Creative Biolabs offers highly specific and sensitive pan anti-butyryllysine antibodies and site-specific anti-butyrylated protein antibodies based on our excellent High-Affi™ technology. These antibodies are produced by immunizing mice with butyrylated BSA or KLH or with a synthetic butyryl peptide and purified by affinity chromatography. They do not cross-react with unmodified peptides, acetylated peptides, and other acylated peptides.
Butyrylation is a newly identified post-translational modification on lysine. With the help of integrated proteomics and biochemical techniques, lysine butyrylation has been well demonstrated in both prokaryotes and eukaryotes in wide ranges of proteins including histones and non-histone substrates. Study results also proved that histone lysine butyrylation is an evolutionarily conserved PTM in eukaryotic cells, as many modified sites can repeatedly be found both in mouse tissues and human cells.
Histone substrates and modified sites:
H2B: lys5, lys12, lys15, lys20, lys23
H3: lys9, lys18, lys23, lys27, lys115
H4: lys5, lys8, lys12
Non-histone substrates: p53, p300, and CREB-binding protein
Butyrylation of lysine is structurally similar to lysine acetylation and lysine propionylation. In regulating process, it is also reversible and dynamic. Histone acetyltransferases that catalyze acetylation can also catalyze butyrylation of lysine. This hypothesized that histone deacetylases (HDACs), which remove lysine acetylation, also remove lysine butyrylation. Mass spectrometry results show that many butyrylated sites are also the acetylated sites. This indicates that lysine butyrylation competes with lysine acetylation in some conditions. Recently discovered histone lysine butyrylation increase the functional diversity of nucleosomes well beyond acetylation. For example, in the context of sperm cell differentiation, histone butyrylation competes with acetylation, especially at H4K5, to prevent the binding of Brdt, a bromodomain-containing protein mediating stage-specific gene expression programs and post-meiotic chromatin reorganization. Additionally, H4 K5K8 butyrylation also marks retarded histone removal during late spermatogenesis.
Fig. 1. Histone butyrylation competes with acetylation in the context of sperm cell differentiation.
Recently, researchers identified increased protein lysine butyrylation in short-chain acyl-CoA dehydrogenase (SCAD) deficient mice as a result of the accumulation of butyryl-CoA. Since lysine acylation can greatly impact protein function, aberrant lysine acylation in inherited disorders associated with acyl-CoA accumulation may well play a role in their disease pathophysiology. Although the functions of lysine butyrylation are most unclear currently, it was proposed that it may play a vital role in epigenetic modulation by impacting on chromatin dynamics and plasticity, DNA transcriptional regulation and metabolism regulation. Dysfunction of lysine butyrylation may cause metabolism disorders and tumorigenesis, etc.
Antibodies are the most convenient tools in PTM analysis, especially in PTM discovery fields. Creative Biolabs has years of experience in PTM antibody discovery and production services. The products supplied by us are high affinity and specificity with 100% guarantee.
Creative Biolabs can provide a comprehensive list of PTM-specific antibody production services of your choice.