Melanocyte protein Pmel 17 precursor (45-57)

Melanocyte protein PMEL;gp100;pmel 17

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

CAT No: ta-042

Synonyms/Alias:Melanocyte protein Pmel 17 precursor (45-57)

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

Melanocyte protein Pmel 17 precursor (45-57) is a synthetic peptide fragment derived from the Pmel 17 protein, a critical component in the biogenesis of melanosomes within melanocytes. This peptide segment encompasses amino acids 45 to 57 of the precursor protein, a region implicated in the early stages of melanosomal matrix formation and pigment deposition. As a well-defined sequence, it is highly relevant to researchers investigating the molecular mechanisms of pigmentation, melanosomal structure, and protein aggregation phenomena associated with pigment cell biology. Its unique biochemical properties make it a valuable reagent for studies focused on peptide structure-function relationships, protein-protein interactions, and the development of analytical assays targeting melanosomal components.

Peptide aggregation studies: The 45-57 fragment of Pmel 17 is particularly well-suited for research into amyloid fibril formation and aggregation, processes fundamental to both normal melanosome maturation and pathological conditions involving protein misfolding. By using this peptide as a model system, investigators can elucidate the sequence determinants and environmental factors that promote or inhibit amyloid-like assembly, providing insight into the controlled formation of functional amyloids in pigment cells as well as broader implications for amyloid research.

Melanosome biogenesis research: The peptide serves as a molecular tool for dissecting the early events of melanosome formation, specifically the transition from non-pigmented to pigmented organelles. Researchers can employ this fragment in in vitro assays to examine its role in the nucleation and stabilization of the melanosomal matrix, thereby advancing understanding of how Pmel 17 contributes to the compartmentalization and polymerization of melanin precursors. Such studies are critical for unraveling the regulatory mechanisms underlying pigmentation and melanosome dynamics.

Epitope mapping and antibody validation: As a defined linear epitope, the Pmel 17 (45-57) peptide is valuable for the characterization and validation of antibodies raised against the Pmel 17 protein. It enables precise mapping of antibody binding sites, assessment of antibody specificity, and optimization of immunodetection protocols. This application is essential for the development of robust immunoassays and for ensuring reagent fidelity in studies of pigment cell biology and related fields.

Peptide-protein interaction assays: The fragment can be utilized in binding studies to identify and characterize molecular partners that interact with the Pmel 17 protein during melanosome maturation. By incorporating the peptide into surface plasmon resonance, pull-down, or co-immunoprecipitation experiments, researchers can probe the affinity and specificity of interactions with chaperones, structural proteins, or regulatory factors, thereby deepening understanding of the protein networks governing melanosomal function.

Analytical method development: The availability of this synthetic peptide enables the calibration and validation of mass spectrometry and chromatographic methods for the detection and quantification of Pmel 17-derived sequences in complex biological samples. Its use as a standard or spike-in control supports the development of sensitive and reproducible analytical workflows, facilitating studies on pigment cell proteomics, post-translational modification analysis, and biomarker discovery within the context of melanocyte biology.

Source#
Homo sapiens (human)
Epitope
45-57
Restricting HLA
HLA-DRB1
References
Shuming Chen; J Immunol 2013

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