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Specificity: 8E5 binds to the amino-terminal region of the Beta-chain of human fibrin at an epitope consiting of GHRPLDKC. Binding is possible in both the monomeric form and the polymeric form of the protein. The epitope recognised by this clone is only accessible upon conversion of fibrinogen to fibrin, which entails the proteolytic removal of fibrinopeptides A & B from fibrinogen by thrombin. The antibody is there is therefore fibrin specific. Fibrin is a non-globular protein which plays a role in the clotting of blood and circulates as the precursor fibrinogen. Polymerization occurs through the action of the protease thrombin, which results in the active fibrin. Fibrin polymerizes as an insoluble matrix and forms a clot along with platelets over a wound site.
FIBB is the beta component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in its gene lead to several disorders, including afibrinogenemia, dysfibrinogenemia, hypodysfibrinogenemia and thrombotic tendency.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: epididymis secretory sperm binding protein Li 78p; Fibrinogen beta chain; fibrinogen, B beta polypeptide; MGC104327; MGC120405
Gene Aliases: FGB; HEL-S-78p
UniProt ID: (Human) P02675
Entrez Gene ID: (Human) 2244
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