|Application ||WB, IHC|
|Calculated MW||44552 Da|
|Other Names||Cathepsin D, Cathepsin D light chain, Cathepsin D heavy chain, CTSD, CPSD|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus of human Cathepsin D was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|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. 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).|
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Provided below are standard protocols that you may find useful for product applications.
Cathepsin D is a ubiquitously expressed lysosomal protease that is involved in proteolytic degradation, cell invasion, and apoptosis (1). It is suspected to play important roles in protein catabolism, antigen processing, degenerative diseases, and breast cancer progression (2). Cathepsin D is induced by estrogens in mammary cancer cells where its concentration is correlated with a higher risk of metastasis (3). It is possibly involved in Alzheimer's disease-related neurodegeneration through cleavage of amyloid precursor protein into amyloidogenic components (4). Preprocathepsin D (43 kDa) is cleaved and glycosylated to form procathepsin D (46 kDa), and then further cleaved, forming light and a heavy chains (15 kDa and 28 kDa, respectively) (5).
1. Steinfeld R, et al. Am J Hum Genet. 78(6):988-98, 2006
2. Baldwin ET, et al. Proc Natl Acad Sci U S A. 90(14):6796-800, 1993
3. Augereau P, et al. Mol Endocrinol. 8(6):693-703, 1994
4. Papassotiropoulos A, et al. Ann Neurol. 47(3):399-403,2000
5. Shewale JG, et al. PNAS 81(12): 3703-3707, 1984-06
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