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E1782

Sigma-Aldrich

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

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

Synonim(y):

Anti-ER degradation enhancer, mannosidase alpha-like 2

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About This Item

Kod UNSPSC:
12352203

pochodzenie biologiczne

rabbit

białko sprzężone

unconjugated

forma przeciwciała

affinity isolated antibody

rodzaj przeciwciała

primary antibodies

klon

polyclonal

Postać

buffered aqueous solution

masa cząsteczkowa

antigen ~70 kDa

reaktywność gatunkowa

mouse, rat, human

stężenie

~1.0 mg/mL

metody

indirect immunofluorescence: suitable
western blot: 0.5-1.0 μg/mL using whole extracts of human HepG2 and rat NRK cells.

numer dostępu UniProt

Q9BV94

Warunki transportu

dry ice

temp. przechowywania

−20°C

informacje o genach

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

Opis ogólny

Three EDEM homologs, EDEM1, EDEM2 and EDEM3 have been identified, which are transcriptionally upregulated upon ER stress by the activated IRE1/Xbp-1 branch. EDEM2 is localized to the ER, mainly as a soluble glycoprotein, interacts with calnexin and lacks mannosidase activity.

Zastosowanie

Anti-EDEM2 antibody produced in rabbit is suitable for indirect immunofluorescence and immunoblotting at a working concentration of 0.5-1.0μg/mL using whole extracts of human HepG2 and rat NRK cells.

Działania biochem./fizjol.

EDEM2 (ER degradation-enhancing α-mannosidase-like protein 2), a stress-regulated mannosidase-like protein, targets misfolded glycoproteins for degradation in an N-glycan dependent manner. Over-expression of EDEM2 accelerates ERAD (ER-associated degradation) by promoting the release of terminally misfolded glycoproteins from the calnexin cycle, without affecting the rate of degradation of non-glycosylated polypeptides or the maturation of model secretory proteins.

Postać fizyczna

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

Oświadczenie o zrzeczeniu się odpowiedzialności

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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Kod klasy składowania

12 - Non Combustible Liquids

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

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

Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Yukako Oda et al.
Science (New York, N.Y.), 299(5611), 1394-1397 (2003-03-01)
Terminally misfolded proteins in the endoplasmic reticulum (ER) are retrotranslocated to the cytoplasm and degraded by proteasomes through a mechanism known as ER-associated degradation (ERAD). EDEM, a postulated Man8B-binding protein, accelerates the degradation of misfolded proteins in the ER. Here
Cristian V A Munteanu et al.
Molecular & cellular proteomics : MCP, 20, 100125-100125 (2021-08-01)
Various pathologies result from disruptions to or stress of endoplasmic reticulum (ER) homeostasis, such as Parkinson's disease and most neurodegenerative illnesses, diabetes, pulmonary fibrosis, viral infections, and cancers. A critical process in maintaining ER homeostasis is the selection of misfolded
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
Cristina Pintado et al.
Scientific reports, 7(1), 8100-8100 (2017-08-16)
Proteostasis alteration and neuroinflammation are typical features of normal aging. We have previously shown that neuroinflammation alters cellular proteostasis through immunoproteasome induction, leading to a transient decrease of proteasome activity. Here, we further investigated the role of acute lipopolysaccharide (LPS)-induced
Min Ni et al.
FEBS letters, 581(19), 3641-3651 (2007-05-08)
The field of endoplasmic reticulum (ER) stress in mammalian cells has expanded rapidly during the past decade, contributing to understanding of the molecular pathways that allow cells to adapt to perturbations in ER homeostasis. One major mechanism is mediated by
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