Anti-EIF4EBP1 (Ab-45) antibody produced in rabbit

4E-BP1 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.

The gene EIF4EBP1 (eukaryotic translation initiation factor 4E binding protein 1) is mapped to human chromosome 8p12.

Peptide sequence around aa. 43-47 (S-T-T-P-G), according to the protein EIF4EBP1.

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.

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Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol