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C8696
Cathepsin D from human liver
lyophilized powder, ≥250 units/mg protein (E1%/280)
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About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.32
Empfohlene Produkte
Form
lyophilized powder
Qualitätsniveau
Spezifische Aktivität
≥250 units/mg protein (E1%/280)
Mol-Gew.
~45 kDa
Farbe
white
UniProt-Hinterlegungsnummer
Lagertemp.
−20°C
Angaben zum Gen
human ... CTSD(1509)
Allgemeine Beschreibung
Cathepsin D is an aspartic protease, which is located in lysosomes. It is involved in protein catabolism and maintains hormone and antigen processing. Cathepsin D is implicated in neoplasia and neurodegenerative changes. It regulates lysosomal proteolysis and endogenous fibrinolysis.
Anwendung
Cathepsin D from human liver has been used:
- in β-secretase activity assay
- for enzymatic degradation of amyloid β 1-42
- in microinjection of human foreskin fibroblasts
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.
Sonstige Hinweise
Contains α, β and γ isoenzymes as observed by isoelectric-focusing.
Einheitendefinition
One unit will produce an increase in A280 of 1.0 in 30 min at pH 3.3 at 37 °C measured as TCA-soluble products using acid-denatured hemoglobin as substrate (1 cm light path).
Physikalische Form
Powder containing sodium phosphate buffer salt.
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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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.
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