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AB56276

Recombinant Human eIF4E protein

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(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

1 Images
SDS-PAGE - Recombinant Human eIF4E protein (AB56276)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human eIF4E protein (AB56276)

SDS Page analysis of ab56276

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

GST tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P06730

Animal free

No

Carrier free

No

Species

Human

Storage buffer

Constituents: 25% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.79% Tris HCl, 0.307% Glutathione, 0.00386% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00292% EDTA, 0.00174% PMSF

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"51 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P06730","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The eIF4E protein also known as the eukaryotic translation initiation factor 4E functions mainly in the initiation phase of mRNA translation. It plays a role by binding to the 7-methylguanylate cap structure at the 5’ end of mRNA facilitating ribosome assembly on mRNA. The molecular weight of eIF4E is approximately 25 kDa and it is ubiquitously expressed in various tissues across eukaryotic organisms. Additionally phosphorylation of eIF4E affects its activity and is an important post-translational modification.
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.

EIF4E has been linked to cancer and neurodegenerative conditions. In cancer overexpression of eIF4E leads to increased translation of oncogenes facilitating tumorigenesis. The mTOR pathway proteins like mTOR and 4EBP1 are often dysregulated in these cases. Conversely its role in neurological disorders involves the aberrant regulation of synaptic proteins like PSD95 impacting neuronal communication and function.

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).

Product protocols

Target data

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).
See full target information EIF4E

Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Science advances 10:eadq6342 PubMed39565848

2024

Hepatovirus translation requires PDGFA-associated protein 1, an eIF4E-binding protein regulating endoplasmic reticulum stress responses.

Applications

Unspecified application

Species

Unspecified reactive species

Takayoshi Shirasaki,Erik Lenarcic,Ichiro Misumi,Ling Xie,William G Fusco,Bryan Yonish,Anshuman Das,Hyejeong Kim,Craig E Cameron,Mélissa Léger-Abraham,Xian Chen,John M Cullen,Jason K Whitmire,You Li,Joseph A Duncan,Nathaniel J Moorman,Stanley M Lemon

Molecular reproduction and development 79:767-76 PubMed22968905

2012

The eIF4E repressor protein 4E-BP2 is merely truncated, despite 4E-BP1 degradation in the porcine uterine tissue during implantation.

Applications

Unspecified application

Species

Unspecified reactive species

Karin Wollenhaupt,Klaus-Peter Brüssow,Dirk Albrecht,Wolfgang Tomek

Molecular reproduction and development 78:895-905 PubMed21887718

2011

4E-BP1 degradation and eIF4E truncation occur spatially distinctly in the porcine uterine epithelia and are features of noninvasive implantation in the pig.

Applications

Unspecified application

Species

Unspecified reactive species

Karin Wollenhaupt,Kati Reinke,Klaus-Peter Brüssow,Wilhelm Kanitz,Wolfgang Tomek

The Biochemical journal 432:353-63 PubMed20854261

2010

Natural occurrence and physiological role of a truncated eIF4E in the porcine endometrium during implantation.

Applications

Unspecified application

Species

Unspecified reactive species

Karin Wollenhaupt,Kati Reinke,Klaus-Peter Brüssow,Dirk Albrecht,Ute Tiemann,Hans-Martin Seyfert,Wolfgang Tomek

Molecular reproduction and development 76:1208-19 PubMed19697362

2009

Analysis of mRNA associated factors during bovine oocyte maturation and early embryonic development.

Applications

Unspecified application

Species

Unspecified reactive species

Corinna Siemer,Tatjana Smiljakovic,Monika Bhojwani,Claus Leiding,Wilhelm Kanitz,Michal Kubelka,Wolfgang Tomek
View all publications

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