Melanocyte protein PMEL;gp100;pmel 17
CAT No: ta-261
Synonyms/Alias:Melanocyte protein PMEL (86-95); gp100 (86-95)
gp100 (86-95) is a synthetic peptide fragment derived from the human glycoprotein 100 (gp100), a melanocyte differentiation antigen widely recognized for its role in immunological and cancer research. This decapeptide sequence corresponds to amino acids 86 through 95 of the gp100 protein, a region frequently studied for its immunogenic properties and relevance in antigen processing and presentation. As a well-defined peptide epitope, it is of significant interest in the investigation of T cell recognition, antigen-specific immune responses, and the broader study of tumor-associated antigens within the context of melanoma and related research fields. The availability of this peptide in a highly characterized form enables precise experimental design in both basic and translational studies.
Epitope mapping: The gp100 (86-95) peptide is extensively utilized in epitope mapping experiments aimed at delineating the specific regions of the gp100 antigen recognized by T cells. By presenting this defined sequence to immune cells, researchers can systematically identify and characterize T cell receptor interactions, elucidating the molecular determinants of antigen recognition. Such studies are vital for advancing the understanding of immune surveillance mechanisms in melanoma and for the rational design of antigen-specific immunological assays.
Antigen presentation studies: In the context of MHC class I-restricted antigen presentation, this peptide serves as a model substrate to investigate the processing and display of tumor-associated antigens by antigen-presenting cells. Researchers employ the gp100 (86-95) fragment to analyze peptide binding affinities to various HLA alleles, assess the efficiency of peptide loading, and study the impact of sequence variation on immune recognition. These applications provide valuable insights into the molecular basis of immune evasion and the development of effective immunotherapeutic strategies.
T cell activation assays: The defined nature of the gp100 (86-95) peptide makes it a preferred reagent for in vitro T cell activation assays. By exposing T lymphocytes to this epitope, investigators can monitor antigen-specific activation, cytokine secretion, and cytotoxic responses. Such assays are critical for evaluating the functional competence of T cell populations, screening for antigen-specific clones, and optimizing protocols for adoptive cell transfer research. The peptide's utility in these settings supports the development of robust experimental models for immune monitoring.
Peptide vaccine research: As a representative tumor-associated epitope, the gp100 (86-95) sequence is commonly incorporated into experimental vaccine formulations designed to elicit targeted immune responses against melanoma antigens. Its use in preclinical immunization studies enables the assessment of immunogenicity, specificity, and the generation of memory T cell responses. These investigations contribute to the optimization of peptide-based vaccine platforms and the identification of key parameters influencing antigen-driven immunity.
Analytical assay development: The well-characterized nature of this synthetic peptide facilitates its application in the development and validation of analytical assays, such as ELISPOT, flow cytometry-based tetramer staining, and peptide-MHC multimer technologies. By serving as a standardized antigenic target, it aids in the quantification and phenotypic analysis of antigen-specific T cell populations. Such assays are instrumental for immune monitoring in research settings, supporting the advancement of diagnostic tools and immunological studies related to melanoma and antigen recognition.
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