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  • E9906 - Anti-EDEM2 (N-terminal) antibody produced in rabbit

E9906 Sigma

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

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

Synonym: Anti-ER degradation enhancer, mannosidase alpha-like 2


Related Categories Alphabetical Index, Antibodies, Antibodies for Cell Biology, Antibodies for Cell Stress, Antibodies to Oxidative Stress Proteins,
species reactivity   mouse, human, rat (predicted)
application(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
clone   polyclonal
concentration   ~1.0 mg/mL
antibody form   affinity isolated antibody
form   buffered aqueous solution
mol wt   antigen mol wt ~70 kDa
shipped in   dry ice
storage temp.   −20°C
Gene Information   human ... EDEM2(55741)
mouse ... Edem2(108687)
rat ... Edem2(296304)
biological source   rabbit
conjugate   unconjugated



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.

Physical form

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


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.

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Biochem/physiol Actions

ER degradation-enhancing α-mannosidase-like 2 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. EDEM2 is a novel, stress-regulated mannosidase-like protein that operates in the ER lumen. The transcriptional up-regulation of EDEM2 depends on the ER stress-activated transcription factor Xbp1 that accelerates ER-associated degradation (ERAD) of terminally misfolded glycoproteins by facilitating their extraction from the calnexin cycle.

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