OVA-E1 peptide contains a defined sequence of polar, aromatic, and charged residues that promote diverse secondary-structure motifs. Researchers use it to examine antigenic determinants, peptide folding dynamics, and residue-specific interactions. The sequence's balanced polarity aids studies of conformational transitions. Its architecture supports detailed biophysical profiling.
CAT No: R2407
CAS No:153316-01-9
Synonyms/Alias:OVA-E1 peptide;153316-01-9;(2S,5S,8S,11S,14S,17S,20S,23S)-23-Amino-14-(2-amino-2-oxoethyl)-5-(4-aminobutyl)-11-benzyl-17,20-di((S)-sec-butyl)-8-(2-carboxyethyl)-2-isobutyl-4,7,10,13,16,19,22-heptaoxo-3,6,9,12,15,18,21-heptaazahexacosanedioic acid;HY-P2319;AKOS040756882;DA-76497;CS-0129511;(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S,3S)-2-[[(2S,3S)-2-[[(2S)-2-amino-4-carboxybutanoyl]amino]-3-methylpentanoyl]amino]-3-methylpentanoyl]amino]-4-oxobutanoyl]amino]-3-phenylpropanoyl]amino]-4-carboxybutanoyl]amino]hexanoyl]amino]-4-methylpentanoic acid;
OVA-E1 peptide is a synthetic peptide derived from the ovalbumin protein, specifically corresponding to the immunodominant epitope recognized by cytotoxic T lymphocytes in murine models. As a well-characterized peptide antigen, it plays a pivotal role in immunological research, particularly in the context of antigen processing, presentation, and T cell activation studies. Its defined sequence and reproducible immunogenic properties make it a valuable tool for probing fundamental mechanisms of cellular immunity, supporting the development of immunoassays, and facilitating the study of antigen-specific responses in controlled experimental systems.
Immunology research: OVA-E1 peptide is extensively utilized in the field of immunology to investigate the mechanisms of antigen recognition and processing by major histocompatibility complex (MHC) class I molecules. By serving as a model antigen in murine systems, especially in C57BL/6 mice, it enables researchers to dissect the molecular details of CD8+ T cell responses, providing insights into the specificity, activation, and cytolytic functions of cytotoxic T lymphocytes. Its use has been instrumental in characterizing T cell receptor (TCR) repertoires and understanding the rules governing peptide-MHC interactions.
Vaccine development studies: The peptide serves as a benchmark epitope in preclinical vaccine research, where it is employed to assess the efficacy of vaccine candidates and adjuvants in eliciting robust, antigen-specific cellular immunity. By incorporating OVA-E1 into experimental vaccine formulations or delivery systems, researchers can quantitatively evaluate the induction of T cell responses, optimize immunization protocols, and compare the immunogenicity of novel platforms in a standardized manner. These studies are critical for advancing antigen design and improving the predictive value of animal models in translational immunology.
Antigen-specific T cell assays: OVA-E1 peptide is a preferred reagent for the functional analysis of T cells using assays such as enzyme-linked immunospot (ELISpot), intracellular cytokine staining, and cytotoxicity assays. Its defined sequence allows for precise stimulation of antigen-specific T cell populations, facilitating the measurement of cytokine production, proliferation, and effector functions. These applications are essential for evaluating the quality and magnitude of immune responses in basic research, immunotoxicology, and adoptive cell therapy studies.
In vivo immune monitoring: The peptide is widely used in adoptive transfer experiments and in vivo tracking of antigen-specific T cells. By labeling or transferring T cells with defined specificity for OVA-E1, researchers can monitor their migration, expansion, and effector functions within living organisms. This approach provides critical data on the dynamics of T cell responses in various physiological and pathological settings, enabling the study of immune surveillance, tolerance, and memory formation under controlled experimental conditions.
Peptide-MHC tetramer generation: OVA-E1 serves as a key component in the production of MHC class I tetramers, which are powerful tools for the direct visualization and quantification of antigen-specific T cells by flow cytometry. By loading the peptide onto recombinant MHC molecules, researchers can generate fluorescently labeled tetramers that bind specifically to T cells bearing the corresponding TCR. This technique has revolutionized the ability to track and characterize antigen-specific lymphocytes in diverse research contexts, supporting advances in immunophenotyping and functional analysis.
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