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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

Número de CAS:
Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

form

lyophilized powder

Quality Level

specific activity

≥250 units/mg protein (E1%/280)

mol wt

~45 kDa

color

white

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... CTSD(1509)

General description

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.

Application

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 Actions

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.

Other Notes

Contains α, β and γ isoenzymes as observed by isoelectric-focusing.

Unit Definition

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).

Physical form

Powder containing sodium phosphate buffer salt.

Related product

inhibitor

Referencia del producto
Descripción
Precios

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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Aspartic Proteinases Physiology and Pathology (1995)
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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.
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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.
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