Description
Key facts
Purity:>95% SDS-PAGE,
Expression system:Native,
Tags:Tag free,
Applications:WB, SDS-PAGE, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:>=300 units per mg protein. One unit is defined as the amount of enzyme that digests hemoglobin-releasing peptides which are soluble in 10% TCA. The reaction is measured by an increase of an A280 of 1.0 per 60 minutes at 37°C . Substrate: acid denatured hemoglobin, pH 1.8 (0.2% in reaction mixture). Buffer: 100 mM formate, pH 3.3.,
Accession:P07339,
Animal free:No,
Carrier free:No,
Species:Human,
Reconstitution:Resuspend a 25ug vial with 71.4uL of deionized H2O to give a protein concentration of 0.350mg/mL, which is the original protein concentration of the lot when it was finished. This should then be aliquotted into suitable amounts in a screw top vial to prevent sublimation and stored at <70 deg C. Aliquots should be diluted to appropriate concentration once thawed. We recommend 2mM NaP pH 6.5 to make dilutions.,
Storage buffer:pH: 6.5Constituents: 0.0328% Sodium phosphate
Product details:
Lyophilized from 2 mM Na phosphate, pH 6.5.
Protein Determination: Extinction Coefficient (E) 0.1% at 280nm, 1cm pathway = 1.0 Prepared from tissue shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--80°C
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.
