Fibrinogen Antibodies

Affinity Biologicals, Inc. manufactures a broad range of Fibrinogen antibodies which can be found in the listing below.   Further information about each individual Fibrinogen antibody is available by following the associated links.  Our Fibrinogen antibodies are excellent for use in immunoassays where high sensitivity is required and are frequently the preferred reagent for immunopreciptaion techniques and activity neutralization assays.  These antibodies have proven to be extremely useful in the preparation of immune-adsorbent resins for use in immuno-depletion of specific proteins from plasma as well as immuno-affinity purification of proteins.  Affinity’s Fibrinogen antibodies are manufactured for use in research applications.

Fibrinogen, HumanHostCatalogue No.Size
Purified IgGSheepSAFG-IG10mg vial
Affinity Purified IgGSheepSAFG-AP0.5mg vial
Peroxidase Conjugated IgGSheepSAFG-HRP0.2mg vial
Affinity Purified, Peroxidase conj. IgGSheepSAFG-APHRP0.1mg vial
Matched Pair Antibodies for EIAFG-EIA5 plates
Fibrinogen, RabbitHostCatalogue No.Size
Purified IgGSheepSARFG-IG10mg vial
Affinity Purified IgGSheepSARFG-AP0.5mg vial
Peroxidase Conjugated IgGSheepSARFG-HRP0.2mg vial
Matched Pair Antibody Set for EIARBFG-EIA4 plates
Fibrinogen, Murine Catalogue No.Size
Matched Pair Antibody Set for EIAMFG-EIA4 plates
Fibrin Fragment E, HumanHostCatalogue No.Size
Purified IgGSheepSAFNE-IG10mg vial
Peroxidase Conjugated IgGSheepSAFNE-HRP0.2mg vial
Fibrinogen, gamma prime, HumanHostCatalogue No.Size
Purified IgGSheepSAFGP-IG10mg vial
Peroxidase Conjugated IgGSheepSAFGP-HRP0.2mg vial
Fibrinopeptide A, HumanHostCatalogue No.Size
Purified IgGSheepSAFPA-IG10mg vial
Affinity Purified IgGSheepSAFPA-AP0.5mg vial
Peroxidase Conjugated IgGSheepSAFPA-HRP0.2mg vial

Listing of Fibrinogen Antibodies

Description of Fibrinogen (Fg)

Human fibrinogen is a 340 kDa plasma protein produced in the liver.  Plasma concentrations are typically 1.7 – 3.5 g/L (5-10 μM).  The intact fibrinogen molecule consists of two identical subunits, each consisting of three non-identical polypeptide chains denoted as Aα, Bβ and γ.  The letters A and B in the Aα and Bβ 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 γ chains and, to a lesser extent, α chains of the fibrin molecules.

Proteolysis of fibrinogen by plasmin initially liberates C-terminal residues from the Aα chain to produce fragment X (intact D-E-D, which is still clottable).  Fragment X is further degraded to non-clottable 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 γ chains), fragment E (central E domain) as well as DDE in which fragment E is non-covalently 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 (Aα2, Bβ2, γA2), but in normal plasma approximately 10% of the fibrinogen molecules contain one γA chain and one variant γ chain (termed γ), 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 (γA) but has also been called fibrinogen 2 or peak 2 fibrinogen because it elutes separately from fibrinogen 1 (γA2) by ion exchange chromatography.  Residues 414-427 of the γ 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 antithrombin1-4.

References and Reviews

  1. Hantgan RR, Francis CW, Marder VJ; Fibrinogen Structure and Physiology; in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp 277-300, J.B. Lippincott Co., Philadelphia PA, USA, 1994.
  2. Binnie CG, Lord ST; The Fibrinogen Sequences that Interact with Thrombin;  Blood 81,  pp 3186-3192, 1993.
  3. Pospisil CH, Stafford AR, Fredenburgh JC, Weitz JI; Evidence that both Exosites on Thrombin Participate in Its High Affinity Interaction with Fibrin; JBC 278, pp 21584-21591, 2003.
  4. Medved L, Weisel JW; Recommendations for Nomenclature on Fibrinogen and Fibrin; JTH 7, pp 355-359, 2009.