Cathepsin D (CTSD) antibody
|Synonyms||CPSD, CLN10, MGC2311, CD, CatD, catD, fb93e11, fj17b09, wu:fb93e11, wu:fj17b09, CTSD, LOC398557, Cathd, LOC100136761, DKFZp469J0315|
Alternatives Western Blotting (WB)
|4 references available|
|Quantity||50 µg (250 µg/ml) (Variants)|
|Price||Product not available in this region.|
|Alternative name||Cathepsin D|
|Immunogen||Human Cathespin D|
|Description||Cathepsin D, an enzyme that degrades proteins, was originally cloned during the search of estrogen responsive genes in MCF-7 cells. Cathepsin D is synthesized as the 43kDa preprocathepsin D that is cleaved to form a 46kDa glycosylated procathepsin D. Procathepsin is then processed into a 44kDa active Cathepsin D. The active and mature forms undergo a further cleavage that yields 28kDa and 15kDa (heavy and light chains, respectively) fragments in SDS-PAGE. The heavy and light chains of Cathepsin D are released into the extracellular medium. The maturation process of Cathepsin D occurs through the transit from the endoplasmic reticulum, Golgi apparatus, and to the lysosomes. Estrogens stimulate cell proliferation in a number of tumor cell lines and anti-estrogen therapy is often used in the treatment of breast cancer patients. Therefore, Cathepsin D, which is estrogen inducible, may have a role during the pathogenesis of breast tumors. Additionally, several other roles have been proposed for this enzyme, such as tissue remodeling, tumor invasion, and embryo implantation.|
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
|Molecular Weight||43/28 kDa|
Related Products: ABIN968587, ABIN967389
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution containing BSA, glycerol.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at -20°C.|
|Research Area||Proteolysis / Ubiquitin, Extracellular Matrix, Proteases, Signaling|
|Restrictions||For Research Use only|
|Western blot analysis of Cathespin D on HepG2 cell lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000, dilution of anti-Cathespin D antibody.|
Westley, May: "Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive human breast cancer cells." in: Nucleic acids research, Vol. 15, Issue 9, pp. 3773-86, 1987 (PubMed).
Faust, Kornfeld, Chirgwin: "Cloning and sequence analysis of cDNA for human cathepsin D." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 82, Issue 15, pp. 4910-4, 1985 (PubMed).
Erickson, Conner, Blobel: "Biosynthesis of a lysosomal enzyme. Partial structure of two transient and functionally distinct NH2-terminal sequences in cathepsin D." in: The Journal of biological chemistry, Vol. 256, Issue 21, pp. 11224-31, 1981 (PubMed).
Kageyama, Takahashi: "A cathepsin D-like acid proteinase from human gastric mucosa. Purification and characterization." in: Journal of biochemistry, Vol. 87, Issue 3, pp. 725-35, 1980 (PubMed).