Fibrinopeptide B, human is a compound released from fibrinogen by thrombin action. Release of fibrinopeptide B from fibrinogen appears to be necessary for Ca2+ uptake and subsequent binding to fibrin.
CAT No: 10-101-290
CAS No:36204-23-6
Synonyms/Alias:Fibrinopeptide B;36204-23-6;Fibrinopeptide B, human;Fibrinopeptide B (human);FPB,human;Fibrinopeptides B;Fibrinopeptide B (human) acetate salt;Fibrinopeptide B human;DA-73358;
Fibrinopeptide B, human is a synthetic peptide corresponding to the N-terminal sequence cleaved from the Bβ chain of human fibrinogen during the coagulation cascade. As a well-characterized peptide fragment, it plays a pivotal role in the study of blood clotting mechanisms, serving as a molecular marker for thrombin activity and fibrin formation. Its defined sequence and biochemical properties make it a valuable tool for researchers investigating the dynamics of hemostasis, peptide-protein interactions, and the regulation of coagulation pathways. The availability of this peptide in a purified form enables controlled experimental designs in both basic and applied biochemical research.
Coagulation pathway research: Fibrinopeptide B is instrumental in elucidating the molecular events underlying blood coagulation. Upon activation of thrombin, fibrinogen is cleaved to release Fibrinopeptide B, marking a critical step in the transformation of soluble fibrinogen into insoluble fibrin. By incorporating this peptide into in vitro assays, researchers can monitor thrombin activity, dissect the kinetics of fibrin formation, and explore the regulation of clot assembly. Its use provides insight into the temporal sequence and specificity of proteolytic events in the coagulation cascade, facilitating a deeper understanding of hemostatic control.
Mass spectrometry calibration and assay development: As a well-defined peptide fragment, Fibrinopeptide B serves as a standard or calibrant in mass spectrometry-based proteomics. Its consistent ionization properties and known sequence allow for accurate calibration of mass spectrometers, ensuring reproducibility and sensitivity in peptide mapping and protein identification workflows. The peptide is frequently utilized in method development for quantitative assays, enabling precise detection and measurement of target peptides in complex biological samples.
Thrombin substrate specificity studies: The sequence of Fibrinopeptide B provides a model substrate for probing the enzymatic specificity of thrombin and related serine proteases. By employing this peptide in kinetic assays or cleavage studies, scientists can investigate the substrate preferences, catalytic efficiency, and inhibition profiles of coagulation enzymes. Such applications are critical for the characterization of novel anticoagulant compounds, the design of therapeutic inhibitors, and the fundamental understanding of protease-substrate interactions within the coagulation system.
Antibody production and immunoassay development: The unique epitope presented by Fibrinopeptide B is exploited in the generation of specific antibodies used in immunoassays. These antibodies facilitate the sensitive detection and quantification of the peptide in plasma or experimental samples, supporting studies of thrombin generation and fibrinogen turnover. The peptide's role as an immunogen or assay target underpins the development of ELISA kits and other immunodetection platforms, which are essential tools in both research and diagnostic laboratories.
Peptide structure-function analysis: As a representative peptide derived from fibrinogen, Fibrinopeptide B is employed in structural biology and peptide chemistry studies. Researchers utilize it to investigate conformational dynamics, aggregation behavior, and interaction with other biomolecules. Such studies contribute to the broader understanding of peptide folding, stability, and the influence of post-translational modifications on biological activity. The insights gained from these analyses inform the rational design of peptide analogs and the development of novel biomaterials inspired by natural fibrinogen-derived sequences.
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