Histone-lysine N-methyltransferase EZH2 (735-743)

Histone-lysine N-methyltransferase EZH2 (735-743) is a synthetic peptide fragment derived from the Enhancer of Zeste Homolog 2 (EZH2), a key enzymatic component of the Polycomb Repressive Complex 2 (PRC2). This peptide encompasses amino acids 735 to 743 of the human EZH2 sequence, a region implicated in the regulation of histone methylation and epigenetic gene silencing. As a representative segment of the EZH2 protein, it serves as a valuable molecular tool for dissecting the structure-function relationships of chromatin-modifying enzymes and for advancing research in the field of epigenetics.

Epigenetic research: The 735-743 peptide fragment of EZH2 is frequently employed as a research substrate or competitive inhibitor in studies investigating histone methyltransferase activity. By mimicking a critical region of the full-length enzyme, this peptide enables detailed analysis of substrate specificity, enzyme kinetics, and the molecular determinants of methyl group transfer to lysine residues on histone tails. Its use supports the elucidation of the mechanistic basis for gene repression mediated by PRC2.

Antibody validation: Synthetic peptides corresponding to defined regions of target proteins are essential for the validation and characterization of antibodies used in chromatin immunoprecipitation (ChIP), Western blotting, and immunofluorescence assays. The EZH2 (735-743) fragment serves as a highly specific antigen for generating and testing antibodies that recognize this segment of the methyltransferase, ensuring reliable detection and quantification in a variety of experimental platforms.

Protein-protein interaction studies: Short, sequence-defined peptides derived from chromatin-modifying enzymes are widely used to map interaction interfaces and binding partners. The 735-743 region of EZH2 is of particular interest for probing contacts with regulatory proteins, cofactors, or small-molecule inhibitors. Incorporation of this peptide into pull-down assays or surface plasmon resonance experiments facilitates the identification and characterization of novel interactors that modulate EZH2 function.

Peptide modification and structure-function analysis: Researchers utilize the EZH2 (735-743) peptide as a model substrate for chemical modification, such as methylation or labeling, to investigate the functional consequences of post-translational modifications. By introducing defined chemical groups or isotopic labels, scientists can monitor the dynamics of methyl group transfer, study recognition by reader domains, and explore the structural requirements for enzymatic activity or inhibitor binding.

Mass spectrometry calibration and assay development: The defined sequence and physicochemical properties of the EZH2 (735-743) peptide make it a suitable standard for developing and calibrating mass spectrometry-based assays targeting methyltransferase-derived peptides. Its use in assay optimization ensures accurate detection, quantification, and characterization of methylated species in complex biological samples, thereby supporting the advancement of quantitative proteomics in epigenetic research.

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