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-known acute-phase reactant involved in the body's inflammatory response. This peptide segment, encompassing amino acids 77 to 82, has garnered significant interest in biochemical and immunological research due to its unique structural properties and its role in mimicking specific functional domains of the native protein. CRP (77-82) is characterized by its sequence specificity and its ability to interact with various cellular and molecular targets, making it a versatile tool for probing the biological mechanisms underlying inflammation, immune regulation, and protein-protein interactions. Its synthetic nature allows for precise control in experimental settings, enabling researchers to dissect the contributions of this particular region to the overall function of C-reactive protein in both physiological and pathological contexts.
Inflammatory Pathway Investigation: CRP (77-82) peptide serves as a valuable probe in the study of inflammatory signaling pathways. By introducing this fragment into cell cultures or biochemical assays, researchers can evaluate its influence on the activation or inhibition of key mediators such as cytokines, chemokines, and adhesion molecules. Its sequence, which is implicated in the modulation of complement activation, aids in unraveling the molecular mechanisms by which C-reactive protein exerts its pro- or anti-inflammatory effects. The peptide's use in these studies provides insights into the fundamental processes that govern acute and chronic inflammatory responses, supporting the identification of novel therapeutic targets for inflammatory diseases.
Protein-Protein Interaction Studies: The CRP (77-82) fragment is frequently utilized to map interaction sites within the full-length C-reactive protein and its binding partners. By employing techniques such as surface plasmon resonance, co-immunoprecipitation, or peptide array analysis, scientists can delineate the specific residues involved in intermolecular recognition events. This application is particularly relevant for understanding how CRP engages with complement components, Fc receptors, and other immune effectors. Insights gained from such studies inform the rational design of peptide-based inhibitors or mimetics that can modulate these interactions for research or biotechnological purposes.
Immunological Assay Development: As a well-defined epitope, CRP (77-82) is instrumental in the creation of immunoassays aimed at detecting antibodies or other proteins that recognize this region. Synthetic peptides corresponding to this sequence are conjugated to carrier proteins or immobilized on assay platforms to facilitate the quantification of immune responses in experimental models. These assays are pivotal in elucidating the antigenic determinants of C-reactive protein and in validating the specificity of antibody reagents, thereby enhancing the reliability of immunological research tools.
Structural Biology and Epitope Mapping: The defined sequence of CRP (77-82) makes it an ideal candidate for structural studies using techniques like nuclear magnetic resonance (NMR) spectroscopy or X-ray crystallography. Researchers utilize this peptide to investigate the conformational dynamics and surface accessibility of the C-terminal region, which are critical for understanding its role in ligand binding and immune recognition. Additionally, it serves as a reference epitope for mapping the binding sites of monoclonal antibodies or small molecules, contributing to the detailed characterization of structure-function relationships within the protein.
Biomarker Discovery and Validation: The CRP (77-82) peptide is also employed in the identification and validation of biomarker candidates related to inflammation and immune status. By incorporating this fragment into proteomic workflows or multiplex assay systems, scientists can assess the presence and relevance of CRP-derived peptides in biological samples. This approach aids in the discovery of peptide signatures associated with disease states, supporting the development of diagnostic and prognostic tools for research applications.
Peptide-based Research Tool: As a synthetic fragment, CRP (77-82) offers versatility as a research reagent for applications such as competitive binding assays, peptide mapping, and functional screening. Its defined sequence and reproducible synthesis ensure consistency across experiments, making it a reliable standard for comparative studies. The peptide enables researchers to dissect the specific contributions of the C-terminal segment to the overall activity of C-reactive protein, fostering a deeper understanding of its biological functions and facilitating the advancement of peptide-based technologies in immunology and inflammation research.
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