Recombinant Human eIF4E protein (ab56276)

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SDS-PAGE - Recombinant Human eIF4E protein (ab56276)

    Key features and details

    • Expression system: Escherichia coli
    • Purity: > 90% SDS-PAGE
    • Tags: GST tag N-Terminus
    • Suitable for: Functional Studies, SDS-PAGE

    Description

    • Product name

      Recombinant Human eIF4E protein
      See all eIF4E proteins and peptides

    • Purity

      > 90 % SDS-PAGE.

    • Expression system

      Escherichia coli

    • Protein length

      Full length protein

    • Animal free

      No

    • Nature

      Recombinant

      • Species

        Human

      • Predicted molecular weight

        51 kDa including tags

      • Tags

        GST tag N-Terminus

    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.

    • Applications

      Functional Studies

      SDS-PAGE

    • Form

      Liquid
    • Concentration information loading...

    Preparation and Storage

    • 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 (glycerin, glycerine), 0.87% Sodium chloride

    General Info

    • Alternative names

      • AUTS19
      • CBP
      • eIF 4E
      • EIF 4F
      • eIF 4F 25 kDa subunit
      • eIF-4E
      • eIF-4F 25 kDa subunit
      • eIF4E
      • EIF4E1
      • EIF4EL1
      • EIF4F
      • Eukaryotic translation initiation factor 4 E
      • Eukaryotic translation initiation factor 4E
      • Eukaryotic translation initiation factor 4E like 1
      • IF4E_HUMAN
      • Messanger RNA Cap Binding Protein eIF 4E
      • MGC111573
      • mRNA cap binding protein
      • mRNA cap-binding protein
      see all

    • Function

      Its 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.

    • 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.
    • Information by UniProt

    Images

    • SDS-PAGE - Recombinant Human eIF4E protein (ab56276)
      SDS-PAGE - Recombinant Human eIF4E protein (ab56276)
      SDS Page analysis of ab56276

    Protocols

    To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.

    Click here to view the general protocols

    References (4)

    Publishing research using ab56276? Please let us know so that we can cite the reference in this datasheet.

    ab56276 has been referenced in 4 publications.

    • 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). 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). PubMed: 21887718
    • Wollenhaupt K  et al. Natural occurrence and physiological role of a truncated eIF4E in the porcine endometrium during implantation. Biochem J 432:353-63 (2010). PubMed: 20854261
    • Siemer C  et al. Analysis of mRNA associated factors during bovine oocyte maturation and early embryonic development. Mol Reprod Dev 76:1208-19 (2009). PubMed: 19697362

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