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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
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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

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C8696C0715SRP0289
Gene Information

human ... CTSD(1509)

Gene Information

human ... CTSD(1509)

Gene Information

human ... CTSD(1509)

Gene Information

human ... CTSB(1508)

technique(s)

activity assay: suitable

technique(s)

-

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:200 using human breast carcinoma tissue, indirect ELISA: suitable, microarray: suitable, western blot: 1:1,000 using human breast carcinoma cell line extract

technique(s)

activity assay: suitable

assay

≥95% (SDS-PAGE)

assay

-

assay

-

assay

≥90% (SDS-PAGE)

biological source

human

biological source

-

biological source

mouse

biological source

human

application(s)

life science and biopharma

application(s)

-

application(s)

-

application(s)

life science and biopharma

form

lyophilized

form

lyophilized powder

form

-

form

aqueous solution

General description

Research area: Cell signalling. Cathepsin D belongs to the peptidase A1 family,[1] an estrogenic-induced lysosomal protease.[2] 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.[3]
This gene is mapped to human chromosome 11p15.5.[4]

Application

Cathepsin D has been used in the protease digestion of haemoglobin.[5]

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.[6] Elevated circulating CatD is observed in type 2 diabetes and can be considered an important biomarker for type 2 diabetes-dependent cardiac dysfunction.[7] Increased CatD, is observed in non-alcoholic steatohepatitis.[8]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,[3] and breast cancer.[2]

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


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    Alexis L Gabbey et al.
    Organic letters, 24(17), 3173-3178 (2022-04-27)
    The transition-metal-catalyzed α-arylation of secondary amides remains a synthetic challenge due to the presence of a free N-H bond. We report a strategy to synthesize secondary α-aryl amides via a Ni-catalyzed reductive arylation of redox-active N-hydroxyphthalimide (NHP) esters of malonic

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