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Merck
모든 사진(2)

Key Documents

SAB4200148

Sigma-Aldrich

Anti-Derlin-1 antibody, Mouse monoclonal

clone Derlin1-1, purified from hybridoma cell culture

동의어(들):

Anti-DER-1, Anti-DERL1, Anti-Der1-like domain family, member 1

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About This Item

UNSPSC 코드:
12352203
NACRES:
NA.41

생물학적 소스

mouse

결합

unconjugated

항체 형태

purified from hybridoma cell culture

항체 생산 유형

primary antibodies

클론

Derlin1-1, monoclonal

분자량

antigen ~22 kDa

종 반응성

mouse, bovine, rat, canine, human

농도

~1.0 mg/mL

기술

immunoprecipitation (IP): suitable
western blot: 2-4 μg/mL using whole extracts of mouse NIH-3T3 or rat NRK cells

동형

IgG1

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

human ... DERL1(79139)
mouse ... Derl1(67819)
rat ... Derl1(362912)

일반 설명

Derlin-1 (DERL1) gene with seven exons is mapped to human chromosome 8q24.13. DERL1 is an endoplasmic reticulum (ER) membrane protein and is a key component of p97 ATPase complex.
Monoclonal Anti-Derlin-1 (mouse IgG1 isotype) is derived from the hybridoma Derlin1-1 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide. Derlin-1, a human homolog of yeast Der1p, is a membrane protein.

면역원

synthetic peptide corresponding to the C-terminal region of human Derlin-1, conjugated to KLH. The corresponding sequence is identical in mouse, rat, monkey, pig, bovine and canine.

애플리케이션

Monoclonal Anti-Derlin-1 antibody produced in mouse has been used in western blotting and immunoprecipitation.

생화학적/생리학적 작용

Derlin-1 is a multifunctional protein. It acts as a key growth factor-responsive endothelial antigen that stimulates endothelial cell survival and growth. The encoded protein might also be implicated in endoplasmic reticulum stress in neuronal cells in Alzheimer′s disease.Elevated expression of DERL1 has been observed in various types of cancer including bladder and lung cancer. Additionally, overexpression of the gene is also associated with the development of colon cancers. Thus, DERL1 can be used as a potential therapeutic target for colon cancer. DERL1 plays an essential role in proteostasis regulation of potassium channel (KATP)channels.
Derlin-1 is required for the dislocation of misfolded proteins from the endoplasmic reticulum (ER) lumen to the cytosol. It interacts with peptide:N-glycosidase (PNGase), a deglycosylating enzyme, bringing it close to misfolding dislocating glycoproteins. Derlin-1 interacts with VIMP (VCP-interacting membrane protein), a membrane protein that recruits p97 and its cofactors, ubiquitin recognition factor in ER associated degradation 1 (Ufd1) and nuclear protein localization 4 (Npl4). Derlin-1 and VIMP form a membrane protein complex that serves as a receptor for p97.

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

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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문서 라이브러리 방문

Role of Derlin-1 protein in proteostasis regulation of ATP-sensitive potassium channels.
Wang F
The Journal of Biological Chemistry, 287, 10482-10493 (2012)
Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation
Oda Y, et al.
The Journal of cell biology, 172, 383-393 (2006)
Derlin-1 is overexpressed in human colon cancer and promotes cancer cell proliferation.
Tan X
Molecular and Cellular Biochemistry, 408, 205-213 (2015)
Derlin-1-immunopositive inclusions in patients with Alzheimer's disease.
Honjo Y
Neuroreport, 23, 611-615 (2012)
Ubiquitin-Dependent Intramembrane Rhomboid Protease Promotes ERAD of Membrane Proteins
Fleig L
Molecular Cell, 47, 558-569 (2012)

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