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Anti-Cathepsin D antibody, Mouse monoclonal

clone CTD-19, purified from hybridoma cell culture

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Anti-CTSD, cleaved into the following 2 chains: Cathepsin D light chain and Cathepsin D heavy chain

biological source


Quality Level

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies


CTD-19, monoclonal


buffered aqueous solution

species reactivity

human, rabbit


~1.0 mg/mL


immunoblotting: 2-4 μg/mL using human breast cancer MCF7 cell line
immunofluorescence: 5-10 μg/mL using HeLa cells
immunohistochemistry: 10-20 μg/mL using heat-retrieved formalin-fixed, paraffin-embedded human liver sections



UniProt accession no.

shipped in

dry ice

storage temp.


target post-translational modification


Gene Information

human ... CTSD(1509)

Related Categories

General description

Anti-Cathepsin D antibody, Mouse monoclonal (mouse IgG2a isotype) is derived from the CTD-19 hybridoma, produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mouse immunized with cathepsin D purified from human liver. Cathepsin D (CatD or CTSD) is synthesized in the rough endoplasmic reticulum as pre-proprotein. After removal of signal peptide, the pro-CatD is targeted to endosomes to form an active, ~48 kDa, single-chain intermediate then to the lysosomes to form the fully active mature protease, composed of a ~30 kDa heavy chain and a ~14 kDa light chain.


Cathepsin D Purified from human liver


Anti-Cathepsin D antibody, Mouse monoclonal has been used in:
  • immunoblotting
  • immunohistochemistry
  • immunofluorescence

Biochem/physiol Actions

CatD plays numerous physiological functions in the cells including metabolic degradation of intracellular proteins and the activation of enzymatic precursors. In the central nervous system, CatD is particularly important for the control of neuronal homeostasis, cell migration and interneuron communication. CatD-mediated proteolysis mediates the degradation of unfolded/oxidized protein aggregates in lysosome. The level of CatD synthesized by the cells is increased in response to mitogenic signals from estrogen, epidermal growth factor (EGF), fibroblast growth factor (FGF), and insulin like growth factor-I (IGF- I). The ability of tumor cells to invade the extracellular matrix has been attributed to cathepsins released by tumor cells or associated with its plasma membrane.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage Class

10 - Combustible liquids


Not applicable


Not applicable

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Cathepsin D as a therapeutic target in Alzheimer's disease.
Di Domenico F, et al.
Expert Opinion on Therapeutic Targets, 20(12), 1393-1395 (2016)
The role of cathepsin D in the pathogenesis of human neurodegenerative disorders
Vidoni C, et al.
Medicinal Research Reviews, 36(5), 845-870 (2016)
Veronika Stoka et al.
Ageing research reviews, 32, 22-37 (2016-04-30)
Lysosomes and lysosomal hydrolases, including the cathepsins, have been shown to change their properties with aging brain a long time ago, although their function was not really understood. The first biochemical and clinical studies were followed by a major expansion
Nuclear cathepsin D enhances TRPS1 transcriptional repressor function to regulate cell cycle progression and transformation in human breast cancer cells
Bach AS, et al.
Oncotarget, 6(29), 28084-28084 (2015)
Clivia Lisowski et al.
Autophagy, 18(8), 1785-1800 (2021-11-17)
Modulation of the host cell cycle has emerged as a common theme among the pathways regulated by bacterial pathogens, arguably to promote host cell colonization. However, in most cases the exact benefit ensuing from such interference to the infection process

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