyl protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. This proteinase, which is a member of the peptidase C1 family, has a specificity similar to but narrower than that of pepsin A. Cathepsin D are indicative of breast cancer recurrence in both node-negative and node-positive diesease. Cathepsin D Antibody detects endogenous levels of preprocathepsin D, procathepsin D and the heavy chain subunit of mature cathepsin D.
Cathepsin D is isolated from human liver and is supplied as a powder, lyophilized from 2.5mM Sodium Phosphate, pH 6.5 ± 0.1.In addition, Protein is determined prior to lyophilization using the Bradford method. One unit of the enzyme will produce an increase in absorbance of 1.0 per ml per hour, measured at 280nm, pH 3.3, 37°C, using bovine hemoglobin as the substrate. The approach was based on random inactivation of genes by transfections with antisense cDNA expression libraries, followed by the selection of cells that survived in the presence of the external apoptotic stimulus.
A functional approach of gene cloning was applied to HeLa cells in an attempt to isolate positive mediators of programmed cell death. Cathepsin D is associated with amyloid formation in Alzheimer's plaques as is possibly linked to lung tissue damage in cigarette smokers. An antisense cDNA fragment identical to human cathepsin D aspartic protease was rescued by this positive selection.
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