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Propionylation-Specific Antibody Production Services

Creative Biolabs provides highly specific and sensitive pan anti-propionyllysine antibodies and site-specific anti-propionylated protein antibodies based on our excellent High-Affi™ technology. These antibodies are produced by immunizing mice with propionylated BSA or KLH or with a synthetic propionyl peptide and purified by affinity chromatography. They do not cross-react with acetylated and other acylated peptides.

Propionylation has been identified as a novel type of protein post-translational modification on lysine. Lysine propionylation is structurally similar to lysine acetylation, has been well demonstrated in both prokaryotes and eukaryotes. The reversible lysine propionylation has been found in histones with different modified sites, such as lys12, lys14, lys18, lys23 of H3 and lys12, lys16 of H4. Besides histones, propionylation was also found in non-histones such as p53 and regulatory enzymes p300/CBP. The two previously known acetyltransferases, CREB-binding protein and p300, could catalyze lysine propionylation in histones. The two enzymes can carry out autopropionylation in vitro in a fashion similar to autoacetylation. Propionylation of lysine is dynamically regulated as histone deacetylase sirtuin 2 (Sir 2) can remove this modification in the presence of NAD+. These results suggest that histone propionylation might share the same set of enzymes with histone acetylation.

Like acetyl-CoA, propionyl-CoA is an important intermediate in biosynthesis and energy production. Propionyl-CoA versus acetyl-CoA may determine the difference of modifications. Human histone H4 and bacterial propionyl-CoA synthetase are propionylated at specific lysine residues that have been known previously to be acetylated. Histone propionylation may provide a novel epigenetic regulatory mark for cell metabolism. Generally, given the unique roles of propionyl-CoA in energy metabolism and the significant structural changes induced by the modifications, propionylation are likely to have important but distinct functions in the regulation of biological processes. It includes:


The identification of lysine propionylation described here provides an entry point for future functional studies in cellular physiology and pathology.

A. Structures of three short-chain CoAs, the acetyl-CoA, propionyl-CoA, and butyryl-CoA, as well as the three modified lysines, acetyllysine, propionyllysine, and butyryllysine. B. An illustration of novel lysine propionylation and butyrylation sites in histone H4. Ac, acetyl; Me, methyl; Buty, butyryl; Prop, propionyl.Fig. 1. A. Structures of three short-chain CoAs, the acetyl-CoA, propionyl-CoA, and butyryl-CoA, as well as the three modified lysines, acetyllysine, propionyllysine, and butyryllysine. B. An illustration of novel lysine propionylation and butyrylation sites in histone H4. Ac, acetyl; Me, methyl; Buty, butyryl; Prop, propionyl. (Chen Y. et al. 2007)

However, other proteins subject to this modification remain to be identified, and the enzymes processing this modification need to be characterized. Antibodies are the most powerful tools in PTM discovery and identification, and they also benefit for studying the functions. Creative Biolabs has years of experience in antibody discovery and production services. We can tailor your need and provide the most highly specific and high-quality antibody products.

Creative Biolabs can provide a comprehensive list of PTM-specific antibody production services of your choice.


Reference

  1. Chen Y, Sprung R, Tang Y, et al. (2007) “Lysine propionylation and butyrylation are novel post-translational modifications in histones”. Mol Cell Proteomics, 6(5): 812-819.



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