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    Histone Methylation Epigenomics

      Histone methylation is a crucial epigenetic modification, playing a key role in gene expression, chromosomal structure, and cell fate. Methylation is present at various sites on histones, but mainly concentrated on lysine (Lys) and arginine (Arg) at the N-terminal tail.


      Lysine Methylation

      Common histone methylation modification sites on lysine include H3K4, H3K9, H3K27, H3K36, H3K79, and H4K20, where mono-, di-, and tri-methylation modifications can occur. Its function is to regulate gene expression by affecting the activity of different regions of chromosomes.


      Arginine Methylation

      Common histone methylation modification sites on arginine include H3R2, H3R8, H3R17, H3R26, H4R3, and H2AR3, which can undergo mono-methylation, symmetric di-methylation, and asymmetric di-methylation. It regulates gene expression by participating in other histone methylation modifications or recruiting proteins of different natures to the DNA promoter.


      Histone methylation is also a part of protein post-translational modification (PTM). Its research can be referred to PTM proteomics, which combines immunoprecipitation and mass spectrometry for quantitative analysis. After parallel analysis of a series of samples (different concentrations of drug stimulation, gene knockout, etc.), the changes of this PTM at a specific protein site due to different experimental conditions can be obtained. Histone methylation, as a type of PTM, has similar research methods. Currently, the arginine and lysine site methylation sequence antibodies developed by CST have been efficiently applied in large-scale methylation proteomics identification. It should be noted that symmetric and asymmetric arginine dimethylation modifications will result in the same molecular weight increase. Their structural differences cannot be distinguished by mass spectrometry, so the study of arginine dimethylation needs to independently enrich the samples using symmetric dimethyl and asymmetric dimethyl antibodies.


      MtoZ Biolabs uses Thermo Fisher's Orbitrap Fusion Lumos mass spectrometry platform in combination with nanoLC-MS/MS nanospray chromatography to provide histone methylation proteomics analysis technology services. You only need to tell us your experimental objectives and send the samples. MtoZ Biolabs provides one-stop service including protein extraction, protein digestion, methylation peptide enrichment, peptide separation, mass spectrometry analysis, mass spectrometry raw data analysis, and bioinformatics analysis. Feel free to consult for free.

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