C3138
Cathepsin D from bovine spleen
lyophilized powder, ≥2.0 units/mg protein
Synonyme(s) :
CTSD
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32
Produits recommandés
Source biologique
bovine spleen
Pureté
10—70% protein (biuret)
Forme
lyophilized powder
Activité spécifique
≥2.0 units/mg protein
Poids mol.
~45 kDa
Fabricant/nom de marque
Sigma-Aldrich
Technique(s)
activity assay: suitable
Couleur
dark brown
Adéquation
suitable for molecular biology
Numéro d'accès UniProt
Application(s)
life science and biopharma
Température de stockage
−20°C
Informations sur le gène
cow ... CTSD(282883)
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Description générale
Research area: Cell Signaling
Cathepsin D is a soluble endosomal-lysosomal aspartic protease and is synthesized in the rough endoplasmic reticulum as preprocathepsin D. It is encoded by the CTSD gene located in the 11p15.5 region.
Cathepsin D is a soluble endosomal-lysosomal aspartic protease and is synthesized in the rough endoplasmic reticulum as preprocathepsin D. It is encoded by the CTSD gene located in the 11p15.5 region.
Application
Cathepsin D from bovine spleen has been used:
- in in vitro dose-dependent fluorometric activity assays.
- in in vitro myelin oligodendrocyte glycoprotein (MOG) digestion to study the uptake of malondialdehyde (MDA)-modified MOG and its implications in central nervous system autoimmunity.
- for enzymatic digestion of the proteoglycan moiety of the articular cartilage in order to determine its dynamic elastic modulus at two different levels of tissue organization.
- in cathepsin D activity assay.
Actions biochimiques/physiologiques
Cathepsin D is an endosomal-lysosomal aspartic protease implicated in breast cancer metastasis and Alzheimer′s disease. Lysosomal release of cathepsin D has been found to precede cytochrome c release and loss of membrane potential in apoptotic human foreskin fibroblasts. Cathepsin D levels in PC12 cells increase 12 to 24 hours after apoptosis is induced.
Définition de l'unité
One unit will produce an increase in A280 of 1.0 per min per mL at pH 3.0 at 37 °C measured as TCA-soluble products using hemoglobin as substrate (1 cm light path).
Forme physique
Lyophilized powder containing citrate buffer salts
Inhibiteur
Produit(s) apparenté(s)
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Les clients ont également consulté
Martin Stolz et al.
Biophysical journal, 86(5), 3269-3283 (2004-04-28)
Cartilage stiffness was measured ex vivo at the micrometer and nanometer scales to explore structure-mechanical property relationships at smaller scales than has been done previously. A method was developed to measure the dynamic elastic modulus, |E(*)|, in compression by indentation-type
Olja Mijanovic et al.
Pharmaceutics, 13(6) (2021-07-03)
Lysosomal proteases play a crucial role in maintaining cell homeostasis. Human cathepsin D manages protein turnover degrading misfolded and aggregated proteins and favors apoptosis in the case of proteostasis disruption. However, when cathepsin D regulation is affected, it can contribute
Jason S King et al.
Molecular biology of the cell, 24(17), 2714-2726 (2013-07-26)
Wiskott-Aldrich syndrome protein and SCAR homologue (WASH) is an important regulator of vesicle trafficking. By generating actin on the surface of intracellular vesicles, WASH is able to directly regulate endosomal sorting and maturation. We report that, in Dictyostelium, WASH is
Gabriel C Baltazar et al.
PloS one, 7(12), e49635-e49635 (2012-12-29)
Lysosomal enzymes function optimally in acidic environments, and elevation of lysosomal pH can impede their ability to degrade material delivered to lysosomes through autophagy or phagocytosis. We hypothesize that abnormal lysosomal pH is a key aspect in diseases of accumulation
Maria Pernemalm et al.
Journal of proteome research, 12(9), 3934-3943 (2013-08-02)
In this study, we have analyzed human primary lung adenocarcinoma tumors using global mass spectrometry to elucidate the biological mechanisms behind relapse post surgery. In total, we identified over 3000 proteins with high confidence. Supervised multivariate analysis was used to
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