Rabbit Anti-Hypusine Recombinant Antibody (clone Hpu98); Fab Fragment (CAT#: PFBL-577)

Wątor, Elżbieta, et al. "Cryo-EM structure of human eIF5A-DHS complex reveals the molecular basis of hypusination-associated neurodegenerative disorders." Nature Communications 14.1 (2023): 1698. https://doi.org/10.1038/s41467-023-37305-2

This research presents a groundbreaking structural analysis of the eukaryotic translation factor 5A (eIF5A) and deoxyhypusine synthase (DHS) complex, revealing the molecular mechanism behind hypusination - a unique post-translational modification essential for overcoming ribosome stalling at polyproline sequences. Using cryo-electron microscopy, the researchers determined the structure of the human eIF5A-DHS complex at 2.8 Å resolution, complemented by a crystal structure of DHS trapped in the key reaction transition state. The study demonstrates how the binding of eIF5A unmasks the DHS active site, allowing the transfer of the 4-aminobutyl moiety from spermidine to eIF5A's lysine-50 residue, and reveals the conformational changes in key residues like Trp327 that facilitate this reaction.
Creative Biolabs provided the rabbit FabHpu98 antibody, which was crucial for detecting deoxyhypusination in the functional assays. This antibody enabled researchers to assess the hypusination capacity of various DHS variants, including clinically relevant mutants associated with neurodegenerative disorders. By allowing specific detection of the deoxyhypusinated eIF5A, the FabHpu98 antibody helped establish how disease-associated DHS variants impair complex formation and hypusination efficiency, providing valuable insights into the molecular basis of these rare neurodevelopmental conditions.