|Reactivity||Human, Mouse, Rat|
|Calculated MW||44954 Da|
|Application & Usage||Western blot analysis (0.5-4 µg/ml) and in immunoprecipitation. However, the optimal conditions should be determined individually. The purified antibody detects both the 52 kDa proform and the 34 kDa cleaved fragment of Cathepsin D.|
|Other Names||CTSD , CLN10, CPSD, MGC2311|
|Formulation||100 µg (0.5 mg/ml) affinity purified rabbit anti-cathepsin D polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 30% glycerol, 0.5% BSA, 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||Cathepsin D Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation.|
|Cellular Location||Lysosome. Melanosome. Secreted, extracellular space|
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Provided below are standard protocols that you may find useful for product applications.
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 52 kDa pro-enzyme. Activation involves the proteolytic removal of the 43 amino acid profragment and an internal cleavage to generate the two-chain form made up of 34 and 14 kDa 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 52 kDa precursor form. Numerous clinical studies as well as in vitro evidence s µggest that cathepsin D plays an important role in malignant transformation and may be a useful prognostic indicator for breast cancer.
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