Recombinant Human Cathepsin D protein
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(1 Publication)
Recombinant Human Cathepsin D protein is a Human Full Length protein, in the 19 to 412 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.
View Alternative Names
CPSD, CTSD, Cathepsin D
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
Specifications
Form
Liquid
Additional notes
Purity is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. ab151860 has been 0.2 µM filtered.
General info
Function
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.
Sequence similarities
Belongs to the peptidase A1 family.
Post-translational modifications
N- and O-glycosylated.. Undergoes proteolytic cleavage and activation by ADAM30.. As well as the major heavy chain which starts at Leu-169, 2 minor forms starting at Gly-170 and Gly-171 have been identified (PubMed:1426530). An additional form starting at Ala-168 has also been identified (PubMed:27333034).
Subcellular localisation
Lysosome
Target data
Publications (1)
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Experimental cell research 383:111494 PubMed31306655
2019
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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