Cathepsin D is a normal lysosomal protease that is expressed in all cells. It is an aspartyl protease with a pH optimum in the range of 3-5, and contains two N-linked oligosaccharides. Cathepsin D is synthesized as an inactive 52kD pro enzyme. Activation involves the proteolytic removal of the 43aa profragment and an internal cleavage to generate the two-chain form made up of 34 and 14kD subunits. Cathepsin D contains the mannose-6-phosphate lysosomal localization signal that targets the enzyme to the lysosomal compartment where it functions in the normal degradation of proteins. In certain tumor cells, Cathepsin D is abnormally processed and is secreted in its 52kD precursor form. Numerous clinical studies as well as in vitro evidence suggest that cathepsin D plays an important role in malignant transformation and may be a useful prognostic indicator for breast cancer and possibly Alzheimer's disease.
Application:
Suitable for use in Western Blot, Immunoprecipitation, and Immunohistochemistry. Other applications not tested.
Recommended Dilution:
Western Blot: 0.5-1ug/ml
Immunohistochemistry (paraffin): 1-2ug/ml
Optimal dilutions to be determined by the researcher.
Storage and Stability:
Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile dH20. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
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