Glycated fibrinogen produced by incubating fibrinogen with glucose
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Glycated Fibrinogen

Item No. 44245

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Purity
≥80% estimated by SDS-PAGE
Source
Fibrinogen, purified from human plasma, that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV
MW
α-chain isoform 1 (95 kDa), α-chain isoform 2 (69.8 kDa), β-chain (55.9 kDa) and isoform γ-B chain (51.5 kDa)
Formulation (Request formulation change)
20 mM HEPES, 154 mM sodium chloride, 10% glycerol, pH 7.4
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    1 mg

    $555

    Add
    Cayman Chemical
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    Product Description

    Fibrinogen is a hexameric glycoprotein that has roles in coagulation and hemostasis.1,2 It is composed 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 Under conditions of both intra- and extracellular hyperglycemia, fibrinogen is subject to glycation.5,6 Glycation occurs through multiple non-enzymatic mechanisms, including the formation of early glycation products such as glucosylamines and fructosamines at lysine residues and modification by highly reactive products, such as methylglyoxal (MGO), which are formed under oxidative stress induced by a hyperglycemic environment.6 Blood levels of glycated fibrinogen are increased in patients with type 2 diabetes.7 Cayman’s Glycated Fibrinogen was produced by incubating fibrinogen with glucose. This protein exhibits a >180% increase in glycation compared with a non-glycated fibrinogen control as confirmed by mass spectrometry.

    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. Borghi, S., Nencini, F., Giurranna, E., et al. Fibrinogen glycosylation and glycation: Molecular insights into thrombosis and vascular disease. Front. Mol. Biosci. 12, 1680332 (2025).

    6. Luzak, B., Boncler, M., Kosmalski, M., et al. Fibrinogen glycation and presence of glucose impair fibrin polymerization-an in vitro study of isolated fibrinogen and plasma from patients with diabetes mellitus. Biomolecules 10(6), 877 (2020).

    7. Pieters, M., Covic, N., Loots, d., et al. The effect of glycaemic control on fibrin network structure of type 2 diabetic subjects. Thromb. Haemost. 96(5), 623-629 (2006).