Nucleoprotein (396-404) is the 396 to 404 fragment of lymphocytic choriomeningitis virus (LCMV). Nucleoprotein (396-404) is the H-2D(b)-restricted immunodominant epitope and can be used as a molecular model of viral antigen .
CAT No: R1877
CAS No:158475-79-7
Synonyms/Alias:Nucleoprotein 396-404;158475-79-7;Nucleoprotein (396-404);NP 396;(2S,3S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[2-[[(2S)-4-amino-2-[[(2S)-5-amino-2-[[(2S)-1-[(2S)-5-amino-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-5-oxopentanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-4-oxobutanoyl]amino]acetyl]amino]-5-oxopentanoyl]amino]-3-phenylpropanoyl]amino]-3-methylpentanoic acid;DA-76335;MS-31936;G14152;
Nucleoprotein 396-404 (NP 396) is a synthetic peptide corresponding to amino acids 396 through 404 of the nucleoprotein sequence, a region commonly studied in the context of viral immunology and T cell epitope mapping. As a defined peptide fragment derived from a viral nucleoprotein, NP 396 serves as a valuable research tool for dissecting antigen-specific immune responses, particularly in the study of host-pathogen interactions and adaptive immunity. Its precise sequence and biochemical properties make it ideal for applications requiring high specificity and reproducibility in immunological assays, peptide-MHC binding studies, and functional cellular assays.
Epitope Mapping: NP 396 is widely employed in the mapping of T cell epitopes within viral nucleoproteins. By serving as a defined antigenic determinant, it enables researchers to identify and characterize the specific regions of viral proteins recognized by cytotoxic T lymphocytes (CTLs). This application is crucial for understanding the molecular basis of immune recognition and for delineating the immunodominant regions that drive antiviral immunity in experimental models.
Immunogenicity Assessment: As a well-characterized peptide epitope, NP 396 is utilized to evaluate the immunogenic potential of viral antigens in both in vitro and in vivo systems. Its defined sequence allows for controlled stimulation of antigen-specific T cells, facilitating the measurement of cytokine production, proliferation, and cytolytic activity. Such studies are fundamental for elucidating the mechanisms of cellular immune responses and for comparing the efficacy of different vaccine candidates or immunization strategies.
Peptide-MHC Binding Studies: The defined sequence of NP 396 makes it an ideal substrate for major histocompatibility complex (MHC) binding assays. Researchers use this peptide to assess binding affinities to various MHC class I molecules, informing the selection and optimization of epitopes for immunological research or peptide-based vaccine design. These studies contribute to a detailed understanding of antigen processing and presentation, which is central to the development of targeted immunotherapies.
Functional T Cell Assays: NP 396 is frequently used in functional assays designed to evaluate the specificity and activity of T cell populations. By providing a consistent and reproducible stimulus, the peptide enables the detection and quantification of antigen-specific T cells through techniques such as ELISPOT, intracellular cytokine staining, and cytotoxicity assays. These applications are instrumental in immunomonitoring, adoptive cell transfer studies, and the development of immunodiagnostic tools.
Vaccine Development Research: The use of NP 396 in preclinical research supports the rational design and evaluation of peptide-based vaccines targeting viral pathogens. Its role as a model epitope allows for the systematic assessment of immune responses elicited by candidate formulations, adjuvants, and delivery platforms. Insights gained from these studies inform the optimization of vaccine components and strategies, advancing the field of prophylactic and therapeutic vaccine research.
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