Transcription factor SOX-10 (331-340)

Transcription factor SOX-10

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: ta-403

Synonyms/Alias:Transcription factor SOX-10 (331-340)

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  • Drug master files (DMF) filing
Sequence
SAWISKPPGV
Areas of Interest
Antigen-presenting Cells; Cancer Research

Transcription factor SOX-10 (331-340) is a synthetic peptide fragment corresponding to amino acid residues 331 to 340 of the SOX-10 protein, a member of the SRY-related HMG-box (SOX) family of transcription factors. SOX-10 plays a pivotal role in the regulation of gene expression during neural crest development, melanocyte biology, and glial cell differentiation. The 331-340 peptide segment is derived from a functionally significant region of the protein, making it valuable for research focused on protein-protein interactions, post-translational modifications, and antigenic epitope mapping. As a peptide compound, it offers researchers a precise tool for dissecting the molecular mechanisms underlying SOX-10's regulatory functions in cellular and developmental biology.

Epitope mapping: Researchers frequently utilize the SOX-10 (331-340) peptide to define and characterize antigenic determinants within the full-length transcription factor. By employing this peptide in immunological assays such as ELISA or western blotting, scientists can identify antibody binding sites and evaluate the specificity and sensitivity of SOX-10-directed antibodies. Such studies are instrumental in the development and validation of immunodetection reagents for basic research and diagnostic applications, especially in contexts where SOX-10 serves as a lineage marker.

Protein interaction studies: The synthetic peptide corresponding to SOX-10 (331-340) serves as a valuable probe for investigating direct and indirect protein-protein interactions involving the SOX-10 transcription factor. By immobilizing the peptide or using it in pull-down assays, researchers can examine how this specific region contributes to the recruitment of co-regulators, binding partners, or chromatin-associated proteins. These studies advance the understanding of the mechanistic basis of SOX-10's regulatory activity within transcriptional complexes.

Post-translational modification analysis: The defined sequence of SOX-10 (331-340) enables focused investigation into potential post-translational modifications, such as phosphorylation, acetylation, or methylation, that may occur within this region. Synthetic peptides are routinely used as substrates in in vitro modification assays or as standards in mass spectrometry-based proteomics workflows. Such analyses help elucidate the regulatory impact of site-specific modifications on SOX-10 function and stability.

Peptide-based inhibitor screening: The SOX-10 (331-340) peptide can serve as a molecular template in the screening and design of small molecule inhibitors or peptidomimetics targeting the interaction interfaces of SOX-10. By mimicking a defined segment of the native protein, the peptide facilitates high-throughput screening assays aimed at identifying compounds that disrupt critical protein-protein contacts. This approach is particularly relevant in the context of dissecting transcriptional regulation and identifying potential chemical probes for basic research.

Antibody production: The defined sequence and synthetic accessibility of the SOX-10 (331-340) peptide make it well-suited as an immunogen for the generation of polyclonal or monoclonal antibodies. When conjugated to carrier proteins, the peptide can elicit a targeted immune response, yielding antibodies that recognize the corresponding epitope within the native SOX-10 protein. Such antibodies are valuable for use in diverse immunoassays, including immunohistochemistry and immunoprecipitation, supporting studies of SOX-10 expression and function in developmental, neurobiological, and cell lineage research.

Source#
Homo sapiens (human)
Epitope
331-340
Restricting HLA
HLA-A2
References
Khong; Cancer Res 2002

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