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Merck

C8696

Sigma-Aldrich

Cathepsin D from human liver

lyophilized powder, ≥250 units/mg protein (E1%/280)

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About This Item

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

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

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WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

Aspartic Proteinases Physiology and Pathology (1995)
Platelet membrane beta-secretase activity in mild cognitive impairment and conversion to dementia: a longitudinal study
McGuinness B, et al.
Journal of Alzheimer'S Disease, 49(4), 1095-1103 (2016)
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
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

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