MAGEA-10 (254-262)

MAGEA-10

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

CAT No: ta-562

Synonyms/Alias:MAGEA-10 (254-262)

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

MAGEA-10 (254-262) is a synthetic peptide corresponding to amino acid residues 254 to 262 of the Melanoma Antigen Gene A10 (MAGEA10) protein. As a member of the cancer-testis antigen family, MAGEA10 is predominantly expressed in various malignancies and is minimally present in normal somatic tissues, making its peptide fragments valuable tools for immunological and oncological research. The 254-262 epitope is recognized for its role in antigen presentation and T-cell recognition, positioning this peptide as a significant reagent for dissecting immune responses, evaluating antigen processing, and developing peptide-based research models.

Epitope mapping: The MAGEA-10 (254-262) peptide serves as a defined epitope for mapping T-cell recognition sites within the MAGEA10 protein. Researchers utilize it to identify and characterize cytotoxic T lymphocyte (CTL) responses specific to this region, enabling the elucidation of immune surveillance mechanisms in cancer. By incorporating this peptide into ex vivo assays, investigators can determine which T-cell subsets recognize MAGEA10-derived antigens and assess the immunodominance hierarchy of tumor-associated epitopes.

Antigen processing studies: This peptide is frequently employed in studies investigating the antigen processing and presentation pathways in human antigen-presenting cells. By pulsing dendritic cells or other antigen-presenting cells with the MAGEA-10 (254-262) sequence, scientists can analyze how peptide loading onto major histocompatibility complex (MHC) molecules occurs, and subsequently monitor the activation of specific T-cell clones. These experiments provide insights into the efficiency and specificity of antigen presentation, which is critical for understanding immune recognition of tumor antigens.

Assay development: The defined sequence of this peptide makes it a valuable standard for developing and validating immunological assays, such as ELISPOT, intracellular cytokine staining, and tetramer-based flow cytometry. Using the MAGEA-10 (254-262) epitope enables precise quantification of antigen-specific T-cell populations, assessment of T-cell functionality, and evaluation of immune responses in preclinical models. Its application enhances assay reproducibility and supports the development of robust experimental protocols for immunomonitoring.

Peptide-based screening: In the context of high-throughput screening platforms, the MAGEA-10 (254-262) peptide is utilized to evaluate the binding affinity and specificity of T-cell receptors (TCRs) or antibodies targeting the MAGEA10 antigen. This approach aids in the identification of novel immune reagents, such as TCR-mimic antibodies or engineered T-cell receptors, by providing a consistent and well-characterized target for functional screening campaigns. The peptide's defined structure supports the rapid assessment of candidate molecules in vitro.

Structural and binding studies: Structural biologists use this peptide to investigate the molecular interactions between MAGEA10-derived epitopes and MHC class I molecules or TCRs. By incorporating the peptide into crystallization trials or biophysical binding assays, researchers can resolve the three-dimensional architecture of immune complexes and delineate the critical residues involved in antigen recognition. Such studies contribute to a deeper understanding of peptide-MHC-TCR interactions and inform the rational design of next-generation immunological reagents.

Source#
Homo sapiens (human)
Epitope
254-262
Restricting HLA
HLA-A2
References
KA Chianese-Bullock; Am Assoc Immnol 2005

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