Lysine-specific demethylase 6A
UTX protein (1264-1273) is a synthetic peptide fragment corresponding to amino acids 1264 through 1273 of the human UTX protein, also known as KDM6A. As a segment of a histone demethylase involved in chromatin remodeling and epigenetic regulation, this peptide holds significant value for researchers investigating the molecular mechanisms of gene expression and cellular differentiation. The region represented by this sequence can be critical for understanding protein-protein interactions, post-translational modifications, and the structural dynamics of UTX within the context of chromatin biology. Its availability as a chemically defined peptide enables precise experimental manipulation and facilitates a range of investigative approaches in molecular and cellular biology.
Epigenetics research: The 1264-1273 peptide fragment is frequently utilized in studies focused on the functional domains of UTX and their role in chromatin remodeling. By serving as a model substrate or binding motif, it allows researchers to probe the interactions between UTX and other chromatin-associated proteins, such as histone modifiers or transcriptional co-regulators. This approach is instrumental in dissecting the contribution of specific UTX regions to the regulation of gene expression and the maintenance of cellular identity, advancing the broader understanding of epigenetic control mechanisms.
Antibody development and validation: Synthetic peptides derived from defined regions of target proteins are invaluable for generating and validating sequence-specific antibodies. The UTX 1264-1273 peptide can be conjugated to carrier proteins to elicit immune responses in host animals, leading to the production of polyclonal or monoclonal antibodies that recognize the corresponding epitope within the native protein. Such antibodies are essential tools for applications including Western blotting, immunoprecipitation, and immunohistochemistry, where specificity and sensitivity for the UTX protein are paramount.
Protein interaction mapping: The defined sequence of this peptide enables its use in mapping protein-protein interactions involving UTX. By immobilizing the peptide on solid supports or incorporating it into binding assays, researchers can identify and characterize interaction partners that specifically recognize the 1264-1273 region. This strategy facilitates the elucidation of signaling pathways, cofactor associations, and regulatory complexes that modulate UTX function, thereby providing insights into the molecular networks underpinning chromatin dynamics.
Post-translational modification analysis: The UTX 1264-1273 peptide serves as a valuable tool for investigating post-translational modifications, such as phosphorylation, acetylation, or methylation, that may occur within this region. By subjecting the peptide to in vitro modification reactions or mass spectrometry analysis, scientists can identify modification sites, characterize their functional consequences, and study the regulatory mechanisms controlling UTX activity. These findings contribute to a deeper understanding of how dynamic chemical changes influence chromatin regulation and gene expression.
Peptide-based assay development: The defined nature and sequence specificity of the 1264-1273 peptide make it suitable for incorporation into biochemical and biophysical assays. It can be utilized as a standard or competitor in enzyme activity assays, binding studies, or high-throughput screening platforms designed to identify modulators of UTX or its interacting partners. The use of such peptides enhances assay reproducibility and enables quantitative evaluation of molecular interactions, supporting drug discovery and mechanistic research in the field of epigenetics.
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