Direkt zum Inhalt
Merck

E9906

Sigma-Aldrich

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

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

Synonym(e):

Anti-ER degradation enhancer, mannosidase alpha-like 2

Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise


About This Item

UNSPSC-Code:
12352203

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

antigen ~70 kDa

Speziesreaktivität

human, rat (predicted), mouse

Konzentration

~1.0 mg/mL

Methode(n)

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

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

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

Allgemeine Beschreibung

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.

Immunogen

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.

Anwendung

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.

Biochem./physiol. Wirkung

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.

Physikalische Form

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

Haftungsausschluss

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.

Sie haben nicht das passende Produkt gefunden?  

Probieren Sie unser Produkt-Auswahlhilfe. aus.

Lagerklassenschlüssel

10 - Combustible liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

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


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

Besitzen Sie dieses Produkt bereits?

In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

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

Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..

Setzen Sie sich mit dem technischen Dienst in Verbindung.