Melanoma-associated antigen C2 (191-200)

Melanoma-associated antigen C2

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

CAT No: ta-046

Synonyms/Alias:Melanoma-associated antigen C2 (191-200)

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

Melanoma-associated antigen C2 (191-200) is a synthetic peptide fragment derived from the C2 isoform of the melanoma-associated antigen (MAGE) protein family, specifically encompassing amino acid residues 191 through 200. As a member of the MAGE protein group, this peptide is notable for its restricted expression in various tumor types, particularly melanoma, and its limited presence in normal tissues. The 191-200 sequence represents a functionally significant epitope that is frequently studied for its role in antigen presentation, immune recognition, and tumor immunology. Its defined sequence and biochemical properties make it a valuable reagent in research focused on antigen processing, T-cell epitope mapping, and the molecular mechanisms underlying tumor-associated immune responses.

Epitope mapping: Researchers utilize the 191-200 peptide fragment of MAGE-C2 to delineate T-cell epitopes recognized by cytotoxic lymphocytes in the context of melanoma and other malignancies. By incorporating this peptide into in vitro assays, scientists can identify specific peptide-MHC interactions that drive immune recognition of tumor cells. Such studies are essential for understanding the immunogenic landscape of cancer antigens and provide insights into the diversity and specificity of T-cell responses against tumor-associated antigens.

Antigen presentation studies: The peptide serves as a model substrate in experiments designed to elucidate the processes of antigen processing and presentation by major histocompatibility complex (MHC) molecules. By tracking the binding and stability of the 191-200 fragment within MHC class I or class II complexes, investigators can assess the efficiency of peptide loading, the influence of peptide sequence on MHC affinity, and the dynamics of antigen display on the cell surface. These investigations are pivotal for unraveling the mechanisms that govern immune surveillance and for optimizing peptide-based immunological assays.

Peptide-based assay development: The defined sequence and immunological relevance of this MAGE-C2 fragment make it a preferred standard in the development and validation of peptide-specific detection assays. It is commonly employed as a positive control or calibrator in ELISPOT, intracellular cytokine staining, and tetramer-based flow cytometry protocols aimed at quantifying antigen-specific T-cell populations. The use of a well-characterized peptide standard enhances the reproducibility and interpretability of immunomonitoring studies, particularly in the context of cancer immunology research.

Peptide synthesis and modification studies: As a synthetic peptide, the 191-200 region of MAGE-C2 is frequently used to optimize protocols for solid-phase peptide synthesis, purification, and labeling. Its moderate length and defined sequence allow researchers to investigate the effects of various chemical modifications, such as N-terminal acetylation or incorporation of non-natural amino acids, on peptide stability, solubility, and immunogenicity. These studies contribute to broader efforts in peptide engineering, facilitating the design of improved peptide reagents for research and diagnostic applications.

Tumor immunology research: The unique tumor-associated expression profile of MAGE-C2 and the immunological activity of its 191-200 peptide fragment underpin its value in studies exploring the mechanisms of tumor immune evasion and immune editing. Researchers leverage this peptide to stimulate antigen-specific T-cell responses in vitro, assess the functional capacity of immune effector cells, and investigate the molecular determinants of tumor immunogenicity. Such research advances the understanding of tumor-immune system interactions and informs the rational design of novel immunological tools for basic and translational oncology studies.

Source#
Homo sapiens (human)
Epitope
191-200
Restricting HLA
HLA-A2
References
Rieuwert Hoppes; J Immunol 2014

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