Recombinant Human eIF4E protein
Be the first to review this product! Submit a review
|
(5 Publications)
Recombinant Human eIF4E protein is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
EIF4EL1, EIF4F, EIF4E, Eukaryotic translation initiation factor 4E, eIF-4E, eIF4E, eIF-4F 25 kDa subunit, mRNA cap-binding protein
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human eIF4E protein (AB56276)
SDS Page analysis of ab56276
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
EIF4E regulates gene expression at the translational level and is a part of the eIF4F complex which also includes eIF4A and eIF4G. This complex is essential for the recruitment of ribosomes to the mRNA impacting the rate of protein synthesis. Changes in eIF4E levels can alter the translational efficiency of specific mRNAs thereby influencing cellular growth and proliferation.
Pathways
EIF4E directly involves in the mTOR signaling pathway which regulates cell growth proliferation and survival. Within this pathway eIF4E interacts with proteins such as 4EBP1 which binds to eIF4E and inhibits its function in the absence of phosphorylation by mTOR. This interaction illustrates the control mechanism of protein synthesis under different cellular conditions connecting it to various signaling cascades.
Specifications
Form
Liquid
General info
Function
Acts in the cytoplasm to initiate and regulate protein synthesis and is required in the nucleus for export of a subset of mRNAs from the nucleus to the cytoplasm which promotes processes such as RNA capping, processing and splicing (PubMed : 11606200, PubMed : 22578813, PubMed : 22684010, PubMed : 24335285, PubMed : 29987188). Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). This protein recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (PubMed : 16271312, PubMed : 22578813). Together with EIF4G1, antagonizes the scanning promoted by EIF1-EIF4G1 and is required for TISU translation, a process where the TISU element recognition makes scanning unnecessary (PubMed : 29987188). In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (PubMed : 24335285). Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression : in the complex, EIF4E mediates the binding to the mRNA cap (By similarity). Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis (By similarity). In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation (PubMed : 24335285). May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development (By similarity). As well as its roles in translation, also involved in mRNA nucleocytoplasmic transport (By similarity). Its role in mRNA export from the nucleus to the cytoplasm relies on its ability to bind the m7G cap of RNAs and on the presence of the 50-nucleotide EIF4E sensitivity element (4ESE) in the 3'UTR of sensitive transcripts (By similarity). Interaction with the 4ESE is mediated by LRPPRC which binds simultaneously to both EIF4E and the 4ESE, thereby acting as a platform for assembly for the RNA export complex (By similarity). EIF4E-dependent mRNA export is independent of ongoing protein or RNA synthesis and is also NFX1-independent but is XPO1-dependent with LRPPRC interacting with XPO1 to form an EIF4E-dependent mRNA export complex (By similarity). Alters the composition of the cytoplasmic face of the nuclear pore to promote RNA export by reducing RANBP2 expression, relocalizing nucleoporin NUP214 and increasing expression of RANBP1 and RNA export factors DDX19 and GLE1 (By similarity). Promotes the nuclear export of cyclin CCND1 mRNA (By similarity). Promotes the nuclear export of NOS2/iNOS mRNA (PubMed : 23471078). Promotes the nuclear export of MDM2 mRNA (PubMed : 22684010). Promotes the export of additional mRNAs, including others involved in the cell cycle (By similarity). In the nucleus, binds to capped splice factor-encoding mRNAs and stimulates their nuclear export to enhance splice factor production by increasing their cytoplasmic availability to the translation machinery (By similarity). May also regulate splicing through interaction with the spliceosome in an RNA and m7G cap-dependent manner (By similarity). Also binds to some pre-mRNAs and may play a role in their recruitment to the spliceosome (By similarity). Promotes steady-state capping of a subset of coding and non-coding RNAs by mediating nuclear export of capping machinery mRNAs including RNMT, RNGTT and RAMAC to enhance their translation (By similarity). Stimulates mRNA 3'-end processing by promoting the expression of several core cleavage complex factors required for mRNA cleavage and polyadenylation, and may also have a direct effect through its interaction with the CPSF3 cleavage enzyme (By similarity). Rescues cells from apoptosis by promoting activation of serine/threonine-protein kinase AKT1 through mRNA export of NBS1 which potentiates AKT1 phosphorylation and also through mRNA export of AKT1 effectors, allowing for increased production of these proteins (By similarity).
Sequence similarities
Belongs to the eukaryotic initiation factor 4E family.
Post-translational modifications
Phosphorylation increases the ability of the protein to bind to mRNA caps and to form the eIF4F complex (PubMed:11154262, PubMed:3112145, PubMed:7590282, PubMed:7665584, PubMed:7782323, PubMed:8505316, PubMed:9878069). Phosphorylation also enhances its mRNA transport function (By similarity). Phosphorylation at Ser-209 is not essential for protein synthesis (PubMed:11606200, PubMed:12138083).
Target data
Publications (5)
Recent publications for all applications. Explore the full list and refine your search
Science advances 10:eadq6342 PubMed39565848
2024
Applications
Unspecified application
Species
Unspecified reactive species
Molecular reproduction and development 79:767-76 PubMed22968905
2012
Applications
Unspecified application
Species
Unspecified reactive species
Molecular reproduction and development 78:895-905 PubMed21887718
2011
Applications
Unspecified application
Species
Unspecified reactive species
The Biochemical journal 432:353-63 PubMed20854261
2010
Applications
Unspecified application
Species
Unspecified reactive species
Molecular reproduction and development 76:1208-19 PubMed19697362
2009
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com