Malonylation-Specific Antibody Production Services

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

Malonylation is a newly identified type of protein post-translational modification (PTM) on lysine by mass spectrometry and protein sequence database searching, which is evolutionarily conserved and widespread from bacteria to mammals. Like lysine acetylation, lysine malonylation is also a dynamic and reversible process. Deacetylases sirtuin 5 (Sirt 5), a member of the class III lysine deacetylases, can catalyze lysine demalonylation reaction both in vitro and in vivo. However, at present, the transferases catalyzed the malonylated reaction have not been discovered.

With integrated proteomics technology and biochemical detection methods, lysine malonylation is widely distributed in histones and non-histone substrates. It was found that lysine malonylation on histones play critical roles as disruption of H3K56 lysine malonylation in yeast caused lethality. Bioinformatic analysis of the proteomic results showed malonylated proteins were enriched in metabolic pathways, especially those involved in glucose and fatty acid metabolism. In addition, cetyl-CoA and malonyl-CoA are closely related and inter-convertible, and therefore we suggest that malonylation also functions in metabolism regulation. The levels of lysine malonylation were induced with increased malonyl-CoA in malonyl-CoA decarboxylase (MCD)-deficient cells, suggesting a pathogenic role of lysine malonylation in MCD deficiency. Meanwhile, increasing the level of lysine malonylation caused mitochondrial function and fatty acid oxidation to impair, suggesting that lysine malonylation plays a role in the pathophysiology of malonic aciduria. In the present study, we also observed an elevated lysine malonylation in liver tissues of type 2 diabetes model mice, indicating that a potential role of protein lysine malonylation in type 2 diabetes.

Using affinity enrichment and label-free quantitative proteomics, they characterized the SIRT5-regulated lysine malonylome in wild-type (WT) and Sirt5-/- mice. 1,137 malonyllysine sites were identified across 430 proteins, with 183 sites (from 120 proteins) significantly increased in Sirt5-/- animals. Fig. 1 SIRT5 is a global regulator of lysine malonylation and provides a mechanism for regulation of energetic flux through glycolysis. (Nishida Y, et al. 2015)

As the study of lysine malonylation is still in its early stage, further investigations should be conducted to uncover the biological function of this modification. More types of PTMs have been discovered and identified based on the modified specific antibodies. Creative Biolabs has established the integrated platform servicing for PTM research, especially has years of experience in PTM antibody discovery and production. We provide our global customers with the highest affinity and specificity products.

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


  1. Nishida Y, Rardin M J, Carrico C, et al. (2015) “Sirt5 regulates both cytosolic and mitochondrial protein malonylation with glycolysis as a major target”. Mol Cell, 59(2): 321-332.

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