Zinc finger MYND domain-containing protein 15 isoform 1 (138-147)

Zinc finger MYND domain-containing protein 15 isoform 1 (138-147) is a synthetic peptide fragment derived from a specific region of the MYND-type zinc finger protein family. This peptide corresponds to amino acids 138 through 147 of the human ZMYND15 isoform 1, a protein implicated in transcriptional regulation and chromatin remodeling. The sequence's origin from a functionally relevant domain endows it with unique biochemical properties, making it a valuable molecular tool for researchers investigating protein-protein interactions, post-translational modifications, and the structural determinants of MYND domain function. Its defined sequence and provenance from a regulatory domain provide a foundation for precise mechanistic studies in molecular biology and epigenetics.

Peptide interaction studies: As a synthetic fragment representing a specific segment of ZMYND15, this peptide is frequently employed in assays designed to map protein-protein interactions involving the MYND domain. Researchers utilize it to probe binding affinities with potential interaction partners, such as transcriptional co-repressors or chromatin-associated factors. By serving as a competitive ligand or immobilized bait in pull-down assays, the peptide enables fine dissection of the molecular determinants that govern MYND domain-mediated complex formation, supporting the elucidation of regulatory networks in gene expression.

Epigenetic research: The functional role of ZMYND15 in chromatin remodeling and transcriptional repression positions this peptide as a useful probe in epigenetic studies. Scientists leverage the defined sequence to investigate how post-translational modifications or sequence-specific features influence the recruitment of chromatin modifiers. Incorporating the peptide in in vitro assays or structural analyses can reveal insights into the mechanisms by which MYND domain-containing proteins modulate histone modification patterns and nucleosome positioning, advancing the understanding of epigenetic regulation.

Antibody generation and validation: The 138-147 fragment of ZMYND15 serves as an antigenic epitope for generating sequence-specific antibodies. These antibodies are essential tools for detecting endogenous or recombinant ZMYND15 in immunoassays, such as western blotting or immunoprecipitation. The use of a well-defined peptide epitope ensures high specificity, facilitating the reliable quantification and localization of the target protein in various biological samples and supporting studies on protein expression dynamics.

Peptide-based assay development: Researchers utilize this synthetic peptide in the development of biochemical assays tailored to the MYND domain's functional context. It can be incorporated as a substrate or standard in enzymatic assays, binding studies, or screening platforms aimed at identifying modulators of ZMYND15 activity. The availability of a precise sequence fragment supports assay reproducibility and enables the systematic evaluation of sequence-function relationships within the MYND domain.

Structural and biophysical analysis: The 138-147 peptide fragment is valuable for structural biology applications, including solution-state NMR, circular dichroism, or crystallography studies. By isolating a discrete functional motif, researchers can probe its secondary structure, conformational preferences, and potential to mediate intermolecular contacts. These analyses contribute to a deeper understanding of the structural principles underlying MYND domain recognition and inform the design of engineered peptides or small molecules targeting related protein-protein interfaces.

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