E8159
Anti-EDEM1 antibody,Mouse monoclonal
clone EDEM1-17, purified from hybridoma cell culture
Synonym(s):
Anti-EDEM, Anti-ER degradation enhancer, mannosidase alpha-like 1
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About This Item
NACRES:
NA.43
UNSPSC Code:
12352203
Product Name
Anti-EDEM1 antibody,Mouse monoclonal, clone EDEM1-17, purified from hybridoma cell culture
biological source
mouse
conjugate
unconjugated
antibody form
purified from hybridoma cell culture
antibody product type
primary antibodies
clone
EDEM1-17, monoclonal
form
buffered aqueous solution
mol wt
antigen 75/65 kDa
species reactivity
mouse, human
concentration
~1.0 mg/mL
technique(s)
immunoprecipitation (IP): suitable
western blot: 1-2 μg/mL using whole extracts of HEK-293T cells expressing recombinant human or mouse EDEM1
isotype
IgG2a
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified, unmodified
Quality Level
Gene Information
human ... EDEM1(9695)
Application
Monoclonal Anti-EDEM1 antibody produced in mouse has been used in:
- immunoblotting
- immunoprecipitation
- immuno-electron microscopy
- immunohistochemistry (IHC)
Biochem/physiol Actions
EDEM1 (ER degradation-enhancing alphamannosidase-like protein 1) has the ability to interact with the COOH-terminus of calnexin. It lacks mannosidase activity.
ER degradation-enhancing α-mannosidase-like 1 is an enzyme encoded by the EDEM1 gene in humans. It is a chaperone for rod opsin and its expression can be used to promote correct folding enhancing degradation of mutant proteins in the ER to combat protein-misfolding disease. The endogenous EDEM1 in cells that are not stressed by the expression of a transgenic misfolded protein reaches the cytosol and is degraded by basal autophagy. EDEM may maintain the retrotranslocation competence of NHK by inhibiting aggregation. It is also considered responsible for directing aberrant proteins for ERAD (ER-associated protein degradation).
Disclaimer
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.
General description
Monoclonal Anti-EDEM1 (mouse IgG2a isotype) is derived from the hybridoma EDEM1-17 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to a fragment of human EDEM1. conjugated to keyhole limpet hemocyanin (KLH). EDEM1 (ER degradation-enhancing alphamannosidase-like protein 1) is a putative mannose binding lectin. In mammalian cells, EDEM1 is localized to the endoplasmic reticulum (ER), mainly as a soluble glycoprotein.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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Storage Class
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites
Zuber C, et al.
Proceedings of the National Academy of Sciences of the USA, 104(11), 4407-4412 (2007)
Christine Insinna et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 32(23), 8094-8104 (2012-06-08)
In absence of their natural ligand, 11-cis-retinal, cone opsin G-protein-coupled receptors fail to traffic normally, a condition associated with photoreceptor degeneration and blindness. We created a mouse with a point mutation (F81Y) in cone S-opsin. As expected, cones with this
Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins
Mast SW, et al.
Glycobiology, 15(4), 421-436 (2004)
Nobuko Hosokawa et al.
Genes to cells : devoted to molecular & cellular mechanisms, 11(5), 465-476 (2006-04-25)
Misfolded glycoproteins are degraded by a mechanism known as ERAD (ER-associated degradation) after retrotranslocation out of the endoplasmic reticulum (ER). This mechanism plays an important role in ER quality control. We previously reported that an ER membrane protein, EDEM, accelerates
V Le Fourn et al.
Cellular and molecular life sciences : CMLS, 66(8), 1434-1445 (2009-03-07)
Little is known about the fate of machinery proteins of the protein quality control and endoplasmic reticulum(ER)-associated degradation (ERAD). We investigated the degradation of the ERAD component EDEM1, which directs overexpressed misfolded glycoproteins to degradation. Endogenous EDEM1 was studied since
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