Fibrinogen and Factor XIII (Fg, FXIII, FGA, FGB, FGG, F13A1, F13B)

Fibrinogen and Factor XIII are essential proteins in the final stage of blood coagulation[1][2][3][4][5][6]. After thrombin cleaves fibrinogen to release fibrin monomers that polymerize into insoluble strands, Factor XIII (activated by thrombin and calcium) acts as a transglutaminase to covalently cross-link fibrin, stabilizing the clot and protecting it from premature breakdown by fibrinolysis[2][3][4][5][6]. Both proteins play key roles beyond hemostasis, influencing wound healing, inflammation, innate immunity, and the structure of the extracellular matrix[1][4][5]. Disorders of either protein can manifest as bleeding disorders or problems with wound repair, and therapeutics are available to replace or modulate their function. While frequently studied together due to their functional linkage at the end of the coagulation cascade, they are structurally and genetically distinct entities.

Other names

Factor IFgFibrin stabilizing factorF13A1F13BFXIII

Replacement therapies (restore missing protein, promote normal clotting); Some drugs target the stabilization step (e.g., FXIII inhibitors in research); Fibrinolytic/antifibrinolytic agents modify clot degradation, indirectly interacting with fibrinogen/F XIII function