Recombinant Human eIF4E protein (ab56276)
- Datasheet
- References (4)
- Protocols
Overview
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Product nameRecombinant Human eIF4E protein
See all eIF4E proteins and peptides -
Protein lengthFull length protein
Description
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NatureRecombinant
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SourceEscherichia coli
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Amino Acid Sequence
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SpeciesHuman
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Molecular weight51 kDa including tags
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TagsGST tag N-Terminus
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab56276 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Functional Studies
SDS-PAGE
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Purity> 90 % SDS-PAGE.
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FormLiquid
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 7.50
Constituents: 0.0038% EGTA, 0.00174% PMSF, 0.00385% DTT, 0.79% Tris HCl, 0.00292% EDTA, 25% Glycerol, 0.87% Sodium chloride
General Info
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Alternative names
- AUTS19
- CBP
- eIF 4E
see all -
FunctionIts translation stimulation activity is repressed by binding to the complex CYFIP1-FMR1 (By similarity). Recognizes and binds the 7-methylguanosine-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. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates the binding to the mRNA cap.
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Sequence similaritiesBelongs to the eukaryotic initiation factor 4E family.
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Post-translational
modificationsPhosphorylation increases the ability of the protein to bind to mRNA caps and to form the eIF4F complex. - Information by UniProt
Images
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SDS-PAGE - Recombinant Human eIF4E protein (ab56276)SDS Page analysis of ab56276
Datasheets and documents
References
This product has been referenced in:
- Wollenhaupt K et al. The eIF4E repressor protein 4E-BP2 is merely truncated, despite 4E-BP1 degradation in the porcine uterine tissue during implantation. Mol Reprod Dev 79:767-76 (2012). Read more (PubMed: 22968905) »
- Wollenhaupt K et al. 4E-BP1 degradation and eIF4E truncation occur spatially distinctly in the porcine uterine epithelia and are features of noninvasive implantation in the pig. Mol Reprod Dev 78:895-905 (2011). Read more (PubMed: 21887718) »
