For immunochemical detection of citrullinated fibrinogen
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Measurement and Detection Tool(s)
400076Human Fibrinogen (PAD4 Citrullinated)
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Citrullinated Fibrinogen Monoclonal Antibody (Clone 10E9.3)

Item No. 17088

Technical Information
Immunogen
Human citrullinated fibrinogen
Clone Designation
10E9.3
MW
56 kDa
100 µg of protein G-purified antibody
Storage Buffer
PBS, pH 7.2, with 50% glycerol and 0.02% sodium azide
Host
Mouse
Isotype
IgG2b
Applications
ELISA, WB
Cross Reactivity
(-) Human Fibrinogen
Species Reactivity
(+) Human
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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Certificates of Analysis & Batch Specific Data

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    Product Description

    Fibrinogen is a hexameric glycoprotein that has roles in coagulation and hemostasis.1,2 It is comprised of two sets of Aα, Bβ, and γ polypeptide chains encoded by FGA, FGB, and FGG, respectively, in humans.1 Fibrinogen is synthesized in hepatocytes and secreted into the plasma. Following thrombin-mediated cleavage of N-terminal fibrinopeptides from the Aα and Bβ chains, yielding the α and β chains, respectively, fibrinogen assembles into fibrin protofibrils and then mature fibers, which provide structure and viscoelasticity to blood clots.2,3,4 Mutations in FGA, FGB, or FGG have been found in patients with afibrinogenemia or hypofibrinogenemia.1 Elevated plasma fibrinogen levels are associated with an increased risk of cardiovascular disease.5 Fibrinogen can be citrullinated by protein arginine deiminase 2 (PAD2) and PAD4.6 Immune complexes containing citrullinated fibrinogen have been found in patients with anti-citrullinated protein antibody-positive rheumatoid arthritis.7 Cayman’s Citrullinated Fibrinogen Monoclonal Antibody (Clone 10E9.3) can be used for ELISA and Western blot (WB) applications. The antibody recognizes citrullinated fibrinogen at 56 kDa from human samples.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. de Moerloose, P., Casini, A., and Neerman-Arbez, M. Congenital fibrinogen disorders: An update. Semin. Thromb. Hemost. 39(6), 585-595 (2013).

    2. Pieters, M., and Wolberg, A.S. Fibrinogen and fibrin: An illustrated review. Res. Pract. Thromb. Haemost. 3(2), 161-172 (2019).

    3. Mosesson, M.W. Fibrinogen and fibrin structure and functions. J. Thromb. Haemost. 3(8), 1894-1904 (2005).

    4. Weisel, J.W., and Litvinov, R.I. Fibrin formation, structure and properties. Subcell. Biochem. 82, 405-456 (2017).

    5. Kamath, S., and Lip, G.Y.H. Fibrinogen: Biochemistry, epidemiology and determinants. Q. J. M. 96(10), 711-729 (2003).

    6. Damgaard, D., Senolt, L., Nielsen, M.F., et alDemonstration of extracellular peptidylarginine deiminase (PAD) activity in synovial fluid of patients with rheumatoid arthritis using a novel assay for citrullination of fibrinogen. Arthritis Res. Ther. 16(6), 498 (2014).

    7. Sokolove, J., Zhao, X., Chandra, P.E., et alImmune complexes containing citrullinated fibrinogen costimulate macrophages via toll-like receptor 4 and Fcγ receptor. Arthritis Rheum. 63(1), 53-62 (2011).