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Merck
모든 사진(4)

주요 문서

D4443

Sigma-Aldrich

Anti-Derlin-1 antibody produced in rabbit

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

동의어(들):

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

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About This Item

MDL number:
UNSPSC 코드:
12352203
NACRES:
NA.41

생물학적 소스

rabbit

Quality Level

결합

unconjugated

항체 형태

affinity isolated antibody

항체 생산 유형

primary antibodies

클론

polyclonal

양식

buffered aqueous solution

분자량

antigen ~22 kDa

종 반응성

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

농도

~1 mg/mL

기술

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 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

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

일반 설명

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.

면역원

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.

애플리케이션

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

생화학적/생리학적 작용

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.

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

10 - Combustible liquids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

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


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문서 라이브러리 방문

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
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
Brendan N Lilley et al.
Nature, 429(6994), 834-840 (2004-06-25)
After insertion into the endoplasmic reticulum (ER), proteins that fail to fold there are destroyed. Through a process termed dislocation such misfolded proteins arrive in the cytosol, where ubiquitination, deglycosylation and finally proteasomal proteolysis dispense with the unwanted polypeptides. The

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