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Merck

C3138

Sigma-Aldrich

Kathepsin D aus Rindermilz

lyophilized powder, ≥2.0 units/mg protein

Synonym(e):

CTSD

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About This Item

CAS-Nummer:
EC-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.32

Biologische Quelle

bovine spleen

Qualitätsniveau

Assay

10—70% protein (biuret)

Form

lyophilized powder

Spezifische Aktivität

≥2.0 units/mg protein

Mol-Gew.

~45 kDa

Hersteller/Markenname

Sigma-Aldrich

Methode(n)

activity assay: suitable

Farbe

dark brown

Eignung

suitable for molecular biology

UniProt-Hinterlegungsnummer

Anwendung(en)

life science and biopharma

Lagertemp.

−20°C

Angaben zum Gen

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Allgemeine Beschreibung

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.

Anwendung

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.

Biochem./physiol. Wirkung

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.

Einheitendefinition

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).

Physikalische Form

Lyophilized powder containing citrate buffer salts

Inhibitor

Produkt-Nr.
Beschreibung
Preisangaben

Ähnliches Produkt

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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
Marie Maynadier et al.
Journal of controlled release : official journal of the Controlled Release Society, 171(2), 251-257 (2013-08-01)
Implication of the intracellular proteolytic activity of Cathepsin D (CathD), a lysosomal aspartyl-protease overexpressed in numerous solid tumors, has been evidenced on tumor growth. Its intracellular inhibition by potent inhibitors such as pepstatin constitutes a relevant but challenging molecular target.
Cathepsin D from porcine and bovine spleen.
T Takahashi et al.
Methods in enzymology, 80 Pt C, 565-581 (1981-01-01)
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

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