gp100 (471-480)

Melanocyte protein PMEL;gp100;pmel 17

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

CAT No: ta-266

Synonyms/Alias:Melanocyte protein PMEL (471-480); gp100 (471-480)

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

gp100 (471-480) is a synthetic peptide fragment derived from the melanoma-associated glycoprotein 100, corresponding specifically to amino acids 471 through 480 of the full-length protein. As a defined peptide sequence, it is widely recognized for its importance in immunological and cancer research, particularly in studies focused on antigen presentation and T cell recognition. The precise sequence and biochemical properties of this peptide make it a valuable tool for investigating cellular immune responses, facilitating the exploration of peptide-MHC interactions, and advancing the understanding of tumor-associated antigens. Its relevance extends to basic biochemical studies, assay development, and the design of experimental immunotherapies, positioning it as a critical reagent in both academic and industrial research settings.

Immunological research: The gp100 (471-480) peptide is extensively utilized in studies of antigen-specific T cell responses, particularly within the context of melanoma and other cancers expressing the gp100 protein. By serving as a defined epitope recognized by cytotoxic T lymphocytes, the peptide enables researchers to evaluate the specificity, activation, and functional properties of T cells in vitro. This application is instrumental for dissecting the mechanisms of immune recognition, tolerance, and escape, as well as for characterizing the repertoire and efficacy of T cell populations in both preclinical and translational research settings.

Epitope mapping: As a well-characterized peptide fragment, gp100 (471-480) is commonly employed in epitope mapping studies to identify and validate the minimal sequences required for MHC class I binding and subsequent T cell activation. Its use allows for the systematic evaluation of peptide-MHC interactions, contributing to the refinement of immunodominant epitopes and the development of peptide-based assays. Such studies are essential for advancing the understanding of antigen processing and presentation pathways, as well as for optimizing the design of immunological reagents and diagnostic tools.

Vaccine development research: The defined sequence of gp100 (471-480) makes it a valuable candidate for the design and evaluation of experimental peptide-based vaccines targeting melanoma-associated antigens. In preclinical studies, the peptide can be formulated with appropriate adjuvants or delivery systems to assess its immunogenicity and ability to elicit antigen-specific cellular responses. These investigations support the rational development of novel immunization strategies, providing insight into the parameters that govern the induction and maintenance of effective anti-tumor immunity.

Assay development: gp100 (471-480) is frequently incorporated into in vitro assays designed to monitor antigen-specific immune responses, such as enzyme-linked immunospot (ELISPOT) assays, intracellular cytokine staining, and cytotoxicity assays. Its use as a standardized antigen enables the quantification and functional characterization of T cell responses in experimental models and patient-derived samples. This application is particularly valuable for evaluating immune monitoring protocols, validating assay performance, and supporting quality control in research and development workflows.

Peptide synthesis and modification studies: The peptide's defined sequence and manageable length render it an excellent model for peptide synthesis optimization and structure-activity relationship investigations. Researchers utilize gp100 (471-480) to explore strategies for enhancing peptide stability, solubility, and MHC binding affinity through chemical modifications, such as amino acid substitutions or conjugation approaches. These studies contribute to the advancement of synthetic peptide chemistry and inform the design of next-generation immunological reagents and research tools.

Source#
Homo sapiens (human)
Epitope
471-480
Restricting HLA
HLA-B35
References
Benlalam; J Immunol 2003

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