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Key Documents

Altri documenti

E9906

Sigma-Aldrich

Anti-EDEM2 (N-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinonimo/i:

Anti-ER degradation enhancer, mannosidase alpha-like 2

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About This Item

Codice UNSPSC:
12352203

Origine biologica

rabbit

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

PM

antigen ~70 kDa

Reattività contro le specie

human, rat (predicted), mouse

Concentrazione

~1.0 mg/mL

tecniche

indirect immunofluorescence: 5-10 μg/mL using mouse 3T3 cells
western blot: 0.5-1 μg/mL using whole extracts of HEK-293T cells expressing recombinant human EDEM2

N° accesso UniProt

Q9BV94

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... EDEM2(55741)
mouse ... Edem2(108687)
rat ... Edem2(296304)

Descrizione generale

ER degradation-enhancing α-mannosidase-like 2 is an enzyme encoded by the EDEM2 gene in humans. EDEM2 is localized to the endoplasmic reticulum (ER) mainly as a soluble glycoprotein. It is an enzyme encoded by the EDEM2 gene in humans. It is one of the ER-stress-induced members of the glycosyl hydrolase 47 family.

Immunogeno

synthetic peptide corresponding to amino acids 22-38 of human EDEM2, conjugated to KLH. The corresponding sequence differs by one amino acid in mouse and 2 amino acids in rat EDEM2.

Applicazioni

Anti-EDEM2 (N-terminal) antibody produced in rabbit is suitable for indirect immunofluorescence at a concentration of 5-10μg/mL using mouse 3T3 cells and western blotting at a concentration of 0.5-1μg/mL using whole extracts of HEK-293T cells expressing recombinant human EDEM2.

Azioni biochim/fisiol

Overexpression of ER degradation-enhancing alphamannosidase-like protein 2 (EDEM2) accelerates ER associated degradation (ERAD) by promoting the release of terminally misfolded glycoproteins from the calnexin cycle, without affecting the rate of degradation of nonglycosylated polypeptides or the maturation of model secretory proteins.

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Certificati d'analisi (COA)

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Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
Molinari M, et al.
Science, 299(5611), 1397-1400 (2003)
Steven W Mast et al.
Glycobiology, 15(4), 421-436 (2004-11-13)
In the endoplasmic reticulum (ER), misfolded proteins are retrotranslocated to the cytosol and degraded by the proteasome in a process known as ER-associated degradation (ERAD). Early in this pathway, a proposed lumenal ER lectin, EDEM, recognizes misfolded glycoproteins in the
Silvia Olivari et al.
FEBS letters, 581(19), 3658-3664 (2007-05-15)
Proteins synthesized in the endoplasmic reticulum (ER) lumen are exposed to several dedicated chaperones and folding factors that ensure efficient maturation. Nevertheless, protein folding remains error-prone and mutations in the polypeptide sequence may significantly reduce folding-efficiency. Folding-incompetent proteins carrying N-glycans
Silvia Olivari et al.
The Journal of biological chemistry, 280(4), 2424-2428 (2004-12-08)
Proteins expressed in the endoplasmic reticulum (ER) are subjected to a tight quality control. Persistent association with ER-resident molecular chaperones prevents exit of misfolded or incompletely assembled polypeptides from the ER and forward transport along the secretory line. ER-associated degradation

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