HIST1H3A (Histone Cluster 1 H3 Family Member A) is a core component of nucleosomes, essential for DNA packaging and transcriptional regulation . The 2-hydroxyisobutyryl modification at lysine 14 (K14hib) alters chromatin structure, influencing gene activation or repression. Unlike acetylation, Khib introduces bulkier acyl groups, which may uniquely affect protein interactions .
The antibody enables detection of Khib in:
Cancer: Khib is elevated in pancreatic cancer (PC) and correlates with proliferation and metastasis. Inhibition of Khib via Tip60 (a Khib "writer") suppressor MG149 reduces PC cell viability and invasion .
Metabolic Regulation: Khib-modified proteins are enriched in metabolic pathways (e.g., glycolysis, TCA cycle), suggesting roles in cellular energy balance .
Cross-Reactivity: Rigorous validation minimizes off-target binding. For example, Khib antibodies show no reactivity with unmodified or acetylated H3K14 peptides .
Functional Studies: In PC, antibody-based profiling identified 10,367 Khib sites across 2,325 proteins, highlighting its utility in large-scale proteomic analyses .
Khib in Cancer: Global Khib levels are elevated in pancreatic tumors. Knockdown experiments using MG149 reduced Khib, suppressing PC cell migration and invasion by >50% .
Structural Impact: Khib’s steric effects may compete with acetylation for lysine residues, creating distinct chromatin states .