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Merck
모든 사진(2)

Key Documents

E4781

Sigma-Aldrich

Anti-eRF3a/GSPT1 antibody produced in rabbit

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

동의어(들):

Anti-Eukaryotic Release Factor 3a, Anti-G1 to S phase transition 1, Anti-GST1, homolog of yeast

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About This Item

MDL number:
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 76.5 kDa

종 반응성

human

포장

antibody small pack of 25 μL

농도

~1 mg/mL

기술

immunoprecipitation (IP): 1-2 μg using HeLa cell lysates
indirect immunofluorescence: 5-10 μg/mL using paraformadehyde-fixed HeLa cells
western blot: 0.5-1 μg/mL using HeLa cell lysates

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

human ... GSPT1(2935)
mouse ... Gspt1(14852)
rat ... Gspt1(24420)

일반 설명

Eukaryotic release factor 3 a (eRF3a) is encoded by the gene G1 to S phase transition 1 (GSPT1) in humans. The eRF3a/GSPT1 exon 1 is a translation termination protein characterized with a tri-nucleotide GGC repeat coding for a polyglycine expansion in the amino-terminal end.

면역원

synthetic peptide corresponding to amino acids 190-204 of human eRF3a/GSPT1, conjugated to KLH via a C-terminal added cysteine residue. The sequence is conserved in human, rat, and mouse.

애플리케이션

Anti-eRF3a/GSPT1 antibody produced in rabbit has been used in immunoprecipitation, indirect immunofluorescence and western blotting.

생화학적/생리학적 작용

Eukaryotic release factor 3 a (eRF3a) is proteolytically processed into an IAP (Inhibitors of Apoptosis Proteins)-binding protein. Processed eRF3a interacts with IAPs and can promote caspase activation, IAP ubiquitination and apoptosis. The IAP binding motif is exposed only after proteolytic cleavage of a 69-residue leader sequence. eRF3a also affects mRNA stability and translation initiation by interacting with Poly(A)-binding protein (PABP) and the surveillance factor Upf1.
Eukaryotic release factor 3a (eRF3a) is a translation termination protein that is encoded by G1 to S phase transition 1 gene (GSPT1) in humans. The eRF3a/GSPT1 exon 1 contains a tri-nucleotide GGC repeat coding for a polyglycine expansion in the N-terminal of the protein. It is associated with protein translation as a regulator of apoptosis signal-regulating kinase 1 (ASK1). GSPT1 interacts with ASK1 and enhances ASK1-induced apoptotic activity by activating caspase-3. It plays a novel role in the regulation of ASK1-mediated apoptosis. GSPT1 is found to be up-regulated in various human cancers and is considered as a potential proto-oncogene.

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)


시험 성적서(COA)

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문서 라이브러리 방문

Calpain mediates processing of the translation termination factor eRF3 into the IAP-binding isoform p-eRF3
Hashimoto, Y, et al.
Febs Letters, 589 (2015)
The GTP-binding Release Factor eRF3 as a Key Mediator Coupling Translation Termination to mRNA Decay
Kobayashi T, et al.
The Journal of Biological Chemistry, 279 (2004)
The GTP-binding Release Factor eRF3 as a Key Mediator Coupling Translation Termination to mRNA Decay
Kobayashi T, et al.
Test, 279 (2004)
The GTP-binding Release Factor eRF3 as a Key Mediator Coupling Translation Termination to mRNA Decay
Kobayashi T, et al.
The Journal of biological chemistry, 279 (2004)
GGCn polymorphism of eRF3a/GSPT1 gene and breast cancer susceptibility
Miri M, et al.
Medical Oncology (Northwood, London, England), 29 (2012)

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