Tyrosinase 369-377, human is a HLA-A2.1-restricted epitope derived from tyrosinase, has been used to develop tumor-targeted vaccines with mixed efficacy.
CAT No: R1116
CAS No:168650-46-2
Synonyms/Alias:168650-46-2;[Asp371]-Tyrosinase (369-377), human;2-[[5-amino-2-[[2-[[2-[[2-[[2-[[2-[[2-[[2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylsulfanylbutanoyl]amino]-3-carboxypropanoyl]amino]acetyl]amino]-3-hydroxybutanoyl]amino]-4-methylsulfanylbutanoyl]amino]-3-hydroxypropanoyl]amino]-5-oxopentanoyl]amino]-3-methylbutanoic acid;2,2,2-trifluoroacetic acid;(Asp371)-Tyrosinase (369-377) (human) acetate salt;168650-46-2(free basis);H-Tyr-Met-Asp-Gly-Thr-Met-Ser-Gln-Val-OH; H-YMDGTMSQV-OH;YMDGTMSQV;Asp371;Tyrosinase 369-377;FA73646;DA-69124;FA109106;FA110240;[Asp371] Tyrosinase(369-377), human;(Asp371)-Tyrosinase (369-377) (human) trifluoroacetate salt;
[Asp371]-Tyrosinase (369-377), human is a synthetic peptide fragment derived from the human tyrosinase enzyme, specifically encompassing residues 369 to 377 with an aspartic acid substitution at position 371. As a segment of the tyrosinase protein, this peptide holds particular significance in the study of melanogenesis and enzymatic regulation, as tyrosinase is a key copper-containing enzyme involved in melanin biosynthesis. The structural and sequence-specific properties of this region make it a valuable tool for researchers investigating the functional domains of tyrosinase, protein-protein interactions, and the molecular mechanisms underlying pigment formation and enzyme modulation.
Enzyme structure-function analysis: The peptide serves as a model substrate for elucidating the structure-function relationships within the tyrosinase enzyme. By isolating and studying this specific fragment, researchers can assess the contribution of the 369-377 region—especially the effect of the Asp371 substitution—on the enzyme's catalytic activity, substrate recognition, and overall conformational dynamics. Such insights are crucial for mapping functional domains and identifying residues critical for enzymatic efficiency or regulation.
Epitope mapping and antibody development: The defined sequence of this human tyrosinase fragment enables its use in epitope mapping studies, facilitating the identification of antigenic determinants recognized by antibodies. Researchers can employ the peptide to screen for monoclonal or polyclonal antibodies that specifically target this region, supporting the development of highly selective immunoassays or diagnostic reagents. The presence of the Asp371 modification further allows exploration of antibody specificity and cross-reactivity, which is essential for generating reliable detection tools in biochemical and cell-based assays.
Peptide-based inhibitor screening: As a representative motif from the active or regulatory domains of tyrosinase, the peptide can be utilized in high-throughput screening platforms to identify small molecules or peptide-based inhibitors. By serving as a competitive substrate or binding partner, it aids in the discovery and characterization of compounds that modulate tyrosinase function, which is of interest in pigment biology research and studies of enzymatic regulation. The sequence specificity enhances the relevance of screening outcomes for subsequent mechanistic investigations.
Protein interaction studies: The synthetic fragment provides a defined system for probing interactions between tyrosinase and its molecular partners, such as chaperones, cofactors, or regulatory proteins. Researchers can use the peptide in pull-down assays, surface plasmon resonance, or other biophysical techniques to quantify binding affinities and delineate interaction interfaces. Insights gained from these studies support a deeper understanding of the molecular networks governing tyrosinase stability, localization, and activity within melanogenic pathways.
Post-translational modification analysis: The peptide's sequence context, particularly with the aspartic acid substitution, makes it a useful substrate for studying post-translational modifications such as phosphorylation, glycosylation, or oxidation. By exposing the peptide to relevant modifying enzymes or cellular extracts, investigators can monitor modification patterns and assess their impact on structure or function. These studies contribute to a broader comprehension of how post-translational events influence tyrosinase regulation and activity in physiological and experimental settings.
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