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C3138

Sigma-Aldrich

Cathepsin D from bovine spleen

lyophilized powder, ≥2.0 units/mg protein

Synonym(s):

CTSD

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

biological source

bovine spleen

Quality Level

Assay

10—70% protein (biuret)

form

lyophilized powder

specific activity

≥2.0 units/mg protein

mol wt

~45 kDa

manufacturer/tradename

Sigma-Aldrich

technique(s)

activity assay: suitable

color

dark brown

suitability

suitable for molecular biology

UniProt accession no.

application(s)

life science and biopharma

storage temp.

−20°C

Gene Information

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General description

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.

Application

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 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.

Unit Definition

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).

Physical form

Lyophilized powder containing citrate buffer salts

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Cathepsin D--many functions of one aspartic protease
Benes P, et al.
Critical Reviews in Oncology/Hematology, 68(1), 12-28 (2008)
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.
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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