|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||25097 Da|
|Other Names||Eukaryotic translation initiation factor 4E, eIF-4E, eIF4E, eIF-4F 25 kDa subunit, mRNA cap-binding protein, EIF4E, EIF4EL1, EIF4F|
|Target/Specificity||A synthetic peptide corresponding to residues surrounding Serine 209 of human eIF4E was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||eIF-4E Antibody Phospho (pS209) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Cellular Location||Cytoplasm, P-body. Cytoplasm|
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Provided below are standard protocols that you may find useful for product applications.
eIF-4E is a eukaryotic translation initiation factor involved in directing ribosomes to the cap structure of mRNAs. It exists in two forms: as a free form (25 kDa) and as part of a multi-protein complex eIF-4F (1). eIF-4E appears to be the least abundant of the initiation factors and acts as a rate-limiting step of initiation (2). Since translation is regulated by phosphorylation, eIF-4E phosphorylation at Ser 209 by MAPK signal-integrating kinase 1 (Mnk1) and kinase 2 (Mnk2) may directly regulate the rate of protein synthesis initiation (3). There is also evidence that eIF-4E can function as an oncogene (4-5)
1. Rychlik, et al Proc. Nat. Acad. Sci. 84: 945-949, 1987.
2. Rhoads, R. E., Joshi-Barve, S., and Rinker-Schaeffer, C.(1993) Prog. Nucleic Acids Res. Mol. Biol.46, 183-219
3. Gert C. Scheper, Nick A. Morrice, Miranda Kleijn and Christopher G. Proud Molec. Cell. Biol.; February 2001, p. 743-754, Vol. 21, No. 3
4. Jone et al. Molec. Cell. Biol. 16: 4754-4764, 1996.
5. Wendel et al. Nature 428: 332-337, 2004.
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