Anti-EIF2S1 (Ab-51) antibody produced in rabbit

Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.

The eukaryotic translation initiation factor 2 subunit α (EIF2S1) gene codes for a heterotrimeric GTPase which is localized to the cytoplasm. The EIF2S1 gene is mapped to human chromosome 14q23.3.

Peptide sequence around aa. 49-53 (E-L-S-R-R), according to the protein EIF2S1.

EIF2S1 (eukaryotic translation initiation factor 2 subunit α) serves as an important enzyme in protein elongation during translation. EIF2S1 catalyses the translocation of peptidyl-tRNA from A site to P site in the ribosome. Phosphorylation by EF2 kinase, inactivates EIF2S1 followed by inhibition of protein synthesis. Upregulation of EIF2S1 gene is observed in malignant tumors, such as gastrointestinal cancer, lung adenocarcinoma, ovary cancer, soft-tissue sarcomas and hepatocellular carcinoma. The GTP-bound eIF2S1 protein is regarded as the active form and recruits initiator methionyl tRNA to 40S ribosomal subunit, one of the key step in translation initiation.

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Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol

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