EIF5A Human
Description
Product Specs
Product Science Overview
Eukaryotic Translation Initiation Factor 5A (eIF5A) is a highly conserved protein found in eukaryotic cells. It plays a crucial role in the initiation and elongation phases of protein synthesis. The human recombinant form of eIF5A is particularly significant in research due to its involvement in various cellular processes and its potential therapeutic applications.
eIF5A is a small protein, approximately 17 kDa in size, composed of 157 amino acids . One of its most distinctive features is the presence of the unusual amino acid hypusine, which is formed post-translationally through the modification of a specific lysine residue . This modification is essential for the protein’s function and is unique to eIF5A and its homologs .
Initially identified as a translation initiation factor, eIF5A has since been found to play a role in translation elongation and termination as well . It binds between the exit (E) and peptidyl (P) sites of the ribosome, promoting the rescue of stalled ribosomes and facilitating the translation of polyproline-containing peptides . This function is critical for maintaining the efficiency and fidelity of protein synthesis.
eIF5A is involved in various physiological processes, including:
- Cell Proliferation and Differentiation: eIF5A is essential for cell growth and division, and its dysregulation is associated with cancer progression .
- Stress Response: It plays a role in cellular stress responses, including ischemic tolerance and metabolic adaptation .
- Immune Function: eIF5A is implicated in the differentiation and function of immune cells .
Due to its involvement in critical cellular processes, eIF5A is a potential target for therapeutic interventions. Its role in cancer progression makes it a candidate for anti-cancer drug development . Additionally, its involvement in stress responses suggests potential applications in treating conditions such as myocardial infarction and stroke .
