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BD Transduction Laboratories™ Purified Mouse Anti-Cathepsin D
Clone 49/Cathepsin D (RUO)




Western blot analysis of Cathepsin D on HepG2 cell lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000, dilution of anti-Cathepsin D.


ImageTitle~BD Transduction Laboratories™ Purified Mouse Anti-Cathepsin D

Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml.
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Cathepsin D, an enzyme that degrades proteins, was originally cloned during the search for 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 44kDa active Cathepsin D. The active and mature form undergoes 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, to the lysosomes. Estrogen stimulates 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.
Development References (4)
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Erickson AH, Conner GE, Blobel G. Biosynthesis of a lysosomal enzyme. Partial structure of two transient and functionally distinct NH2-terminal sequences in cathepsin D. J Biol Chem. 1981; 256(21):11224-11231. (Biology). View Reference
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Faust PL, Kornfeld S, Chirgwin JM. Cloning and sequence analysis of cDNA for human cathepsin D. Proc Natl Acad Sci U S A. 1985; 82(15):4910-4914. (Biology). View Reference
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Kageyama T, Takahashi K. A cathepsin D-like acid proteinase from human gastric mucosa. Purification and characterization. J Biochem (Tokyo). 1980; 87(3):725-735. (Biology). View Reference
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Westley BR, May FE. Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive human breast cancer cells. Nucleic Acids Res. 1987; 15(9):3773-3786. (Biology). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.