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Description
Purified anti-eIF-2A. eIF-2A was initially considered to be a eukaryotic functional counterpart of the prokaryotic translation initiation factor IF2, because it binds methionyl-tRNAi to 40 S subunits in a codon-dependent manner. But recent studies proved that eIF2-mediated pathway is far more efficient, and only eIF2 is able to form the 80S initiation complex on native globin mRNA. eIF2 is responsible for the loading of Met-tRNAi onto the ribosome in the majority of translation initiation events in eukaryotes, while eIF-2A is involved in the translation of a limited subset of mRNAs.Homologues of eIF-2A are found in a wide range of eukaryotic species, indicating that eIF-2A plays some conserved roles. eIF-2A was reported to be involved in antigen presentation by major histocompatibility complex (MHC) class I molecules. Some antigenic precursors are translated from CUG codons via an unknown mechanism, which is different from the conventional methionine-initiated mechanism. Ribosome profiling experiments also revealed that translation initiation at CUG or GUG codons is a common event in yeast and human, and is not limited to antigen presentation by MHC class I molecules. Under stress conditions, such as amino acid starvation, heat shock and viral infection, eIF-2A migrates from the nucleus to the cytoplasm, where it is utilized for the translation of alphavirus 26S mRNA and hepatitis C viral (HCV) mRNA. So eIF-2A is considered to be a tRNA-loading factor in unconventional translation initiation events, such as non-AUG translation initiation, and an alternative factor of eIF2 when the active eIF2 is limited.
Immunogen
Purified recombinant fragment of human eIF-2A (448-576 a.a.) expressed in E. coli.