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Merck
CN

E1782

Sigma-Aldrich

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

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

别名:

Anti-ER degradation enhancer, mannosidase alpha-like 2

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About This Item

UNSPSC代码:
12352203

生物来源

rabbit

偶联物

unconjugated

抗体形式

affinity isolated antibody

抗体产品类型

primary antibodies

克隆

polyclonal

表单

buffered aqueous solution

分子量

antigen ~70 kDa

种属反应性

mouse, rat, human

浓度

~1.0 mg/mL

技术

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

UniProt登记号

运输

dry ice

储存温度

−20°C

基因信息

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

一般描述

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.

应用

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.

生化/生理作用

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.

外形

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

免责声明

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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储存分类代码

12 - Non Combustible Liquids

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

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

法规信息

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分析证书(COA)

Lot/Batch Number

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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
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
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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