Sheep anti Human Fibrinopeptide A polyclonal antibody [HRP]

Sheep Anti-Human Fibrinopeptide A polyclonal antibody for IEP, ELISA. Human fibrinogen is a 340 kDa plasma protein produced in the liver. Plasma concentrations are typically 1.7-3.5 g/L (5-13 µM). The intact fibrinogen molecule consists of two identical subunits, each consisting of three non-identical polypeptide chains d as A?, B? and ?. The letters A and B in the A? and B? chains designate, respectively, fibrinopeptide A (FpA, residues 1-16), and fibrinopeptide B (FpB, residues 1-14), which are cleaved by thrombin upon conversion of fibrinogen to fibrin. The fibrin monomers polymerize in a half-overlap fashion to form insoluble fibrin fibrils. The polymerised fibrin is subsequently stabilized by activated Factor XIII that forms amide linkages between ? chains and, to a lesser extent, ? chains of the fibrin molecules. Proteolysis of fibrinogen by plasmin initially liberates C-terminal residues from the A? chain to produce fragment X (intact D-E-D, which is still clottable). Fragment X is further degraded to nonclottable fragments Y (D-E) and D. Fragment Y can be digested into its constituent D and E fragments. Proteolysis of crosslinked fibrin by plasmin results in fragment DD (D-Dimer consisting of the D domains of 2 fibrin molecules crosslinked via the ? chains), fragment E (central E domain) as well as DDE in which fragment E is noncovalently associated with DD. The molecular weights of the cleavage fragments produced from human crosslinked fibrin are: 184 kDa for fragment DD, 92 kDa for D, 50 kDa for E, 1.54 kDa for FpA and 1.57 kDa for FpB. Most of the fibrinogen in the circulation consists of 2 copies of each chain (A?2, B?2, ?A2), but in normal plasma approximately 10% of the fibrinogen molecules contain one ?A chain and one variant ? chain (termed ?`), in which the c-terminal AGDV residues are replaced with the amino acid sequence VRPEHPAETEYDSLYPEDDL. This variant fibrinogen is commonly referred to as fibrinogen gamma prime (?A/?`) but has also been called fibrinogen 2 or peak 2 fibrinogen because it elutes separately from fibrinogen 1 (?A2) by ion exchange chromatography. Residues 414-427 of the ?` chain of fibrin gamma prime (contain a high-affinity binding site for exosite II of thrombin, which allows the active site of bound thrombin to remain available to interact with substrates while demonstrating resistance to heparin mediated inhibition by antithrombin.