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SRP6415

Sigma-Aldrich

Cathepsin D human

recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)

Synonym(s):

CLN10, CPSD, CTSD

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in HEK 293 cells

tag

6-His tagged (C-terminus)

Assay

≥95% (SDS-PAGE)

form

lyophilized

mol wt

calculated mol wt 43.6 kDa
observed mol wt 45-55 kDa (DTT-reduced. Protein migrates due to glycosylation. Ser 19 is the predicted N-terminal.)

packaging

pkg of 10 μg

manufacturer/tradename

Sigma-Aldrich

storage condition

dry at room temperature

technique(s)

activity assay: suitable

impurities

<1 EU/μg endotoxin (LAL test)

suitability

suitable for molecular biology

UniProt accession no.

application(s)

life science and biopharma

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... CTSD(1509)

General description

Research area: Cell signalling. Cathepsin D belongs to the peptidase A1 family, an estrogenic-induced lysosomal protease. Cathepsin D can be cleaved into the following 2 chains: N-terminal light chain and C-terminal heavy chain, which is expressed in the aorta extracellular space (at the protein level). ). It is found in most mammalian cells and is located in thelysosomes.
This gene is mapped to human chromosome 11p15.5.

Application

Cathepsin D has been used in the protease digestion of haemoglobin.

Biochem/physiol Actions

Cathepsin D (CatD) takes part in the intracellular degradation of advanced glycation end (AGE) products. AGE deposition is predominant in photoaged skin. Thus, CatD might be useful in antiphotoaging therapy. Elevated circulating CatD is observed in type 2 diabetes and can be considered an important biomarker for type 2 diabetes-dependent cardiac dysfunction. Increased CatD, is observed in non-alcoholic steatohepatitis.Cathepsin D is involved in various physiological processes like apoptosis, autophagy, and protein degradation. Cathepsin D plays an important role in the pathogenesis of Alzheimer’s disease, neuronal ceroid lipofuscinosis, and breast cancer.

Physical form

Lyophilized from 0.22 μm filtered solution in 50 mM MES, pH 6.5 with 100 mM NaCl. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.

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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Plasma cathepsin D correlates with histological classifications of fatty liver disease in adults and responds to intervention
Walenbergh SMA, et al.
Scientific reports, 6(1), 38278-38278 (2016)
Cluster analysis of risk factor genetic polymorphisms in Alzheimer?s disease
Randall CN, et al.
Neurochemical Research, 34(1), 23-28 (2009)
Increased Cathepsin D Correlates with Clinical Parameters in Newly Diagnosed Type 2 Diabetes
Liu L, et al.
Disease Markers, 2017(1), 23-28 (2017)
Xiaolai Zhou et al.
Molecular neurodegeneration, 12(1), 62-62 (2017-08-25)
Mutations resulting in progranulin (PGRN) haploinsufficiency cause frontotemporal lobar degeneration with TDP-43-positive inclusions (FTLD-TDP), a devastating neurodegenerative disease. PGRN is localized to the lysosome and important for proper lysosome function. However, the metabolism of PGRN in the lysosome is still
Cathepsin D contributes to the accumulation of advanced glycation end products during photoaging
Xu X, et al.
Journal of Dermatological Science, 90(3), 263-275 (2018)

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