Fibrinogen gamma chain (E1U3Z) XP^® Rabbit mAb recognizes endogenous levels of total fibrinogen gamma chain protein. This antibody may cross-react with an unidentified protein of 70 kDa in some cell extracts.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser190 of human fibrinogen gamma chain protein.

Fibrinogen is a large, multimeric plasma glycoprotein that is constitutively synthesized by liver hepatocytes. As a key component of blood clots, fibrinogen plays a central role in hemostasis and thrombosis. In total, six polypeptide chains (2Aα, 2Bβ, and 2γ) are produced intracellularly in a coordinated manner, which are then covalently linked together by a network of disulfide bonds to form a fibrinogen heterohexamer (1). Research studies have shown that expression of the three fibrinogen genes is upregulated as part of the acute phase inflammatory response (2,3).

Upon engagement of the clotting cascade, thrombin-mediated cleavage of the fibrinogen Aα and Bβ chains creates fibrin monomers and a platform for the polymerization of fibrin monomers into protofibrils and an insoluble web of stable fibrin fibers (4,5). Whereas thrombin is the enzyme that drives fibrin polymerization and clot formation, plasmin is the enzymatic counterpart that facilitates fibrinolysis and clot breakdown (6).

In addition to its position as a central node in the normal coagulation cascade, dysregulated fibrin deposition has been observed in pathological conditions such as cancer and viral infection (7,8).
The fibrinogen gamma chain is expressed as two isoforms that result from alternative mRNA splicing, the γA chain and the γ' chain. Research studies have shown that the fibrinogen gamma chain plays important roles in shaping the architecture of fibrin clots and modulates the innate immune response through interaction with its receptor, CD11b, expressed on neutrophils and monocytes (9,10).