C0715
Monoclonal Anti-Cathepsin D antibody produced in mouse
clone CTD-19, ascites fluid
Szinonimák:
Anti-CLN10, Anti-CPSD, Anti-HEL-S-130P
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(3)
About This Item
Javasolt termékek
biológiai forrás
mouse
Minőségi szint
konjugátum
unconjugated
antitest forma
ascites fluid
antitest terméktípus
primary antibodies
klón
CTD-19, monoclonal
molekulatömeg
antigen 34 kDa
antigen 52 kDa (weaker band)
faj reaktivitás
human
technika/technikák
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:200 using human breast carcinoma tissue
indirect ELISA: suitable
microarray: suitable
western blot: 1:1,000 using human breast carcinoma cell line extract
izotípus
IgG2a
UniProt elérési szám
kiszállítva
dry ice
tárolási hőmérséklet
−20°C
célzott transzláció utáni módosítás
unmodified
Géninformáció
human ... CTSD(1509)
Általános leírás
Cathepsins are lysosomal proteases that play an important role in the intracellular degradation of exogenous and endogenous proteins, in activation of enzyme precursors, and in tumor invasion and metastasis. They are normally localized in lysosomes of almost all mammalian cells, but under certain conditions they can be secreted from the cells.
Cathepsin D (CD, EC 3.4.23.5), an aspartyl endopeptidase, is induced by estrogen in certain estrogen receptor (ER)-positive breast cancer cell lines, but is produced constitutively by ER-negative cell lines. Cathepsin D is synthesized as a 52 kDa inactive precursor (pro-cathepsin D). Proteolytic removal of the amino-terminal 43 amino acid fragment and cleavage at an internal site results in an enzymatically active 48 kDa heterodimer consisting of two chains of 14 and 34 kDa.
The level of CD synthesized by cells is increased in response to mitogenic signals from estrogen, EGF, FGF, and IGF- I. The ability of tumor cells to invade the extracellular matrix has been attributed to cathepsins released by tumor cells or associated with the plasma membrane of tumor cells. CD is capable of digesting extracellular matrix proteins in in vivo models. Transfection of the CD gene into rat cells increases their tumorigenicity when injected into nude mice. Indeed, the concentrations of CD are significantly higher in breast carcinomas than in either normal breast tissues or benign breast tumors.
Cathepsin D (CD, EC 3.4.23.5), an aspartyl endopeptidase, is induced by estrogen in certain estrogen receptor (ER)-positive breast cancer cell lines, but is produced constitutively by ER-negative cell lines. Cathepsin D is synthesized as a 52 kDa inactive precursor (pro-cathepsin D). Proteolytic removal of the amino-terminal 43 amino acid fragment and cleavage at an internal site results in an enzymatically active 48 kDa heterodimer consisting of two chains of 14 and 34 kDa.
The level of CD synthesized by cells is increased in response to mitogenic signals from estrogen, EGF, FGF, and IGF- I. The ability of tumor cells to invade the extracellular matrix has been attributed to cathepsins released by tumor cells or associated with the plasma membrane of tumor cells. CD is capable of digesting extracellular matrix proteins in in vivo models. Transfection of the CD gene into rat cells increases their tumorigenicity when injected into nude mice. Indeed, the concentrations of CD are significantly higher in breast carcinomas than in either normal breast tissues or benign breast tumors.
Egyediség
Monoclonal Anti-Cathepsin D reacts specifically with cathepsin D (34 kDa with a weaker band at 52 kDa) in immunoblotting. It is also reactive in ELISA and in immunohistochemical staining of formalin-fixed paraffin-embedded human tissue sections. The product does not react with bovine cathepsins D and B, nor with human cathepsins B, C, G, and H.
Immunogen
human liver cathepsin D.
Alkalmazás
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Western Blotting (1 paper)
Immunohistochemistry (1 paper)
Western Blotting (1 paper)
Monoclonal Anti-Cathepsin D may be used for the localization of cathepsin D using various immunochemical assays such as ELISA, immunoblotting, and immunohistochemistry. Antibodies that react specifically with cathepsin D may be used to study the distribution of CD in human breast cancers and to relate its concentrations to various biochemical, histological, and clinical characteristics.
Egyéb megjegyzések
Jogi nyilatkozat
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Tárolási osztály kódja
10 - Combustible liquids
WGK
WGK 3
Analitikai tanúsítványok (COA)
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