MAGE-10 (254-262)

Melanoma-associated antigen 10; MAGE-10

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

CAT No: ta-479

Synonyms/Alias:Melanoma-associated antigen 10 (254-262); MAGE-10 (254-262)

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Sequence
GLYDGMEHLl
Areas of Interest
Antigen-presenting Cells; Cancer Research

MAGE-10 (254-262) is a synthetic peptide fragment derived from the melanoma-associated antigen gene family member 10, specifically encompassing amino acid residues 254 to 262. As a nonapeptide corresponding to an immunologically relevant epitope, it is widely recognized for its role in antigen presentation and immune recognition studies. The sequence is of particular interest in tumor immunology and molecular oncology, where it serves as a model system for understanding peptide-MHC interactions, T-cell specificity, and antigen processing mechanisms. Its defined structure and sequence fidelity make it a valuable tool for researchers investigating the molecular underpinnings of cancer-associated antigenicity and peptide-based immune responses.

Epitope mapping: MAGE-10 (254-262) is frequently utilized in epitope mapping experiments to identify and characterize T-cell recognition sites within the MAGE-10 antigen. By employing this peptide in in vitro assays, researchers can delineate the precise regions within the parent protein that elicit cytotoxic T lymphocyte responses. This capability is essential for advancing the understanding of antigen-specific T-cell activation and for the rational design of immune monitoring assays in cancer research.

Peptide-MHC binding studies: The nonapeptide is instrumental in evaluating the binding affinity and specificity of peptide antigens to major histocompatibility complex (MHC) molecules, particularly within the context of HLA-restricted presentation. Its defined sequence enables quantitative binding assays, structural analyses, and computational modeling to elucidate the structural determinants governing peptide-MHC interactions. Such studies provide foundational insights into immune surveillance and the molecular basis for antigen presentation in tumor immunology.

Functional immunoassays: Researchers employ this peptide in functional assays designed to assess T-cell activation, cytokine release, and cytolytic activity. By incorporating the peptide into ex vivo or in vitro stimulation protocols, it is possible to measure antigen-specific immune responses using techniques such as ELISPOT, intracellular cytokine staining, or flow cytometry-based readouts. These applications are pivotal for validating T-cell receptor specificity and for monitoring immune responses in preclinical or translational research settings.

Peptide synthesis and analytical validation: MAGE-10 (254-262) serves as a reference standard and positive control in peptide synthesis workflows and analytical validation procedures. Its well-characterized sequence and immunological relevance make it a preferred choice for calibrating chromatographic methods, mass spectrometry analyses, and quality assurance protocols in peptide production laboratories. The use of such standards ensures reproducibility and accuracy in both synthesis and analytical characterization, supporting robust experimental outcomes.

Structural and biophysical studies: The defined length and sequence of this peptide facilitate its application in structural biology and biophysical research. It is suitable for studies involving NMR spectroscopy, crystallography, or surface plasmon resonance to probe peptide conformation, stability, and intermolecular interactions. Insights gained from these investigations contribute to a deeper understanding of how tumor-associated peptides adopt conformations conducive to immune recognition, aiding in the rational design of next-generation peptide-based research tools and immunological probes.

Source#
Homo sapiens (human)
Epitope
254-262
Restricting HLA
HLA-A2
References
Huang; J Immunol 1999

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