SEB Domain 144-153 is Staphylococcal Enterotoxin B domain amino acid residue 144-153. SEB Domain 144-153 inhibits transcytosis of multiple staphylococcal enterotoxins, SEA, SEE, and TSST-1. Staphylococcal enterotoxin B (SEB) is a toxin produced by Staphylococcus aureus.
CAT No: R1668
CAS No:210229-94-0
Synonyms/Alias:SEB Domain 144-153 acetate;AKOS040764069;PD159388;TS-10434;SEB Domain 144-153 acetate(210229-94-0 free base);210229-94-0;acetic acid;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[(2S)-2,6-diaminohexanoyl]amino]hexanoyl]amino]hexanoyl]amino]-3-methylbutanoyl]amino]-3-hydroxybutanoyl]amino]propanoyl]amino]-5-oxopentanoyl]amino]-4-carboxybutanoyl]amino]-4-methylpentanoyl]amino]butanedioic acid;
SEB Domain 144-153 is a synthetic peptide fragment derived from Staphylococcal enterotoxin B (SEB), a well-characterized bacterial superantigen known for its potent immunostimulatory properties. This peptide encompasses amino acid residues 144 to 153 of the SEB protein, a region implicated in key interactions with host immune components. Its defined sequence and structural features make it an important biochemical tool for researchers investigating antigenic determinants, T-cell activation mechanisms, and host-pathogen interactions at the molecular level. As a research-use peptide, SEB Domain 144-153 supports a range of experimental applications in immunology, structural biology, and peptide-based assay development.
Epitope mapping: SEB Domain 144-153 is frequently utilized in epitope mapping studies to delineate the minimal sequences recognized by specific antibodies or T-cell receptors. By providing a discrete segment of the SEB molecule, this peptide enables researchers to systematically assess immunodominant regions and identify critical residues involved in immune recognition. Such investigations are instrumental for advancing our understanding of superantigen-host interactions and for guiding the rational design of targeted immunological assays.
T-cell activation studies: As a defined superantigen-derived peptide, SEB Domain 144-153 serves as a valuable reagent for probing T-cell activation pathways in vitro. Its application allows for controlled stimulation of T-cell populations, facilitating the analysis of cytokine release, proliferation, and downstream signaling events. This approach supports the dissection of superantigen-mediated immune responses and aids in characterizing the molecular mechanisms that underlie T-cell receptor engagement and activation.
Peptide-MHC binding assays: The sequence of SEB Domain 144-153 is suitable for use in peptide-major histocompatibility complex (MHC) binding assays, which are essential for elucidating the structural basis of antigen presentation. By incorporating this peptide into binding studies, researchers can investigate its affinity for various MHC class II alleles, thereby gaining insights into peptide-MHC specificity, stability, and the determinants of immunogenicity. These findings have broad implications for both basic immunology and the development of diagnostic tools.
Antibody specificity testing: The defined nature of SEB Domain 144-153 permits its use in evaluating the specificity and cross-reactivity of monoclonal or polyclonal antibodies raised against SEB or related superantigens. By serving as a target in enzyme-linked immunosorbent assays (ELISAs), western blots, or other immunodetection platforms, the peptide helps confirm antibody selectivity and supports the optimization of immunoassays for research or quality control purposes.
Structural and biophysical analysis: SEB Domain 144-153 provides a model system for structural and biophysical investigations, including nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), and molecular dynamics simulations. These approaches enable researchers to characterize the conformational preferences, stability, and interaction profiles of the peptide both in isolation and in complex with binding partners. Such studies contribute to a deeper molecular understanding of superantigen function and inform the design of novel peptide-based probes or inhibitors.
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