The alpha subunit of elongation factor-1 (EEF1A) is involved in the binding of aminoacyl-tRNAs to 80S ribosomes. During the process, GTP is hydrolyzed into GDP. To perform this function, EEF1A has domains that bind guanine nucleotides, 80S ribosomes, and aminoacyl-tRNAs. Also, EEF1A interacts with the beta subunit of EEF1 to exchange bound GDP for GTP. Multimolecular complexes involving the eukaryotic elongation factor 1A (eEF1A) have been suggested to play an important role in the channeling (vectorial transfer) of tRNA during protein synthesis (1) HIV-1 matrix protein (MA) was found to interact with elongation factor 1-alpha (EF1alpha), an essential component of the translation machinery that delivers aminoacyl-tRNA to ribosomes. The interaction between MA and EF1alpha impairs translation in vitro, a result consistent with a previously proposed model in which inhibition of translation by the accumulation of Gag serves to release viral RNA from polysomes, permitting the RNA to be packaged into nascent virions. (2) It has been identified that the translation elongation factor, eEF1A, and its guanine nucleotide exchange factor, eEF1Bbeta, as translationally controlled tumor protein (TCTP) -interacting partners. (3)

Gene synonym include CCS-3; CCS3; EE1A1; EEF-1; EEF1A; eEF1A-1; EF-Tu; EF1A; FLJ25721; GRAF-1EF; HNGC:16303; LENG7; MGC102687; MGC131894; MGC16224 and PTI1.

Recombinant GST-EF1α was expressed in a E.coli system and purified by an affinity column in combination with FPLC chromatography.
Research Use Only and not for Diagnostic purposes. Recombinant GST-EF1α can be used for protein-protein interaction assays.
The purified recombinant protein is greater than 90% homogeneous and contains no detectable protease, DNase and RNase activity.
1 unit equals 1 nanogram of purified protein.
0.5 mg/ml (in 1X dilution buffer A)
Buffer A; Tris, Glycerol, KCl, DTT, and EDTA

References:
1. Brands, J. H. et al., Europ. J. Biochem. 155: 167-171, 1986.
2. Cimarelli,A. et al., J. Virol. 73 (7), 5388-5401 (1999)
3. Cans,C., et al., Proc. Natl. Acad. Sci. U.S.A. 100 (24), 13892-13897 (2003)