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Description
Purified anti-Cathepsin D. Cathepsin D (CTSD) is a major lysosomal aspartic endoproteinase. It is active in acidic conditions with a pH range from 3.5 to 5.0, and its activity is inhibited by pepstatin A. CTSD is involved in lysosomal protein turnover and many other cellular processes. CTSD participates in the resolution of inflammation by initiating the apoptotic program in neutrophils. CTSD is released from neutrophil azurophilic granules during the initial stage of apoptosis, which leads to death receptor-independent activation of caspase-8. CTSD induces apoptosis in other cells as well. In T cells, CTSD activates Bax, which leads to the release of mitochondrial apoptosis-inducing factor (AIF), and subsequently induces an early caspase-independent apoptotic phenotype. CTSD also takes part in the release of cytochrome C from the mitochondria and activation of caspases in fibroblast apoptosis, which is induced by staurosporine. In addition, CTSD participates in cell proliferation, and it also increases proliferation and metastatic potential of many cancer cell lines. Overexpression of CTSD has been reported in many different cancers including malignant glioma, melanoma, breast, ovarian, endometrial, and bladder cancer. CTSD is also involved in neurodegenerative diseases. CTSD knockout mice die shortly after birth and display some neurodegeneration phenotypes. Mutations of CTSD cause congenital neuronal ceroid lipofuscinosis in humans and animals. CTSD cleaves the amyloid precursor protein and may play a role in Alzheimer’s disease. CTSD-deficiency has also been associated with Parkinson disease. Like CTSB and CTSL, CTSD functions outside the cells and is able to cleave extracellular matrix proteins including collagen, fibronectin, proteoglycans, and laminin.
Immunogen
Partial human cathepsin D recombinant protein (21-412 a.a.) expressed in 293E cells.