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E9906

Sigma-Aldrich

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

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

Synonyme(s) :

Anti-ER degradation enhancer, mannosidase alpha-like 2

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About This Item

Code UNSPSC :
12352203

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~70 kDa

Espèces réactives

human, rat (predicted), mouse

Concentration

~1.0 mg/mL

Technique(s)

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

Numéro d'accès UniProt

Q9BV94

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Description générale

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.

Immunogène

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.

Application

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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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