- CITATIONS: 0
|Application ||WB, IHC-P, E|
|Other Accession||P48597, P63074, P29338, P63073, Q9N0T5, Q9DFS6|
|Predicted||Zebrafish, Bovine, Mouse, Rabbit, Rat, Xenopus|
|Calculated MW||25097 Da|
|Antigen Region||32-61 aa|
|Other Names||Eukaryotic translation initiation factor 4E, eIF-4E, eIF4E, eIF-4F 25 kDa subunit, mRNA cap-binding protein, EIF4E, EIF4EL1, EIF4F|
|Target/Specificity||This EIF4E antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 32-61 amino acids from the N-terminal region of human EIF4E.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|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.
eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4E is also known to interact with other partners. The interaction with EIF4ENIF1 mediates the import into the nucleus. Nonphosphorylated EIF4EBP1, EIF4EBP2 and EIF4EBP3 compete with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. Rapamycin can attenuate insulin stimulation, mediated by FKBPs. this gene also interacts mutually exclusive with EIF4A1 and EIF4A2.
Rychlik,W., J. Biol. Chem. 262 (22), 10434-10437 (1987)
Dorfman,J., Genomics 9 (4), 785-788 (1991)
Pelletier,J., Genomics 10 (4), 1079-1082 (1991)
Whalen,S.G., J. Biol. Chem. 271 (20), 11831-11837 (1996)
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