MAGE-3 (149-160)

Melanoma-associated antigen 3; MAGE-3

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

CAT No: ta-464

Synonyms/Alias:Melanoma-associated antigen 3 (149-160); MAGE-3 (149-160)

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

MAGE-3 (149-160) is a synthetic peptide fragment derived from the melanoma-associated antigen 3 (MAGE-3) protein, a member of the MAGE family of cancer-testis antigens. As a well-characterized epitope, this peptide comprises amino acids 149 to 160 of the full-length MAGE-3 protein and is recognized for its immunological relevance, particularly in the context of tumor antigenicity and T cell recognition. Its defined sequence and immunogenic properties have made it a valuable reagent in tumor immunology, epitope mapping, and the study of antigen processing and presentation. MAGE-3 (149-160) is widely used in research settings to elucidate the mechanisms of immune recognition of cancer cells and to support the development of novel immunological assays and screening platforms.

Epitope mapping: Researchers utilize this peptide fragment to identify and characterize specific T cell epitopes within the MAGE-3 protein. By employing it in peptide binding assays or T cell activation studies, investigators can determine which segments of the MAGE-3 antigen are most immunologically relevant. This application is crucial for dissecting the fine specificity of T cell responses in the context of cancer immunology, enabling the precise mapping of immune-dominant regions and informing the design of targeted immunotherapeutic strategies.

Antigen presentation studies: The MAGE-3 (149-160) peptide is instrumental in examining the mechanisms of antigen processing and presentation by major histocompatibility complex (MHC) molecules. By pulsing antigen-presenting cells with this defined peptide, researchers can assess the efficiency and specificity of MHC class I or II peptide loading, as well as the subsequent activation of cytotoxic or helper T lymphocytes. Such studies are fundamental for understanding the molecular interactions that govern immune surveillance and tumor immune evasion.

Immunoassay development: Owing to its well-defined sequence and immunogenic properties, this peptide serves as a standard in the development of peptide-based immunoassays. It can be used as a positive control or calibrator in enzyme-linked immunospot (ELISPOT), enzyme-linked immunosorbent assay (ELISA), or flow cytometry-based assays designed to quantify antigen-specific T cell responses. The availability of a synthetic, sequence-defined peptide ensures assay reproducibility and facilitates the benchmarking of immune monitoring platforms in cancer research.

Peptide-MHC tetramer generation: The MAGE-3 (149-160) sequence is frequently employed in the synthesis of peptide-MHC tetramers, which are powerful tools for the detection and enumeration of antigen-specific T cell populations by flow cytometry. By incorporating this peptide into MHC complexes, researchers can selectively label T cells with specificity for the MAGE-3 epitope, allowing for detailed phenotypic and functional characterization of tumor-reactive lymphocytes. This application is particularly valuable in monitoring immune responses in experimental cancer models and in ex vivo studies of patient-derived samples.

Peptide library screening: In the context of high-throughput immunological research, this peptide can be used as part of overlapping peptide libraries to screen for T cell reactivity across the MAGE-3 protein. Such libraries enable systematic evaluation of immune recognition patterns, supporting the identification of novel epitopes and the assessment of cross-reactivity within the MAGE antigen family. The use of well-characterized synthetic peptides such as this one enhances the reliability and interpretability of screening data, advancing the understanding of tumor antigenicity and immune targeting.

Source#
Homo sapiens (human)
Epitope
149-160
Restricting HLA
HLA-DR4/DR7
References
Kobayashi; Cancer Res 2001

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