gp100 (45-59)

Melanocyte protein PMEL;gp100;pmel 17

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

CAT No: ta-035

Synonyms/Alias:Pmel 17 protein (45-59);gp100 (45-59)

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

gp100 (45-59) is a synthetic peptide fragment derived from the human glycoprotein 100 (gp100), a melanocyte differentiation antigen widely studied in immunology, oncology, and cellular signaling research. As a defined sequence corresponding to amino acids 45 to 59 of the gp100 protein, this peptide serves as a valuable tool in the investigation of antigen processing, peptide-MHC complex formation, and T cell recognition. Its utility extends to fundamental studies exploring the molecular basis of antigenicity, as well as applications in the development of immunological assays and the characterization of immune responses against melanocyte-related proteins.

Immunological assay development: The 45-59 peptide fragment of gp100 is frequently utilized in the design and optimization of immune monitoring assays, such as ELISPOT, intracellular cytokine staining, and tetramer-based flow cytometry. By serving as a defined antigenic epitope, it enables precise quantification and characterization of antigen-specific T cell responses in vitro. Researchers leverage this functionality to dissect the dynamics of T cell activation, proliferation, and effector function, particularly in studies focusing on melanocyte antigens and their role in immune surveillance.

Epitope mapping and T cell recognition studies: The defined sequence of gp100 (45-59) makes it an ideal model for mapping T cell epitopes and studying peptide-MHC interactions. Investigators use this peptide to assess the specificity and affinity of T cell receptors (TCRs) for gp100-derived epitopes, facilitating the identification of immunodominant regions within the parent protein. Such studies are critical for elucidating the mechanisms of antigen recognition and for advancing the rational design of immunotherapeutic strategies targeting tumor-associated antigens.

Antigen processing and presentation research: The peptide is instrumental in dissecting the pathways involved in antigen processing and MHC class I or II presentation. By introducing the synthetic fragment into antigen-presenting cells, researchers can evaluate the efficiency of peptide loading, stability of peptide-MHC complexes, and the subsequent activation of CD8+ or CD4+ T cells. These investigations provide foundational insights into the cellular machinery governing immune recognition and tolerance, with implications for understanding autoimmunity and immune escape mechanisms.

Peptide-based vaccine and immunotherapy model systems: In preclinical research, the gp100 (45-59) peptide is widely adopted as a model antigen for evaluating the principles of peptide-based vaccine design and immunotherapy. Its well-characterized sequence and immunogenic properties enable controlled studies into antigen delivery, adjuvant selection, and immune potentiation. Such model systems are essential for optimizing formulation parameters and for benchmarking the performance of novel immunomodulatory strategies in vitro and in vivo.

Analytical and quality control applications: Beyond its role in immunological research, the gp100 (45-59) peptide serves as a reference standard in analytical chemistry and peptide synthesis workflows. It is employed to validate the performance of chromatographic, mass spectrometric, and sequencing methodologies, ensuring the accuracy and reproducibility of peptide identification and quantification. These applications support the rigorous quality control of peptide-based reagents and contribute to the reliability of downstream biochemical and immunological experiments.

Source#
Homo sapiens (human)
Epitope
45-59
Restricting HLA
HLA-DR15
References
Francisco Max Damico; Invest Ophthalmol Vis Sci 2005

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