**Background of EIF5A Antibodies**
Eukaryotic translation initiation factor 5A (EIF5A), initially identified as a translation initiation factor, is now recognized to play a broader role in mRNA translation elongation, particularly for polyproline-rich sequences. A defining feature of EIF5A is its unique post-translational modification called hypusination, where a spermidine-derived hypusine residue is enzymatically added to a conserved lysine. This modification, catalyzed by deoxyhypusine synthase (DHPS) and deoxyhypusine hydroxylase (DOHH), is critical for EIF5A’s functional activation. EIF5A exists in two isoforms, EIF5A1 (ubiquitously expressed) and EIF5A2 (tissue-specific, often linked to cancer), both implicated in cellular processes like proliferation, apoptosis, and stress responses.
Antibodies targeting EIF5A are essential tools for studying its expression, localization, and hypusination status. They enable detection via techniques like Western blotting, immunofluorescence, and immunohistochemistry. Specific antibodies may distinguish between isoforms or hypusinated/non-hypusinated forms, aiding research into diseases such as cancer, neurodegenerative disorders, and viral infections, where EIF5A dysregulation is observed. For example, EIF5A2 overexpression correlates with tumor progression, while hypusination defects are linked to neurodevelopmental conditions.
Researchers must validate EIF5A antibodies for specificity, as cross-reactivity between isoforms or unmodified/modified forms can lead to inaccurate interpretations. These antibodies are pivotal in elucidating EIF5A’s multifaceted roles in health and disease.