MAGE-1 (102-112)

Melanoma-associated antigen 1; MAGE-1

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

CAT No: ta-444

Synonyms/Alias:Melanoma-associated antigen 1 (102-112); MAGE-1 (102-112)

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

MAGE-1 (102-112) is a synthetic peptide fragment derived from the melanoma-associated antigen 1 (MAGE-1) protein, a member of the MAGE gene family that is highly relevant in immunological and cancer-related research. Comprising amino acids 102 to 112 of the MAGE-1 sequence, this peptide is frequently utilized as a model epitope in studies focused on antigen presentation, T-cell recognition, and tumor immunology. Its defined sequence and immunogenic properties make it a valuable tool for dissecting mechanisms of immune surveillance, particularly in the context of tumor-associated antigens and cellular immune responses. The MAGE-1 (102-112) peptide supports diverse investigative directions in basic and applied biomedical research, offering precise control for experimental design in immunological assays and peptide-based studies.

Antigen Presentation Studies: As a well-characterized epitope, the MAGE-1 (102-112) peptide is extensively employed in research exploring the molecular mechanisms of antigen processing and presentation. By loading this peptide onto major histocompatibility complex (MHC) molecules in vitro, researchers can investigate the efficiency and specificity of peptide-MHC binding, as well as the subsequent activation of cytotoxic T lymphocytes (CTLs). These studies are fundamental for understanding how tumor antigens are recognized by the immune system and for identifying key determinants influencing immunogenicity at the cellular level.

T-Cell Activation Assays: The peptide serves as a critical reagent in functional assays designed to assess T-cell responses to tumor-associated antigens. When presented by antigen-presenting cells, MAGE-1 (102-112) can stimulate antigen-specific CD8+ T cells, enabling quantitative and qualitative analysis of T-cell activation, proliferation, and cytokine production. Such assays are instrumental for evaluating T-cell receptor specificity, monitoring immune competence, and screening for immunodominant epitopes in cancer immunology research.

Epitope Mapping and Vaccine Design: In the context of epitope mapping, this peptide is used to delineate the precise regions of MAGE-1 recognized by the immune system, aiding in the identification of immunogenic determinants within the protein. The defined sequence allows for systematic evaluation of immune recognition, supporting the rational design of peptide-based vaccines and immunotherapeutic strategies. By providing a platform for testing immunogenicity and cross-reactivity, MAGE-1 (102-112) contributes to the optimization of candidate vaccine constructs and the development of personalized immunotherapies.

Peptide-MHC Tetramer Production: MAGE-1 (102-112) is a valuable substrate for the generation of peptide-MHC tetramers, which are widely used in flow cytometry and immunophenotyping applications. These tetramers enable the direct detection and quantification of antigen-specific T cells within complex cellular populations, facilitating detailed studies of immune repertoire diversity, T-cell clonality, and the dynamics of tumor-infiltrating lymphocytes. The use of synthetic peptides such as this one ensures reproducibility and specificity in the assembly of tetrameric complexes for advanced immunological analyses.

Peptide-Based Functional Studies: The defined chemical structure and sequence of MAGE-1 (102-112) make it suitable for a variety of peptide-functional studies, including structure-activity relationship investigations, peptide stability assessments, and interaction analyses with cellular receptors or antibodies. By enabling precise experimental manipulation, this peptide supports the elucidation of binding affinities, conformational dependencies, and the molecular basis of immune recognition. Such studies are essential for advancing the understanding of tumor antigenicity and for informing the design of next-generation peptide reagents in immunological research.

Source#
Homo sapiens (human)
Epitope
102-112
Restricting HLA
HLA-B57
References
Corbière; Tissue Antigens 2004

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