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AB126779

Cathepsin D Inhibitor Assay Kit

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(1 Publication)

Cathepsin D Inhibitor Screening Kit (ab126779) is a fluorescence-based assay that uses the preferred cathepsin D substrate sequence GKPILFFRLK(Dnp)-D-R-NH2) labeled with MCA.

View Alternative Names

CPSD, CTSD, Cathepsin D

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Functional Studies - Cathepsin D Inhibitor Assay Kit (AB126779)
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Supplier Data

Functional Studies - Cathepsin D Inhibitor Assay Kit (AB126779)

Typical Pepstatin A Inhibition Profile of Cathepsin D Activity. The red line denotes an IC50 value of 0.067 nM. Results were analyzed by fluorescence plate reader according to the kit instructions.

Key facts

Detection method

Fluorescent

Sample types

Inhibitor compounds

Results type

Quantitative

Assay time

1h

Assay Platform

Microplate reader

Product details

Cathepsin D Inhibitor Screening Kit (ab126779) is a fluorescence-based assay that utilizes the preferred cathepsin D substrate sequence GKPILFFRLK(Dnp)-D-R-NH2) labeled with MCA. Cathepsin D will cleave the synthetic substrate to release the quenched fluorescent group MCA, which can then easily be measured using a fluorometer or fluorescence plate reader at Ex/Em = 328/460 nm. The relative efficacy of test inhibitors are compared to the positive control inhibitor, Pepstatin A (IC50 < 0.1 nM). The Cathepsin D assay is simple, straightforward, and can be adapted to 96-well plate assays and is suitable for high throughput screening (HTS).
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This product is manufactured by BioVision, an Abcam company and was previously called K148 Cathepsin D Inhibitor Screening Kit (Fluorometric). K148-100 is the same size as the 100 test size of ab126779.

Apoptosis can be mediated by mechanisms other than the traditional caspase-mediated cleavage cascade. There is growing recognition that alternative proteolytic enzymes such as the lysosomal cathepsin proteases may initiate or propagate pro-apoptotic signals. Cathepsins are lysosomal enzymes that are also used as sensitive markers in various toxicological investigations.

The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.

What's included?

{ "values": { "100Test": { "sellingSize": "100 Test", "publicAssetCode":"ab126779-100Test", "assetComponentDetails": [ { "size":"1 x 1 Vial", "name":"Human Cathepsin D", "number":"AB126779-CMP01", "productcode":"" }, { "size":"1 x 0.2 mL", "name":"Substrate II", "number":"AB126779-CMP03", "productcode":"" }, { "size":"1 x 10 mL", "name":"CD Reaction Buffer", "number":"AB126779-CMP02", "productcode":"" }, { "size":"1 x 20 µL", "name":"Pepstatin A Solution", "number":"AB126779-CMP04", "productcode":"" } ] } } }

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Please refer to protocols

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Cathepsin D also known as CTSD is a protein with a mass of approximately 45 kDa. It functions as an aspartyl protease and is expressed in lysosomes across various tissues including the liver and kidneys. This enzyme acts by cleaving peptide bonds within proteins which is essential for protein degradation and turnover. Cathepsin D exists as precursor forms that become activated in the acidic environment of the lysosome. It plays a critical role in normal cellular processes by maintaining protein homeostasis.
Biological function summary

The enzymatic activity of Cathepsin D is important for cellular maintenance and apoptosis. This protease does not act within larger protein complexes but contributes to the degradation of extracellular and intracellular proteins. It mediates processes like antigen processing where it deconstructs proteins into peptides that are presented on major histocompatibility complex (MHC) molecules. ELISA tests can quantify its expression levels sometimes termed as CTSD activity in various biological samples offering insights into its role within cellular environments.

Pathways

Cathepsin D involvement includes the lysosomal degradation pathway and the apoptotic signaling pathway. In the lysosomal degradation pathway Cathepsin D breaks down proteins and peptides a process important for cellular recycling and energy release. It interacts with other lysosomal enzymes such as Cathepsin B in this pathway ensuring comprehensive breakdown of cellular waste. The apoptotic signaling pathway involves the regulation of programmed cell death where Cathepsin D can influence the activation of downstream proteins like Bcl-2 and Bax which control cell survival.

The overexpression of Cathepsin D links to breast cancer and Alzheimer's disease. In breast cancer increased Cathepsin D expression correlates with tumor progression and metastasis influencing tumor behavior through interactions with other proteins involved in cell proliferation. Alzheimer's disease features the involvement of Cathepsin D in the breakdown of amyloid precursor protein which relates to amyloid beta plaque accumulation. The abnormal activity of Cathepsin D in these disorders makes it a potential target for therapeutic antibodies such as CTSD antibodies which aim to regulate its function.

Product protocols

Target data

Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation (PubMed : 27333034). Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.
See full target information CTSD

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Autophagy 9:2087-102 PubMed24113242

2013

The antimalarial amodiaquine causes autophagic-lysosomal and proliferative blockade sensitizing human melanoma cells to starvation- and chemotherapy-induced cell death.

Applications

Unspecified application

Species

Unspecified reactive species

Shuxi Qiao,Shasha Tao,Montserrat Rojo de la Vega,Sophia L Park,Amanda A Vonderfecht,Suesan L Jacobs,Donna D Zhang,Georg T Wondrak
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