C-Reactive Protein (CRP) 174-185 is the 174-185 fragment of C-Reactive Protein. C-Reactive Protein (CRP), the prototypic marker of inflammation, is a cardiovascular risk marker and may promote atherogenesis.
CAT No: 10-101-270
CAS No:160369-86-8
Synonyms/Alias:160369-86-8;C-REACTIVE PROTEIN (174-185);2-[[2-[[4-amino-2-[[1-[2-[[2-[[1-[2-[[2-[[2-[[2-[(2-amino-3-methylpentanoyl)amino]-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]acetyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoyl]amino]-3-hydroxypropanoyl]pyrrolidine-2-carbonyl]amino]-4-oxobutanoyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoic acid;C-Reactive Protein (CRP) 174-185;DA-72393;
C-Reactive Protein (CRP) (174-185) is a synthetic peptide fragment derived from the human C-reactive protein, a well-characterized acute-phase reactant involved in the innate immune response. This peptide encompasses amino acid residues 174 to 185 of the CRP molecule, representing a region implicated in ligand recognition and protein-protein interactions. Due to its defined sequence and structural relevance, CRP (174-185) serves as a valuable tool in biochemical research focused on inflammation, immunology, and protein function studies. Its utility extends to investigations of peptide-mediated signaling, biomolecular interactions, and the structural determinants underlying CRP activity.
Peptide mapping: CRP (174-185) is frequently employed as a reference standard or probe in peptide mapping experiments aimed at elucidating the structural domains of C-reactive protein. By providing a defined segment of the native protein, this peptide enables researchers to dissect the contributions of specific sequences to overall CRP conformation and function. Such studies are pivotal for understanding the spatial arrangement of functional motifs and for validating epitope mapping strategies in immunological assays.
Protein interaction studies: The 174-185 fragment of CRP is instrumental in examining the molecular interactions between CRP and its physiological partners, including phosphocholine-containing ligands and complement components. Utilizing this peptide in binding assays or surface plasmon resonance experiments allows for precise characterization of binding affinities, kinetic parameters, and the identification of critical contact residues. These insights are essential for unraveling the mechanisms by which CRP modulates immune responses and for informing the design of CRP-based molecular probes.
Immunological assay development: Synthetic CRP (174-185) serves as a well-defined antigenic determinant for antibody generation and assay calibration. Its application in immunoassays, such as ELISA or western blotting, supports the development of highly specific detection systems targeting CRP or its fragments. By facilitating the production and validation of monoclonal or polyclonal antibodies, the peptide contributes to advancing diagnostic research and the quantitative analysis of CRP-related biomarkers in experimental settings.
Structure-function analysis: Researchers utilize CRP (174-185) in studies aimed at correlating sequence-specific features with biological activity. Through site-directed mutagenesis, alanine scanning, or peptide modification approaches, this fragment provides a platform for probing the functional importance of individual amino acids within the CRP molecule. Such structure-function analyses are critical for delineating the biochemical principles governing CRP's role in inflammation and for identifying potential sites for molecular intervention.
Peptide-based inhibitor screening: The defined sequence of CRP (174-185) makes it a suitable candidate for use in high-throughput screening of peptide-based inhibitors or mimetics. By serving as a template or competitive substrate in biochemical assays, the peptide enables the identification and optimization of compounds that modulate CRP-ligand interactions. This application is particularly relevant for research programs focused on the development of novel modulators targeting inflammatory pathways or protein-protein interactions involving CRP.
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