C8696
Cathepsin D from human liver
lyophilized powder, ≥250 units/mg protein (E1%/280)
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About This Item
Productos recomendados
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.
inhibitor
Referencia del producto
Descripción
Precios
related product
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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In this study, cathepsin D was oxidized in vitro with different concentrations of H2O2, and the activity, structure, and extent of myofibrillar protein degradation by oxidized cathepsin D were evaluated. The sulfhydryl content of cathepsin D decreased to 9.20% after
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