Monoclonal Anti-Fibrinogen antibody produced in mouse

Fibrinogen is a blood coagulation protein that consists of Aα, Bβ and γ polypeptide chains. Fibrinogen expression is induced by acute-inflammatory responses and has also been associated with the risk of cardiovascular disorders. Monoclonal Anti-Fibrinogen antibody recognizes a conformational epitope, which is destroyed by the cleavage of the γ (302-303) bond. This epitope is found in fibrinogen and in fibrin monomers (devoid of either fibrinopeptide A, or both A and B fibrinopeptides), when they are immobilized on ELISA plates. The antibody reacts with the D-dimer and D-fragment. It does not recognize individual fibrinogen/fibrin chains in denatured-reduced forms or their proteolytic fragments. The E fragment is not recognized by the antibody. The antibody reacts with greater avidity with protofibrils than with wider fibrin fibers in electron microscopic analysis. Monoclonal Anti-Fibrinogen is specific for fibrinogen and fibrin in humans, baboons, bovines, sheep, goats, pigs, rabbits and dogs.

Fibrinogen was the first blood coagulation factor to be identified, and it is a precursor of fibrin protein. The three polypeptide chains are coded by three genes located on human chromosome 4q23-q32, and spans 51kb.

human fibrin degradation products

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)

Monoclonal Anti-Fibrinogen antibody is suitable for use in indirect ELISA, dot blot (1:1000 using human fibrinogen), and western blot.

Monoclonal Anti-Fibrinogen antibody produced in mouse has been used in immunohistochemistry and confocal laser scanning microscopy.

Fibrinogen is an acute-phase inflammatory protein, which plays an essential role in blood clotting.

The product recognizes a conformational epitope, which is destroyed by the cleavage of the γ (302-303) bond. This epitope is found in both fibrinogen and in fibrin monomers, devoid of either fibrinopeptide A, or both A and B fibrinopeptides, when they are immobilized on ELISA plates. The antibody reacts with the D-dimer and D-fragment. It does not recognize individual fibrinogen/fibrin chains in the denatured-reduced form and their proteolytic fragments. The E fragment is not recognized by the antibody. Using electron microscopy, the antibody reacts with greater avidity with protofibrils than with wider fibrin fibers.

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