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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.
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준비 및 보관
권장 분석 절차
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml.
제품 고시
- 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.
개발 참고 자료 (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). 참조 보기
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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). 참조 보기
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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). 참조 보기
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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). 참조 보기
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