Human Fibrinogen Matched Antibody Pair

Sample

Plasma

Species Reactivity

Human

Detection Method

Sandwich ELISA

Intended Use

This antibody pair set comes with matched antibody pair to detect and quantify protein level of Human FGA

Contents of Kit

1. Capture antibody (yellow):0.5 ml of affinity-purified polyclonal anti-fibrinogen antibody for coating plates.
2. Detecting antibody (red):0.5 ml of affinity-purified peroxidase conjugated polyclonal anti-fibrinogen antibody for detection of captured fibrinogen.
Note: Reagents are sufficient for at least 5×96 well plates using recommended protocols. Antibodies are supplied in a 50% (v/v) glycerol solution for storage at –10 to -20°C. Keep vials tightly capped. Do not store in frost-free freezers.

Storage

-10 to -20°C

General Description

Fibrinogen is an abundant plasma protein (5-10 uM) 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 Aα, Bβ and γ. 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, Aα1-16) followed by Fibrinopeptide B (FPB, Bβ1-14) 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 α, β and γ, 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 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. 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 γ 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.