Brief Introduction
The histone flexible tails protruding from the surface of the nucleosome are vulnerable to a variety of post-translational modifications (PTMs), including but not limited to methylation, acetylation, phosphorylation, ubiquitination, ADP ribosylation, SUMOylation, crotonylation, etc., and they are usually mediated by enzymatic activity. Histone modification is a significant research area of epigenetics and plays an important role in the regulation of gene expression. PTMs can alter the histone’s interactions with DNA and nuclear proteins, resulting in epigenetic changes that regulate many physiological and pathological processes.
Creative BioMart not only provides quantification and identification analysis of histone modifications based on various technologies, but also offers a variety of assay kits associated with histone modification research to help you understand different histone PTMs information from different aspects.
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| Histone methylation is the modification of certain amino acids by adding methyl groups to histones through the catalysis of histone methyltransferases, which in turn can be removed by histone demethylases. Histone methylation and demethylation lead to epigenetic gene activation and silencing, depending on the target site. Quantitative analysis of histone methylation is helpful for studying gene expression patterns, and measurement of enzymatic activity or inhibition of histone methyltransferase and histone demethylase can assist in better understanding certain pathological processes and facilitating the development of related drugs. In addition, the study of specific reader domain-containing proteins recognizing histone methylation has also become important. |
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| Histone acetylation and deacetylation involve in the addition and removal of acetyl groups on certain amino acid residues in the histone tails, a process mediated by histone acetyltransferases and histone deacetylases. Histone acetylation is also a significant epigenetic marker and plays a crucial role in the regulation of chromatin structure. Quantifying the level of acetylated histones, determining enzymatic activity and inhibition of histone acetyltransferases or histone deacetylases, and studying histone acetylation-specific reader domains will help elucidate epigenetic gene transcription and contribute to the development of drugs. |
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| Histone phosphorylation occurs mainly on serine and threonine residues, but also on tyrosine residues. Phosphorylation of histone H3 at Ser10 and Ser28 has been shown to be involved in controlling chromosome condensation. Histone phosphorylation and histone dephosphorylation are in dynamic equilibrium, mediated by corresponding kinases and phosphatases. Detecting changes in histone phosphorylation can provide useful information for better understanding the pathological processes of certain diseases and for drug development targeting kinases. |
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| Histone H2A and H2B ubiquitination at certain lysine residues are common ubiquitination sites, and ubiquitination is also a reversible regulation. SUMO (small ubiquitin-related modifier) is a member of the ubiquitin-like protein family that covalently binds to lysine residues of histones. SUMOylation is a recently discovered histone modification that also play a role in various cellular processes. Detection of histone ubiquitination and SUMOylation will facilitate the understanding of the biological functions of these two epigenetic modifications. |
Supported by years of experience in the field of biotechnology and rigorous quality control, Creative BioMart offers professional kits to meet all kinds of experimental application needs in epigenetics research. If you have any questions, please feel free to contact us.
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