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Monoclonal Anti-Cathepsin D antibody produced in mouse

SIGMA/C0715 - clone CTD-19, ascites fluid

Synonym: Anti-CLN10; Anti-CPSD; Anti-HEL-S-130P

MDL Number: MFCD00162216
Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-C0715-.5ML 0.5 mL
$761.00
1/EA
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Immunohistochemistry Formalin-fixed, paraffin-embedded tissue section of human breast carcinoma stained with 1:200 Monoclonal Anti-Cathepsin D antibody produced in Mouse clone CTD-19 (Cat. No. C0715) followed by Anti-Mouse IgG (Fab specific)-Biotin antibody produced in Goat (Cat. No. B7151) and by ExtrAvidin®-Peroxidase (Cat. No. E2886).
Immunofluorescence HeLa cells were fixed and permeabilized with methanol followed by methanol:acetone. Fixed cells were stained with 1:500 Monoclonal Anti-Cathepsin D, Clone: CTD-19 (Cat. No. C0715). The antibody was developed using Goat Anti-Mouse IgG, ATTO488 conjugate. Cells were counterstained with DAPI (blue) to stain nuclei.
Immunoblotting MCF7 Human breast carcinoma cells were separated on SDS-PAGE and probed with Monoclonal AB to Cathepsin D (MO) CL:CTD-19 (Prepack) (Cat. No. C0715). The antibody was developed with AlkPhos APA mouse Fab ads HIgG conjugate (Cat. No. A1293) and a NBT/BCIP substrate. Antibody dilution 1/4,000

 

antibody form ascites fluid
antibody product type primary antibodies
biological source mouse
clone CTD-19, monoclonal
conjugate unconjugated
isotype IgG2a
mol wt antigen 34 kDa
  antigen 52 kDa (weaker band)
Quality Level 200 
shipped in dry ice
species reactivity human
storage temp. −20°C
target post-translational modification unmodified
technique(s) 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
UniProt accession no. P07339 
Application: 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) 
Application: 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.
Biochem/physiol Actions: 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.
Disclaimer: 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.
General description: 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.
Immunogen: human liver cathepsin D.
Other Notes: 2024 CiteAb Award Winner for Supplier Succeeding in Parkinson′s Research 
WGK Germany WGK 3
Storage Temp. −20°C
UNSPSC 12352203

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