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Merck
모든 사진(3)

문서

D2194

Sigma-Aldrich

Anti-Derlin-3 antibody produced in rabbit

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

동의어(들):

Anti-DERL3, Anti-Der1-like domain family, member 3

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About This Item

UNSPSC 코드:
12352203
NACRES:
NA.41

생물학적 소스

rabbit

결합

unconjugated

항체 형태

affinity isolated antibody

항체 생산 유형

primary antibodies

클론

polyclonal

형태

buffered aqueous solution

분자량

antigen ~26 kDa

종 반응성

rat (predicted), human, mouse (predicted)

농도

~1 mg/mL

기술

immunoprecipitation (IP): 5-10 μg using extract of HEK-293T cells expressing recombinant human Derlin-3
indirect immunofluorescence: 10-20 μg/mL using human HeLa cells
western blot: 2-5 μg/mL using whole extract of HEK-293T cells expressing recombinant human Derlin-3

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

human ... DERL3(91319)
mouse ... Derl3(70377)
rat ... Derl3(690315)

일반 설명

Derlin-3 is a mammalian homologues of yeast Der1p, a transmembrane protein required for yeast endoplasmic reticulum (ER)-associated degradation (ERAD). Derlin 3 is encoded by the gene mapped to human chromosome 22q11.23. It is expressed in the ER and is a member of the derlin protein family.

면역원

synthetic peptide corresponding to amino acid residues 192-205 of human Derlin-3, conjugated to KLH. The corresponding sequence differs by 3 amino acids in mouse and 2 amino acids in rat.

애플리케이션

Anti-Derlin-3 antibody produced in rabbit has been used in immunoblotting, immunoprecipitation, and immunofluorescence.

생화학적/생리학적 작용

Derlin-3 is involved in the degradation of misfolded glycoproteins in the ER. Derlin-3 shares ~30% sequence identity with Derlin-1 and spans the lipid bilayer of the ER four times, showing structural similarity to Derlin-1. It is a component of the mammalian ER-associated degradation (ERAD) mechanism and is upregulated by unfolded protein response (UPR). Overexpression of this gene leads to increase in degradation of misfolded glycoprotein, whereas its knockdown blocks degradation. Derlin-3 also interacts with the mammalian orthologs of the yeast Hrd1p/Hrd3p ubiquitin-ligase complex.

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

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

Overexpression of Derlin 3 is associated with malignant phenotype of breast cancer cells
Shibata M, et al.
Oncology Reports, 38(3), 1760-1766 (2017)
Yukako Oda et al.
The Journal of cell biology, 172(3), 383-393 (2006-02-02)
Proteins that are unfolded or misfolded in the endoplasmic reticulum (ER) must be refolded or degraded to maintain the homeostasis of the ER. Components of both productive folding and ER-associated degradation (ERAD) mechanisms are known to be up-regulated by the
Brendan N Lilley et al.
Proceedings of the National Academy of Sciences of the United States of America, 102(40), 14296-14301 (2005-09-28)
Polypeptides that fail to pass quality control in the endoplasmic reticulum (ER) are dislocated from the ER membrane to the cytosol where they are degraded by the proteasome. Derlin-1, a member of a family of proteins that bears homology to
Davy Vanhoutte et al.
Nature communications, 12(1), 3928-3928 (2021-06-26)
The thrombospondin (Thbs) family of secreted matricellular proteins are stress- and injury-induced mediators of cellular attachment dynamics and extracellular matrix protein production. Here we show that Thbs1, but not Thbs2, Thbs3 or Thbs4, induces lethal cardiac atrophy when overexpressed. Mechanistically

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