gp100 (570-579)

Melanocyte protein PMEL;gp100;pmel 17

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

CAT No: ta-257

Synonyms/Alias:Melanocyte protein PMEL (570-579); gp100 (570-579)

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

gp100 (570-579) is a synthetic peptide fragment corresponding to amino acid residues 570 to 579 of the human glycoprotein 100 (gp100) molecule, a melanocyte differentiation antigen primarily expressed in melanocytic cells and melanoma. As a well-characterized epitope recognized by cytotoxic T lymphocytes (CTLs), this peptide has become a valuable tool in the study of antigen processing, T cell-mediated immune responses, and melanoma-associated antigens. Its defined sequence allows for precise experimental manipulation, making it a critical reagent for immunological research, peptide-MHC binding studies, and the exploration of tumor immunology.

Epitope mapping: Researchers utilize gp100 (570-579) to investigate the specificity and binding affinity of T cell receptors (TCRs) for peptide-MHC complexes. Its sequence represents a naturally processed epitope presented by HLA-A2 molecules on the surface of melanoma cells, enabling the detailed mapping of immune recognition sites. Such studies are essential for understanding the molecular interactions governing antigen presentation and for identifying key determinants of T cell activation.

Immunogenicity assessment: The peptide serves as a model antigen in assays designed to evaluate CTL responses, including interferon-gamma release, cytotoxicity, and proliferation assays. Its use in in vitro stimulation protocols allows for the quantification and characterization of antigen-specific T cell populations, providing critical insights into immune monitoring strategies and the assessment of T cell functionality in various experimental systems.

Peptide-MHC binding studies: gp100 (570-579) is widely employed in binding affinity assays to examine the interaction between peptides and major histocompatibility complex (MHC) class I molecules. Such studies elucidate the principles of peptide selection, stability, and presentation by MHC molecules, contributing to the rational design of immunotherapeutic strategies and the optimization of peptide-based vaccines.

T cell activation assays: The defined sequence and immunological relevance of this peptide make it an ideal reagent for stimulating antigen-specific T cells in vitro. It is frequently used in co-culture systems, ELISPOT assays, and flow cytometry-based analyses to induce and measure T cell activation, cytokine production, and proliferation. These applications facilitate the functional evaluation of T cell responses and support the development of novel immunomodulatory agents.

Antigen processing research: As a prototypical melanoma antigen epitope, gp100 (570-579) enables the study of intracellular antigen processing and presentation pathways. Researchers employ this peptide to dissect the mechanisms by which tumor-associated antigens are generated, loaded onto MHC class I molecules, and presented to the immune system. Such investigations advance the understanding of tumor immunology and inform the identification of novel targets for immunotherapeutic intervention.

Source#
Homo sapiens (human)
Epitope
570-579
Restricting HLA
HLA-A2
References
Tsai; J Immunol 1997

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