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Key Documents

SAB1403761

Sigma-Aldrich

Monoclonal Anti-EIF4EBP1 antibody produced in mouse

clone 1F7, purified immunoglobulin, buffered aqueous solution

Synonyme(s) :

4E-BP1, 4EBP1, BP-1, MGC4316, PHAS-I

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

1F7, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~39.09 kDa

Espèces réactives

human

Technique(s)

capture ELISA: suitable
indirect ELISA: suitable
western blot: 1-5 μg/mL

Isotype

IgG2aκ

Numéro d'accès NCBI

BC004459

Numéro d'accès UniProt

Q13541

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... EIF4EBP1(1978)

Description générale

This gene encodes one member of a family of translation repressor proteins. The protein directly interacts with eukaryotic translation initiation factor 4E (eIF4E), which is a limiting component of the multisubunit complex that recruits 40S ribosomal subunits to the 5′ end of mRNAs. Interaction of this protein with eIF4E inhibits complex assembly and represses translation. This protein is phosphorylated in response to various signals including UV irradiation and insulin signaling, resulting in its dissociation from eIF4E and activation of mRNA translation. (provided by RefSeq)

Immunogène

EIF4EBP1 (AAH04459, 1 a.a. ~ 118 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI

Actions biochimiques/physiologiques

The gene EIF4EBP1 (eukaryotic translation initiation factor 4E binding protein 1) encodes a translation repressor that interacts with eukaryotic translation initiation factor 4E (eIF4E). eIF4E is a multisubunit complex that recruits 40S ribosomal subunits to the 5′ end of mRNA. The interaction of the encoded binding protein with this complex inhibits translation. The phosphorylation of eIF4Ebp1 in response to stimuli such as, UV irradiation and insulin signaling, results in dissociation of this factor from the eIF4E complex, leading to initiation of translation of mRNA. The encoded protein participates in cell proliferation, apoptosis, invasion, and metastasis. It functions as an effector molecule in mTOR (mammalian target of rapamycin complex 1) signaling pathway that regulates protein synthesis. It is found to be overexpressed in hepatocellular carcinoma tissues and serves as a potential prognostic and therapeutic target.

Forme physique

Solution in phosphate buffered saline, pH 7.4

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism.
Gingras AC, et al.
Genes & Development, 13, 1422-1437 (1999)
High-resolution genomic and expression analyses of copy number alterations in HER2-amplified breast cancer.
Staaf J, et al.
Breast Cancer Research, 12(3) (2010)
EIF4EBP1 overexpression is associated with poor survival and disease progression in patients with hepatocellular carcinoma.
Cha YL, et al.
PLoS ONE, 10(2) (2015)
eIF4E binding protein 1 expression is associated with clinical survival outcomes in colorectal cancer.
Chao MW, et al.
Oncotarget, 6(27), 24092-24104 (2015)
Himalee Sabnis et al.
Journal of translational medicine, 12, 166-166 (2014-06-14)
Overall cure rates in acute myeloid leukemia (AML) continue to range between 60-65% with disease relapse being a major cause of mortality. The PI3K-Akt-mTOR kinase pathway plays a vital role in pro-survival signals within leukemic cells and inhibition of this
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