C-Reactive Protein (CRP) 77-82 is the 77-82 fragment of C-Reactive Protein. C-Reactive Protein (CRP), the prototypic marker of inflammation, is a cardiovascular risk marker and may promote atherogenesis[1].
CAT No: 10-101-269
CAS No:130349-01-8
Synonyms/Alias:130349-01-8;C-REACTIVE PROTEIN FRAGMENT 77-82;2-[[2-[[2-[[2-[[2-[(2-amino-3-methylbutanoyl)amino]acetyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]-4-carboxybutanoyl]amino]-3-methylpentanoic acid;C-Reactive Protein (CRP) 77-82;DA-72394;
Chemical Name:L-valylglycylglycyl-L-seryl-L-α-glutamyl-L-Isoleucine (9CI)
C-Reactive Protein (CRP) (77-82) is a synthetic peptide fragment derived from the C-terminal region of the human C-reactive protein, a well-characterized acute-phase reactant involved in the innate immune response. As a peptide compound, CRP (77-82) encompasses a specific sequence that is highly relevant in studies of protein-protein interactions, inflammation signaling, and the molecular mechanisms underlying immune modulation. Its defined structure and bioactive properties make it a valuable reagent for researchers investigating the functional domains of CRP and their roles in various biochemical pathways. The compound's utility extends to a broad range of experimental applications, supporting advances in immunology, structural biology, and peptide-based assay development.
Peptide-Protein Interaction Studies: CRP (77-82) is frequently employed as a molecular probe to elucidate the specific binding sites and interaction motifs between C-reactive protein and its physiological ligands. By introducing this peptide fragment in in vitro systems, researchers can dissect the contribution of the C-terminal sequence to CRP's affinity for phosphocholine-containing molecules, complement components, and other binding partners. Such studies provide mechanistic insights into the recognition patterns that govern acute-phase protein function and facilitate the mapping of critical contact residues involved in immune complex formation.
Inflammation Pathway Research: The peptide serves as a targeted tool for dissecting the molecular underpinnings of inflammatory signaling cascades. Its sequence, corresponding to a functionally significant region of CRP, allows for the assessment of specific peptide-mediated effects on cellular responses such as cytokine release, leukocyte recruitment, and endothelial activation. By modulating experimental conditions with CRP (77-82), investigators can evaluate the distinct contributions of CRP domains to the regulation of inflammation, thereby advancing understanding of acute-phase dynamics at the peptide level.
Peptide-Based Assay Development: Owing to its well-defined structure and immunologically relevant sequence, CRP (77-82) is suitable for use in the design and optimization of peptide-based detection assays. It can be incorporated as a standard or positive control in immunoassays, biosensors, or binding studies aimed at quantifying CRP or identifying antibodies specific to its C-terminal epitopes. The inclusion of this peptide enhances assay specificity and sensitivity, supporting the development of robust analytical platforms for research applications.
Epitope Mapping and Antibody Characterization: The defined sequence of CRP (77-82) is instrumental in epitope mapping studies, enabling the identification of linear antibody binding sites within the C-reactive protein molecule. By utilizing this peptide in immunological assays, researchers can characterize monoclonal or polyclonal antibodies for their specificity and affinity toward the C-terminal region. Such information is crucial for the validation of antibody reagents, the development of diagnostic tools, and the refinement of immunoassay reagents for basic and applied research.
Structure-Activity Relationship Analysis: CRP (77-82) provides a model system for investigating structure-activity relationships within the C-reactive protein family. By subjecting the peptide to systematic modifications or employing it in comparative studies with other CRP-derived fragments, scientists can delineate the structural features that dictate biological activity, ligand recognition, and functional diversity. These analyses contribute to a deeper understanding of peptide-mediated effects and support the rational design of novel bioactive peptides for research and biotechnological applications.
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