Formylation Specific Antibody Introduction

Lysine formylation is a reversible post-translational modification that is widely distributed in prokaryotes and eukaryotes. Little is known about the mechanism of action and physiological activity of lysine formylation. Therefore, more studies on lysine formylation are needed. Based on our hybridoma platform and phage display technology, Creative Biolabs provides advanced formylation-specific antibody development services to support the study of formylation.

Formylation Modification

Formylation is now considered a new post-translational modification of lysines that mainly occurs in histones. It refers to the covalent binding of a formyl functional group (-CHO) to some lysine residues, catalyzed by various oxidative enzymes to accomplish protein modification, which in turn alters protein conformation and function, allowing them to perform biological roles. Lysine formylation is the shortest type of PTM and has been reported in vitro for biological and chemical modifications. N-terminal lysine formylation has been studied in detail, while N(ε)-lysine formylation is found in chemical modifications of histones and other nuclear proteins. Core and linker histones are formylated at multiple lysine residues located in the histone tails and globular structural domains, where the lysine residues are known to be involved in the organization of ribosomal particles or play important roles in DNA binding.

Formylation is involved in a variety of biological processes and is particularly abundant in chromosomal proteins, potentially interfering with epigenetic mechanisms governing chromatin function, such as the regulation of chromatin conformation and gene expression in histones and other nuclear proteins. A clear distinction between dimethylation (28.0313 Da) and formylation (27.9949 Da) has been made using the high-quality accuracy of modern MS instruments. The two modifications can be distinguished by different LC retention times for both modifications. The results showed that formylation affects lysyl residues, which are important for interaction with DNA, and also those modified by acetylation and methylation. Thus, formylation interferes with the formation and stabilization of binding sites for histone code-mediated regulatory proteins, such as transcription factors and chromatin activity regulators, thereby impairing histone function.

Due to the slow renewal rate of histones and some other chromosomal proteins, lysine formylation accumulates with age and leads to dysfunctional chromatin. In addition, lysine formylation is stimulated by oxidative stress, suggesting a potential association with the development of stress-related diseases, including cancer. Indeed, lysine formylation may be involved in the loss of protein function in organisms similarly to other chemical modifications, such as glycosylation in diabetes or oxidative damage in aging.

The mechanism of toxicity of lysine formylation mainly involves the formation of stable lysine adducts in proteins after exposure to toxicants. The major reactive compounds produced by cytochrome P450 (CYP) metabolism of trichloroethylene (TCE) can form N6-formyl-lysine protein adducts. These TCE-derived protein adducts can serve as a basis for assessing human exposure and risk to TCE. Furthermore, N6-formylation of lysine occurs as a secondary modification of the protein and appears to be derived from the products of DNA oxidation in cells. The N6-formylation modification of lysine may interfere with the signaling function of lysine acetylation, which is thought to be an important determinant of methylation and gene expression in mammalian cells. As a result, this modification may contribute to the pathophysiology of oxidative and nitrosative stress. In addition, the formylation of lysine residues may lead to the binding of chimeric proteins to 2,5-dimethyl-p-benzoquinone diimine, an intermediate of oxidative allergenic p-amino aromatic compounds, including lysine-induced N-formylation to generate antigenic responses.

Formylation-Specific Antibody

Commonly used methods to detect lysine formylation are mass spectrometry, antibody methods, and chemical methods, all of which primarily detect formylation by targeting specific amino acid residues. Antibodies are essential tools for antibody-based assays, and as formylation is a reversible post-translational modification, preparing and detecting antibodies for formylation require strict sample handling. A standard operating procedure can effectively ensure the status of formylation, the validity and specificity of the antibody, and the authenticity and reliability of the test results.

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 formylation-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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