Based on the excellent High-Affi™ technology, Creative Biolabs has the capability of providing highly specific pan anti-crotonyllysine antibody and site-specific anti-crotonylated protein antibodies. These antibodies are produced by immunizing mice with crotonylated BSA or KLH or with a synthetic crotonyl peptide and purified by affinity chromatography. They do not cross-react with non-modified lysine residues, unmodified peptides, acetylated peptides, and other acylated peptides.
Crotonylation of lysine is a newly-identified post-translational modification which is widely distributed from prokaryotes to eukaryotes. Modified proteomic approaches have proved that lysine crotonylation is an evolutionarily conserved PTM in living nature. It has shown that both histones and non-histone substrates can be crotonylated on lysines.
Crotonylation and Acetylation
Crotonylation is a reversible and dynamic process which is catalyzed by crotonyltransferase p300, a coactivator that has both crotonyltransferase and acetyltransferase activities. Incredible, histone lysine crotonylation catalyzed by p300 directly stimulates gene transcription to a greater degree than histone lysine acetylation. But, the regulated mechanisms that govern acetylation versus crotonylation remain unclear.
There is evidence that the evolutionarily conserved YEATS domain family is the readers of crotonyllysine. The YEATS domain of AF9 performs higher binding affinity for crotonylated lysine over acetylated lysine directly, which links histone crotonylation to active transcription. The distinct structure and genomic localization of crotonylation suggest that it is different from acetylation in functions.
Fig. 1 Intracellular crotonyl-COA stimulates transcription through p300-catalyzed histone crotonylation. (Sabari Benjamin R, et al. 2015)
Crotonylation is regulated by the concentration of crotonyl-CoA
The levels of crotonylation are regulated by the cellular concentration of crotonyl-CoA. In a cell model of transcriptional activation, increasing the concentration of crotonyl-CoA leads to enhanced gene expression, instead get the diminished gene expression by decreasing the cellular concentration of crotonyl-CoA. Lysine crotonylation may play more important roles in various cellular pathophysiological processes by affecting the structure of chromatin and PTM pathways.
Functions of crotonylation
Crotonylation of the H3 Lys122 reduced the histone-DNA association by impeding the formation of the hydrogen bond with the DNA backbone and then promoted gene transcription. Specifically, in male germinal cells, crotonylation was taken place immediately following meiosis. Lysine crotonylation is enriched on sex chromosomes and specifically marks testis-specific genes, including a significant proportion of X-linked genes that escape sex chromosome inactivation in haploid cells (Tan M, et al. 2011). Researchers also found that the crotonylation of histone in kidney tissue was increased during acute kidney injury (AKI) and proved that this increasing lysine crotonylation might have a beneficial effect on AKI. As crotonylation was discovered lately, more efforts need to be put into research to make the function of crotonylation more clearly.
Fig. 2. Lysine crotonylation is enriched on sex chromosomes. (Tan M, et al. 2011)
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