MAGE-6 (121-134)

Melanoma-associated antigen 6; MAGE-6

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

CAT No: ta-477

Synonyms/Alias:Melanoma-associated antigen 6 (121-134); MAGE-6 (121-134)

Custom Peptide Synthesis
cGMP Peptide
  • Registration of APIs
  • CMC information required for an IND
  • IND and NDA support
  • Drug master files (DMF) filing
Sequence
LLKYRAREPVTKAE
Areas of Interest
Antigen-presenting Cells; Cancer Research

MAGE-6 (121-134) is a synthetic peptide fragment derived from the melanoma-associated antigen 6 (MAGE-6) protein, a member of the MAGE gene family known for its restricted expression in various tumor types and immunoprivileged tissues. As a defined sequence corresponding to amino acids 121 through 134 of the full-length MAGE-6 protein, this peptide serves as a valuable tool for researchers investigating tumor immunology, antigen processing, and T-cell epitope mapping. Its well-characterized nature and relevance to cancer-associated antigens make it an important reagent for studies focused on antigen presentation, immune recognition, and the molecular underpinnings of tumor-specific immune responses.

Epitope Mapping: Researchers utilize this peptide to delineate T-cell epitopes within the MAGE-6 protein, facilitating the identification of immunodominant regions recognized by cytotoxic T lymphocytes. By incubating immune cells with the defined 121-134 fragment, scientists can assess T-cell reactivity, characterize antigen-specific responses, and map the minimal epitope necessary for immune recognition. This approach supports the development of assays to monitor cellular immunity against tumor antigens and informs the rational design of immunotherapeutic strategies.

Antigen Presentation Studies: The 121-134 peptide fragment is instrumental in dissecting the biochemical mechanisms of major histocompatibility complex (MHC) class I and class II presentation. By loading antigen-presenting cells with the peptide, investigators can evaluate peptide binding affinities, identify optimal presentation conditions, and analyze T-cell activation thresholds. These experiments contribute to a deeper understanding of antigen processing, peptide-MHC complex stability, and the specificity of immune surveillance in the context of cancer biology.

Synthetic Peptide Assay Development: The defined sequence of MAGE-6 (121-134) enables its use as a standard or control in peptide-based immunoassays, including enzyme-linked immunospot (ELISpot), flow cytometry-based intracellular cytokine staining, and tetramer staining assays. Employing this peptide as a reagent allows for the quantification of antigen-specific T-cell responses, the validation of assay sensitivity, and the benchmarking of immune monitoring protocols in preclinical research settings.

Peptide-Protein Interaction Analysis: The peptide's sequence specificity makes it suitable for probing molecular interactions between MAGE-6-derived epitopes and binding partners such as antibodies, T-cell receptors, or MHC molecules. Surface plasmon resonance, isothermal titration calorimetry, and other biophysical techniques can be employed to characterize binding kinetics, affinity, and structural determinants of recognition. These studies provide mechanistic insights into immune engagement and support the engineering of improved immunological reagents.

Cancer Immunology Research: As a representation of a tumor-associated antigenic determinant, the 121-134 region of MAGE-6 is frequently examined in the context of tumor immunogenicity and immune evasion. Its use in experimental systems enables the exploration of immune escape mechanisms, the assessment of antigen loss variants, and the investigation of tolerance versus activation in immune cell subsets. These applications advance the broader understanding of tumor-immune interactions and contribute to the identification of novel targets for immunological intervention.

Source#
Homo sapiens (human)
Epitope
121-134
Restricting HLA
HLA-DR13
References
Chaux; J Exp Med 1999

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