Anti-Crotonyllysine Mouse mAb

Primary Antibodies

Ambient temperature

Multiple

Post-Translational Modificaiton

Lysine crotonylation is a newly-identified histone post-translational modification that has come to light through integrated proteomic approaches and elaborate biochemistry analyses. Lysine crotonylation has been found to be evolutionarily conserved across multiple species, spanning both prokaryotes and eukaryotes, and occurs in a wide range of proteins, incuding histones and non-histone substrates. The unique structure and genomic localization of lysine crotonylation suggest that it is mechanistically and functionally different from lysine acetylation. Given the revealed roles of lysine crotonylation in spermatogenesis, the novel modification may play important roles in multiple cellular pathophysiological processes by exerting its effects on chromatin structure and epigenetic pathways.

Anti-Crotonyllysine Mouse mAb detects proteins with crotonylated lysine residues. This pan antibody recognizes crotonylated lysine independent of its surrounding sequences.

Crotonyl

Crotonylated lysine peptides

Lysine crotonylation is a newly-identified histone post-translational modification by integrated proteomic approaches and elaborate biochemistry analyses. It has been shown that lysine crotonylation is an evolutionarily conserved PTM in multiple species of both prokaryotes and eukaryotes in a wide range of proteins, both in histones and non-histone substrates. The unique structure and genomic localization of lysine crotonylation suggest that it is mechanistically and functionally different from lysine acetylation. Given the revealed roles of lysine crotonylation in spermatogenesis, the novel modification may play important roles in multiple cellular pathophysiological processes by effecting chromatin structure and epigenetic pathways.