Gp100 (25-33), human is the amino acids 25-33 fragment of the human melanoma antigen. It is a 9-amino acid (AA) epitope restricted by H-2Db and recognized by the T cells.
CAT No: R1884
CAS No:212370-40-6
Synonyms/Alias:Gp100 (25-33), human;212370-40-6;gp100 H-2 Db;HY-P1585;DA-53677;CS-0045209;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2,6-diaminohexanoyl]amino]-3-methylbutanoyl]pyrrolidine-2-carbonyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-4-oxobutanoyl]amino]-5-oxopentanoyl]amino]-3-carboxypropanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-methylpentanoic acid;
Gp100 (25-33) (human) is a synthetic peptide corresponding to amino acids 25 through 33 of the human gp100 protein, also known as glycoprotein 100 or PMEL. As a segment derived from a melanocyte lineage-specific antigen, this peptide is of particular interest in immunological, oncological, and cellular biology research. Its sequence represents an epitope recognized by T cells, which has made it a valuable tool for dissecting antigen presentation, immune recognition, and the functional properties of peptide-MHC complexes. The biochemical relevance of Gp100 (25-33) (human) is underscored by its role in studies of antigen processing, T cell activation, and the molecular mechanisms underlying immune surveillance in the context of melanoma and pigment cell biology.
Epitope mapping: Gp100 (25-33) (human) is widely utilized in epitope mapping assays to characterize T cell responses to melanocyte differentiation antigens. By serving as a defined, minimal peptide epitope, it enables researchers to assess the specificity and avidity of T cell receptors for the gp100 antigen, facilitating the identification of immunodominant regions and the fine mapping of T cell epitopes. This utility is particularly important in the context of understanding immune recognition dynamics and in the development of antigen-specific immunological assays.
Antigen presentation studies: The peptide is frequently employed in investigations of major histocompatibility complex (MHC) class I antigen presentation pathways. By loading Gp100 (25-33) (human) onto antigen-presenting cells, researchers can evaluate peptide binding affinity, stability of peptide-MHC complexes, and the efficiency of T cell activation. These studies provide mechanistic insights into antigen processing, cross-presentation, and the rules governing peptide selection by MHC molecules, which are central to adaptive immune responses.
T cell activation assays: In experimental immunology, Gp100 (25-33) (human) serves as a model antigen for stimulating antigen-specific cytotoxic T lymphocytes (CTLs) in vitro. This application is critical for quantifying T cell effector functions, such as cytokine secretion, proliferation, and cytolytic activity, in response to a well-defined peptide stimulus. The peptide's defined sequence allows for controlled and reproducible experiments to evaluate T cell sensitivity, cross-reactivity, and the functional consequences of TCR engagement.
Peptide-based screening: The defined structure and immunological relevance of Gp100 (25-33) (human) make it an excellent candidate for screening peptide libraries and optimizing T cell-based assays. Researchers leverage the peptide in high-throughput formats to identify T cell clones with desired specificity, to test the effects of amino acid substitutions, and to benchmark assay performance. Such screening applications are essential for advancing our understanding of antigen recognition and for the rational design of immunological reagents.
Peptide-MHC structural biology: The peptide is also instrumental in structural biology studies aimed at elucidating the molecular interactions between peptides and MHC class I molecules. By serving as a crystallizable ligand, it allows for the determination of high-resolution structures of peptide-MHC complexes, which in turn inform models of T cell recognition, peptide binding motifs, and the structural basis of immune specificity. These insights are invaluable for both fundamental immunology and the rational design of peptide-based probes or modulators.
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5. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
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