|Other Names||Cathepsin D, Cathepsin D light chain, Cathepsin D heavy chain, CTSD, CPSD|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. 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 (PubMed:27333034). Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.|
|Cellular Location||Lysosome. Melanosome. Secreted, extracellular space. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. In aortic samples, detected as an extracellular protein loosely bound to the matrix (PubMed:20551380).|
|Tissue Location||Expressed in the aorta extrcellular space (at protein level) (PubMed:20551380). Expressed in liver (at protein level) (PubMed:1426530).|
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Provided below are standard protocols that you may find useful for product applications.
CTSD is a lysosomal aspartyl protease composedof a dimer of disulfide-linked heavy and light chains, bothproduced from a single protein precursor. This proteinase, which isa member of the peptidase C1 family, has a specificity similar tobut narrower than that of pepsin A. Transcription of this gene isinitiated from several sites, including one which is a start sitefor an estrogen-regulated transcript. Mutations in this gene areinvolved in the pathogenesis of several diseases, including breastcancer and possibly Alzheimer disease.
Fujita, H., et al. Biochem. Biophys. Res. Commun. 179(1):190-196(1991)Faust, P.L., et al. Proc. Natl. Acad. Sci. U.S.A. 82(15):4910-4914(1985)Knight, C.G., et al. Biochem. J. 155(1):117-125(1976)
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