|Tested species reactivity||Human|
|Host / Isotype||Sheep / IgG|
|Immunogen||Synthetic fibrinopeptide corresponding to Aα 1-16 conjugated to carrier.|
|Storage buffer||0.01M HEPES, pH 7.4, with 0.15M NaCl, 50% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|ELISA (ELISA)||Assay Dependent|
|Immunoelectrophoresis (IE)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
PA1-74099 detects Fibrinopeptide A from human samples.
PA1-74099 has been successfully used in Immunoelectrophoresis, and ELISA applications.
The PA1-74099 immunogen is a synthetic peptide correspnnding to residues 1-16 of human FPA..
Fibrinogen is an abundant plasma protein (5-10 µM) produced in the liver. The intact protein has a molecular weight of 340 kDa and is composed of 3 pairs of disulphide-bound polypeptide chains named Aa, Bß and ?. Fibrinogen is a triglobular protein consisting of a central E domain and terminal D domains. Proteolysis by thrombin results in release of Fibrinopeptide A (FPA, Aa1-16) followed by Fibrinopeptide B (FPB, Bß1-14) and the fibrin monomers that result polymerize in a half-overlap fashion to form insoluble fibrin fibrils.The chains of fibrin are referred to as a, ß and ?, due to the removal of FPA and FPB. The polymerised fibrin is subsequently stabilized by the transglutaminase activated Factor XIII that forms amide linkages between ? chains and, to a lesser extent, a chains of the fibrinn molecules. Proteolysis of fibrinogen by plasmin initially liberates Cterminal residues from the Aa chain to produce fragment X (intact DE- 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. Digestion of non-crosslinked fibrin with plasmin is very similar to the digestion of fibrinogen, which results in production of fragments D and E. Degradation 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 non-covalently associated with DD. For human crosslinked fibrin, the relative weights of the cleavage fragments produced 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 1-3.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.