Technical Data
Fibrinogen (Coagulation Factor I)
Fibrinogen, the precursor of fibrin, is the coagulable protein in the blood plasma of vertebrates. Fibrinogen consists as a dimer of 3 pairs of non-identical chains Aa (Mr= 66,800), Bb (Mr= 52,000) and g (Mr=46,500) cross-linked by disulfide bonds in their N-terminal segments. The molecule has 2 terminal D domains and one central E domain, all three domains are separated when fibrinogen is degradated by plasmin. MW is 340kD (1). Concentration in human plasma is 2-3mg/ml (2).

Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilutions:
ELISA: 1:8000
Western Blot: 1:1000
Optimal dilutions to be determined by the researcher.

X63-Ag8.653. Female CF1 x Balb/c mice immunized by intraperitoneal injection.

Culture Medium:
RPMI 1640 with 10% fetal calf serum

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, aliquot and store at -20C. Aliquots are stable for 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
MabIgG1,k6F100Affinity Purified
100ug-20CBlue IceHumanMouse
Fibrinogen isolated from human plasma.
Purified by Protein A/G affinity chromatography.
Supplied as a liquid in PBS, pH 7.2, 15mM sodium azide, before the addition of glycerol to 40%.
Recognizes human fibrinogen degradation product D-fragment. Reacts with both purified D-monomer, fibrinogen and factor VIII. Epitope specificity differs from that of clone 6F99 as determined by inhibition ELISA. Reacts strongly with D-monomer. Strong reaction is seen in ELISA with antigen directly coated onto the microtiter plate or in sandwich ELISA in combination with a polyclonal antibody against fibrinogen. In Western Blot after SDS-PAGE, this antibody reacts with fibrinogen degradation product D-monomer in nonreduced forms to create a band of approximately 92kD.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Doolittle RF (1977) Structure and function of fibrinogen. Horiz Biochem Biophys 3:164-191. 2. Scott T & Eagleson M (1988) Concise Encyclopedia Biochemistry: Walter de Gruyter, New York.