Fibrinopeptide A, human TFA is a native N-terminal fibrinogen segment enriched in acidic and aromatic residues. The peptide contributes to studies of fibrin assembly, proteolytic cleavage, and conformational motifs. Researchers employ it in structural mapping, solvent-dependent folding, and kinetic assays. Its trifluoroacetate form supports consistent handling in analytical work.
CAT No: R2218
CAS No:61533-47-9
Synonyms/Alias:FIBRINOPEPTIDE A, HUMAN TFA;61533-47-9;G13977;
Fibrinopeptide A, human tfa, is a synthetic peptide fragment derived from the N-terminal region of the human fibrinogen alpha chain. As a critical cleavage product released during the enzymatic action of thrombin on fibrinogen, this peptide has become an invaluable tool in various fields of biochemical and biomedical research. Its unique amino acid sequence and structural properties enable precise modeling of physiological and pathological processes related to blood coagulation. Researchers favor Fibrinopeptide A for its stability, reproducibility, and compatibility with a wide range of analytical techniques, making it a versatile asset in both exploratory and applied scientific investigations.
Blood Coagulation Research: In the study of hemostasis and thrombosis, Fibrinopeptide A provides a direct readout of thrombin activity, as it is one of the first peptides released during the conversion of fibrinogen to fibrin. Scientists utilize this peptide to monitor the kinetics of clot formation, dissect the molecular mechanisms underpinning coagulation, and evaluate the efficacy of anticoagulant compounds in vitro. By quantifying the release of this fragment, researchers can accurately map the initiation and progression of clotting cascades under various experimental conditions, gaining insights into both normal and pathological states.
Proteomics and Mass Spectrometry Calibration: In proteomics, human tfa serves as an ideal internal standard or calibration peptide for mass spectrometry-based analyses. Its well-characterized mass and fragmentation pattern allow for the fine-tuning of instrument sensitivity and accuracy, ensuring reliable peptide identification and quantification. Laboratories often spike samples with this peptide to validate analytical workflows, troubleshoot instrument performance, and benchmark novel mass spectrometric techniques, contributing to the reproducibility and comparability of proteomic datasets across different platforms.
Biomarker Discovery and Quantification: As an established marker of thrombin generation, Fibrinopeptide A is extensively employed in the search for novel biomarkers of cardiovascular and thrombotic disorders. Quantitative assays measuring its concentration in biological fluids provide critical data for understanding disease mechanisms and identifying potential risk factors. Researchers leverage its presence in plasma to develop new diagnostic tools, assess the impact of therapeutic interventions, and explore the dynamic interplay between coagulation and inflammation in various pathological contexts.
Enzyme Kinetics and Substrate Specificity Studies: The synthetic peptide is widely used to characterize the specificity and kinetics of proteolytic enzymes, particularly thrombin and related serine proteases. By offering a defined substrate, it enables precise monitoring of enzymatic cleavage events, facilitating the development of inhibitors and the elucidation of structure-function relationships. This application is fundamental to drug discovery efforts targeting coagulation pathways, as well as to the broader understanding of protease regulation in human health and disease.
Antibody Production and Immunoassay Development: Fibrinopeptide A, human tfa, is frequently utilized as an immunogen or assay standard in the generation of specific antibodies and the design of immunoassays. Its defined sequence allows for the production of high-affinity monoclonal and polyclonal antibodies, which are essential for sensitive and specific detection in research and diagnostic settings. These antibodies underpin a variety of immunological techniques, including ELISA and western blotting, enabling the quantitative and qualitative analysis of thrombin activity and fibrin formation in complex biological samples. Through these diverse applications, Fibrinopeptide A continues to advance scientific understanding and technical innovation across multiple domains of biochemical research.
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4. TMEM16F and dynamins control expansive plasma membrane reservoirs
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