4EBP1 Protein, Human, Recombinant (His Tag)

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4EBP1 Protein, Human, Recombinant (His Tag): Product Information

Purity
> 90 % as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Activity
Testing in progress
Protein Construction
A DNA sequence encoding the human 4EBP1 (NP_004086.1) (Ser 2-Ile 118) with a N-terminal polyhistidine tag was expressed.
Accession#
Expressed Host
E. coli
Species
Human
Predicted N Terminal
Met
Molecule Mass
The secreted recombinant human 4EBP1 comprises 124 amino acids with a predicted molecular mass of 13.4 kDa. It migrates as an approximately 19 kDa band in SDS-PAGE under reducing conditions.
Formulation
Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol
Please contact us for any concerns or special requirements.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

4EBP1 Protein, Human, Recombinant (His Tag): Images

4EBP1 Protein, Human, Recombinant (His Tag): Alternative Names

4E-BP1 Protein, Human; 4EBP1 Protein, Human; BP-1 Protein, Human; PHAS-I Protein, Human

4EBP1 Background Information

The translational suppressor eIF4E binding protein-1, 4E-BP1 functions as a key regulator in cellular growth, differentiation, apoptosis and survival. The Eif4ebp1 gene, encoding 4E-BP1, is a direct target of a transcription factor activating transcription factor-4 (ATF4), a master regulator of gene expression in stress responses. 4E-BP1 is characterized by its capacity to bind specifically to eIF4E and inhibit its interaction with eIF4G. Phosphorylation of 4E-BP1 regulates eIF4E availability, and therefore, cap-dependent translation, in cell stress. Binding of eIF4E to eIF4G is inhibited in a competitive manner by 4E-BP1. Phosphorylation of 4E-BP1 decreases the affinity of this protein for eIF4E, thus favouring the binding of eIF4G and enhancing translation. 4E-BP1 is important for beta-cell survival under endoplasmic reticulum (ER) stress. 4E-BP1 mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. Recently, 4E-BP1 was found to be a key factor, which converges several oncogenic signals, phosphorylates the molecules, and drives the downstream proliferative signals. Recent studies showed that high expression of phosphorylated 4E-BP-1 (p-4E-BP1) is associated with poor prognosis, tumor progression, or nodal metastasis in different human cancers.
Full Name
eukaryotic translation initiation factor 4E binding protein 1
References
  • Azar R, et al. (2008) Phosphatidylinositol 3-kinase-dependent transcriptional silencing of the translational repressor 4E-BP1. Cell Mol Life Sci. 65(19): 3110-7.
  • Tominaga R, et al. (2010) The JNK pathway modulates expression and phosphorylation of 4E-BP1 in MIN6 pancreatic beta-cells under oxidative stress conditions. Cell Biochem Funct. 28(5): 387-93.
  • Ayuso MI, et al. (2010) New hierarchical phosphorylation pathway of the translational repressor eIF4E-binding protein 1 (4E-BP1) in ischemia-reperfusion stress. J Biol Chem. 285(45): 34355-63.
  • Targeting mTOR to overcome epidermal growth factor receptor tyrosine kinase inhibitor resistance in non-small cell lung cancer cells
    Author
    Fei, SJ;Zhang, XC;Dong, S;Cheng, H;Zhang, YF;Huang, L;Zhou, HY;Xie, Z;Chen, ZH;Wu, YL;
    Year
    2013
    Journal
    PLoS ONE
    Application
    substrate
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