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Human EIF-5A / EIF5 Protein (GST Tag)

EIF-5,EIF-5A

Catalog Number P13932-H09E
Organism Species Human
Host E. coli
Synonyms EIF-5,EIF-5A
Molecular Weight The recombinant human EIF5 /GST chimera consists of 384 amino acids and has a predicted molecular mass of 44.1 kDa. It migrates as an approximately 38-43 KDa band in SDS-PAGE under reducing conditions.
predicted N Met
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the mature form of human EIF5 (P55010) (Met1-Asp150) was fused with the GST tag at the N-terminus.
Bio-activity
Research Area Cancer |Signal transduction |Cytoskeleton / ECM |Cell Adhesion |Integrin |Beta integrin |
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background EIF-5A, also known as EIF5, functions in start site selection as a GTPase accelerating protein (GAP) for the eukaryotic translation initiation factor (eIF) 2•GTP•tRNA ternary complex within the ribosome-bound pre-initiation complex. In protein synthesis initiation, eIF2 functions in its GTP-bound state to deliver initiator methionyl-tRNA to the small ribosomal subunit and is necessary for protein synthesis in all cells. EIF-5A stabilizes the binding of GDP to eIF2 and is therefore a bi-functional protein that acts as a GDP dissociation inhibitor (GDI). EIF-5A also interacts with eIF1 and eIF3 and binds the eIF2-GTP/Met-tRNA ternary complex along with the 40S ribosome subunit.
Reference
  • Si K, et al. (1996) Charactatierizon of multiple mRNAs that encode mammalian translation initiation factor 5 (eIF-5). J Biol Chem. 71(28):16934.
  • Das S, et al. (1998) Specific interaction of eukaryotic translation initiation factor 5 (eIF5) with the beta-subunit of eIF2. J Biol Chem. 272(50):31712-8.
  • Conte MR, et al. (2006) Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors. Biochemistry. 45(14):4550-8.