mTRP-2 (180-188) is a murine tyrosinase-related protein 2 (TRP-2) -derived peptide, corresponding to residues 180-188. TRP-2 (180-188) is identified as the major reactive epitope within TRP-2 recognized by anti-B16 CTLs.
CAT No: R1881
CAS No:219312-69-3
Synonyms/Alias:mTRP-2 (180-188);219312-69-3;mTRP-2 180-188;CHEMBL386067;HY-P1827;BDBM50409404;DA-65702;MS-32029;CS-0096087;G16809;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-hydroxypropanoyl]amino]-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-carboxypropanoyl]amino]-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-3-methylbutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-methylpentanoic acid;
mTRP-2 (180-188) is a synthetic peptide fragment corresponding to amino acids 180 through 188 of the mouse Tyrosinase-Related Protein 2 (TRP-2), also known as dopachrome tautomerase. As a member of the melanogenic enzyme family, TRP-2 plays a key role in melanin biosynthesis within melanocytes. The 180-188 sequence represents a defined epitope region, making it highly relevant in immunological and biochemical research focused on antigen processing, peptide-MHC binding, and melanocyte biology. Its well-characterized sequence and defined length render it a valuable tool for studies investigating peptide-based immune responses, antigen presentation, and the molecular mechanisms underlying pigment cell function.
Epitope mapping: The 180-188 region of TRP-2 is frequently utilized in epitope mapping studies to identify and characterize T cell responses specific to melanocyte differentiation antigens. Researchers employ this peptide to dissect the specificity of cytotoxic T lymphocytes (CTLs) and helper T cells, particularly in the context of antigen recognition and immune surveillance. By presenting this defined sequence to immune cells, investigators can elucidate the fine specificity of T cell receptors and better understand the determinants of antigenicity within the TRP-2 protein.
Antigen presentation assays: mTRP-2 (180-188) serves as a model peptide for investigating the mechanisms of antigen processing and presentation via major histocompatibility complex (MHC) class I molecules. It is commonly loaded onto antigen-presenting cells to evaluate peptide-MHC binding affinity, stability, and the efficiency of immune synapse formation. These studies are critical for unraveling the molecular basis of immune recognition and are instrumental in the development of peptide-based immunological assays.
Immunogenicity assessment: The peptide is widely used in immunogenicity studies to assess the activation potential of T cells in vitro. By stimulating splenocytes or isolated T cell populations with this sequence, researchers can quantify cytokine production, proliferation, and cytotoxic activity, thereby gauging the immunostimulatory capacity of the TRP-2 epitope. This approach provides valuable insights into the immune response hierarchy and supports the design of experimental models for antigen-specific activation.
Peptide-based vaccine research: Due to its defined sequence and immunological relevance, the 180-188 fragment is frequently incorporated into peptide vaccine development pipelines for preclinical research. It acts as a prototype antigen for evaluating the efficacy of novel adjuvants, delivery systems, and immunization strategies in eliciting targeted cellular immune responses. Such studies inform the rational design of vaccines aimed at inducing robust and specific T cell-mediated immunity against melanocyte antigens.
Functional studies in pigment cell biology: Beyond its immunological applications, mTRP-2 (180-188) is utilized to probe the functional roles of TRP-2 in pigment cell physiology. By employing the peptide in competitive binding assays or as a molecular probe, researchers can investigate the structural and functional domains of the parent enzyme, elucidate protein-protein interactions, and explore regulatory mechanisms involved in melanogenesis. These studies contribute to a deeper understanding of pigment cell differentiation, enzyme function, and the molecular pathways governing melanin production.
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