Malonylation-Specific Antibody Introduction

Malonylation, a post-translational modification of lysine identified by stable isotope labeling techniques and high-throughput mass spectrometry, was first reported in 2011. It is an evolutionarily conserved acyl modification. A growing number of studies have demonstrated that malonylation is associated with epigenetic mechanisms, angiogenesis, vascular defects, and metabolic pathways. However, since the discovery of malonylation is only about 10 years old, many studies are not in-depth, and more research and efforts need to be invested. Based on our advanced phage display platform, Creative Biolabs offers comprehensive development services for malonylation-specific antibodies to facilitate malonylation research.

Malonylation Modification

As a global regulator of lysine malonylation, SIRT5 has been reported to preferentially remove negatively charged carboxyl and acyl moieties. It acts as a catalyst to remove alanine groups from the lysine side chains of protein substrates and leads to reversible protein alanylation. The reaction is dependent on nicotinamide adenine dinucleotide (NAD). It consumes NAD as a co-substrate and produces the Sirtuin feedback inhibitor nicotinamide, 2'-O-malonyl-ADP-ribose and deacylated substrates.

A mouse liver-based study showed that 28% of alanylated proteins are targets of SIRT5 and 16% of alanine-based lysine sites are regulated by SIRT5. Malonyl-CoA can act as a universal donor in malonylation reactions, possibly through a non-enzymatic mechanism or specific malonyltransferase activity, and is an important intermediate in the cellular metabolic pathway.

Malonyl-CoA can act as a universal donor in malonylation reactions, possibly through a non-enzymatic mechanism or specific malonyl transferase activity, and is an important intermediate in the cellular metabolic pathway. Malonyl-CoA decarboxylase catalyzes the conversion of malonyl-CoA to carbon dioxide and acetyl-CoA. It helps maintain metabolite levels and regulates peroxisomal and mitochondrial activity.

Malonylation plays an important regulatory role in different types of diseases. In metabolic diseases, malonylation is involved in the regulation of protein synthesis, cell proliferation, the regulation of β-oxidation, inflammation, glucose metabolism, and lipid metabolism, affecting the pathological processes of diseases such as vascular deficiency, malonic aciduria, diabetes mellitus, cardiovascular diseases, and neurofibromatosis. In inflammatory diseases, lysine malonylation is an important mechanism of action in the regulation of glycolytic processes. In tumor pathology, malonyl coenzyme A can regulate the glycolytic enzyme activity, inhibit GAPDH activity, NF2 expression level, and other factors to regulate the tumor process. These mechanisms of action in the disease also provide effective ideas for the development of effective therapeutic approaches.

It was found that malonylation is also present in lens proteins. Malonylation occurs mainly in water-soluble (WS) and water-insoluble soluble protein fractions. Moreover, αB-crystallin may be the dominant malonylated protein in the human lens. Also, it was shown that the immunoreactivity of αB-crystallin increased with increasing sample age.

Malonylation-Specific Antibody

Malonylation-specific antibodies are generally generated by immunizing mice with malonylated BSA or KLH or synthetic malonyl peptides and purifying them by affinity chromatography. Their high specificity and sensitivity make them effective in detecting malonylated proteins and are important tools for malonylation studies.

Creative Biolabs has a wealth of knowledge and experience in PTM specific antibody discovery. We would be happy to discuss with you our knowledge and experience in malonylation -specific antibody development.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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