Melanoma-associated antigen C1 (779-787)

Melanoma-associated antigen C1

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

CAT No: ta-487

Synonyms/Alias:Melanoma-associated antigen C1 (779-787)

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

Melanoma-associated antigen C1 (779-787) is a synthetic peptide fragment derived from the MAGE-C1 protein, a member of the melanoma antigen gene family. This peptide sequence represents a specific epitope located within the C-terminal domain of MAGE-C1, a protein known for its restricted expression in various tumor types, particularly malignant melanoma, but with limited presence in normal adult tissues. The unique immunogenic properties and tumor-associated expression profile of this peptide have made it a valuable tool in tumor immunology, epitope mapping, and antigen-specific cellular response studies. Its well-defined sequence and relevance to cancer-testis antigens position it as a critical reagent for researchers investigating tumor antigenicity, immune recognition, and the molecular mechanisms underlying cancer immune surveillance.

Immunological assay development: The 779-787 peptide fragment is widely utilized in the development and optimization of immunological assays aimed at detecting MAGE-C1-specific T cell responses. By incorporating this epitope into ELISPOT, intracellular cytokine staining, or tetramer-based flow cytometry platforms, researchers can quantify antigen-specific cytotoxic T lymphocyte populations in peripheral blood or tissue samples. Such assays are instrumental in evaluating cellular immune responses in both basic research and preclinical settings, enabling detailed characterization of T cell recognition and activation in response to tumor-associated antigens.

Epitope mapping and antigen presentation studies: The defined sequence of the MAGE-C1 (779-787) peptide serves as a model substrate for dissecting the molecular interactions between tumor antigens and major histocompatibility complex (MHC) molecules. Researchers employ this peptide to investigate peptide binding affinity, MHC restriction, and the structural determinants of T cell receptor recognition. These studies provide critical insights into antigen processing and presentation pathways, informing the design of immunogenic epitopes and enhancing understanding of the factors governing immune specificity toward cancer cells.

Cancer immunology research: The immunogenic characteristics of the MAGE-C1 (779-787) sequence make it a valuable reagent for exploring the mechanisms of tumor immune evasion and the dynamics of antigen-specific immune surveillance. By utilizing this peptide in vitro or in ex vivo stimulation protocols, investigators can assess the functional capacity of immune effector cells to recognize and respond to melanoma-associated antigens. Such experiments contribute to elucidating the interplay between tumor cells and the host immune system, supporting efforts to unravel the complexities of tumor immunogenicity and immune escape.

Peptide-based vaccine research: The 779-787 epitope is frequently incorporated into experimental protocols evaluating the immunogenicity and efficacy of peptide-based vaccines targeting tumor-associated antigens. Researchers use this peptide to stimulate antigen-specific T cell responses in preclinical models, assess immunization strategies, and optimize adjuvant formulations. Its inclusion in vaccine development studies enables systematic evaluation of epitope selection, delivery methods, and immune potentiation approaches, contributing to the advancement of next-generation cancer immunotherapies.

Quality control and analytical validation: Synthetic peptides such as the MAGE-C1 (779-787) fragment play a crucial role as reference standards or positive controls in assay validation and quality assurance processes. Laboratories utilize this well-characterized sequence to benchmark the sensitivity, specificity, and reproducibility of immunological assays, ensuring robust performance and reliable data generation in both research and translational applications. The availability of this defined peptide standardizes experimental workflows and supports the reproducibility of results across diverse research settings.

Source#
Homo sapiens (human)
Epitope
779-787
Restricting HLA
HLA-DR15
References
Nuber; Proc Natl Acad Sci U S A 2010

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