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Merck
모든 사진(1)

Key Documents

E1782

Sigma-Aldrich

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

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

동의어(들):

Anti-ER degradation enhancer, mannosidase alpha-like 2

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About This Item

UNSPSC 코드:
12352203

생물학적 소스

rabbit

결합

unconjugated

항체 형태

affinity isolated antibody

항체 생산 유형

primary antibodies

클론

polyclonal

형태

buffered aqueous solution

분자량

antigen ~70 kDa

종 반응성

mouse, rat, human

농도

~1.0 mg/mL

기술

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

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

유전자 정보

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

일반 설명

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.

애플리케이션

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.

생화학적/생리학적 작용

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.

물리적 형태

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

면책조항

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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Storage Class Code

12 - Non Combustible Liquids

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

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


시험 성적서(COA)

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문서 라이브러리 방문

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
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
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
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
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

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