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Merck
CN

D4443

Sigma-Aldrich

Anti-Derlin-1 antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

别名:

Anti-DERtrin 1, Anti-Degradation in endoplasmic reticulum protein 1, Anti-Derl-like protein 1

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关于此项目

MDL编号:
UNSPSC代码:
12352203
NACRES:
NA.41
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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 ~22 kDa

种属反应性

rat, hamster, monkey, mouse, bovine, human, canine

浓度

~1 mg/mL

技术

indirect immunofluorescence: 2.5-5 μg/mL using rat NRK cells
western blot (chemiluminescent): 0.2-0.4 μg/mL using whole extract of human HeLa and mouse 3T3 cells.

UniProt登记号

运输

dry ice

储存温度

−20°C

靶向翻译后修饰

unmodified

基因信息

human ... DERL1(79139)
mouse ... Derl1(67819)

一般描述

Derlin-1 is a 22kDa hydrophobic protein that spans the lipid bilayer of the ER four times with its amino- and carboxy-terminus in the cytosol. It is expressed with high levels in liver, spleen, pancreas, lung, thymus, and ovary.
Derlin-1 shares human homology with yeast Der1p.

免疫原

a synthetic peptide corresponding to the C-terminal region of human Derlin-1 with N-terminal added cysteine, conjugated to KLH. The corresponding sequence is identical in mouse.

应用

Anti-Derlin-1 antibody produced in rabbit has been used in:
  • immunostaining
  • co-immunoprecipitation
  • immunofluorescence

生化/生理作用

Derlin-1 can interact with peptide:N-glycanase (PNGase), a deglycosylating enzyme, bringing it close to misfolding dislocating glycoproteins.
Derlin-1 is required for the dislocation of misfolded proteins from the ER lumen to the cytosol, where they are destroyed by the ubiquitin-proteasome system. It interacts with PNGase, a deglycosylating enzyme, bringing it close to misfolding dislocating glycoproteins. It forms a membrane protein complex with VIMP ( (VCP-interacting membrane protein) and this complex serves as a receptor for p97. p97 interacts with several ubiquitin ligases, thus recruiting them to Derlin-1.

外形

0.01M 磷酸缓冲盐溶液,pH 7.4,含 15mM 叠氮化钠。

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

10 - Combustible liquids

WGK

WGK 3

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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Zlatka Kostova et al.
The EMBO journal, 22(10), 2309-2317 (2003-05-14)
The surveillance of the structural fidelity of the proteome is of utmost importance to all cells. The endoplasmic reticulum (ER) is the organelle responsible for proper folding and delivery of proteins to the secretory pathway. It contains a sophisticated protein
Hui You et al.
Free radical biology & medicine, 207, 260-271 (2023-07-28)
The functions of liver fatty acid binding protein 1 (FABP1) in the regulation of nonalcoholic fatty liver disease (NAFLD) have been previously established. However, how FABP1 expression is dynamically regulated in metabolic disorders is unclear. Previous studies have reported that
Molecular characterization and expression of DERL1 in bovine ovarian follicles and corpora lutea
Ndiaye K, et al.
Reproductive Biology and Endocrinology, 8(1), 94-94 (2010)
Yihong Ye et al.
Proceedings of the National Academy of Sciences of the United States of America, 102(40), 14132-14138 (2005-09-28)
Misfolded proteins are eliminated from the endoplasmic reticulum (ER) by retrotranslocation into the cytosol, a pathway hijacked by certain viruses to destroy MHC class I heavy chains. The translocation of polypeptides across the ER membrane requires their polyubiquitination and subsequent
Yihong Ye et al.
Nature, 429(6994), 841-847 (2004-06-25)
Elimination of misfolded proteins from the endoplasmic reticulum (ER) by retro-translocation is an important physiological adaptation to ER stress. This process requires recognition of a substrate in the ER lumen and its subsequent movement through the membrane by the cytosolic

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