|Application ||WB, IHC|
|Calculated MW||69151 Da|
|Other Names||Eukaryotic translation initiation factor 4B, eIF-4B, EIF4B|
|Target/Specificity||A synthetic peptide corresponding to residues on the C-terminus of human Eif4b 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-4B Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'- terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.|
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Provided below are standard protocols that you may find useful for product applications.
Eukaryotic protein synthesis initiation factor 4B (eIF-4B) is an 80,000 dalton polypeptide which is essential for the binding of mRNA to ribosomes. The amino-terminal domain of eIF-4B contains a consensus RNA binding domain present in a number of other RNA binding proteins (1). It contains a ribonucleoprotein consensus sequence (RNP-CS)/RNA recognition motif (RRM). Deletions which remove this region abolish the ability of eIF-4B to cooperate with eIF-4A in RNA binding and the ability to stimulate the helicase activity of eIF-4A. Results indicate that the carboxy-terminal RNA-binding region of eIF-4B is essential for eIF-4B function and is distinct from the RNP-CS/RRM (2). eIF4F binds to the mRNA cap structure and, in combination with eIF4B, is believed to unwind the secondary structure in the 5' untranslated region to facilitate ribosome binding. It has been suggested that eIF4B participates in mRNA-ribosome binding by acting as an intermediary between the mRNA and eIF3, via a direct interaction with the p170 subunit of eIF3 (3).
1. Milburn SC, et al. EMBO J, 9(9):2783-90, 1990
2. Methot N, et al. Mol Cell Biol 14(4):2307-16, 1994
3. Methot N, et al. Mol Cell Biol 16(10):5328-34, 1996
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