Fibrinogen (Factor I) is a soluble glycoprotein in blood plasma which is synthesized by the liver with a size of 340 kDa and circulating at a concentration of 2.6 to 3 mg/mL. Fibrinogen is a dimer linked by disulfide bridges composed of 3 pairs of non-identical polypeptide chains. Under the action of thrombin, fibrinogen is converted into fibrin. In association with FXIII, calcium ions, fibrin forms a stable network which ensures coagulation. The degradation products of the fibrinogen end produce Fragments D and E. Fragment D corresponds to the globular domains of fibrinogen, or fragment E corresponds to the amino acids of the N-terminal domain of the disulfide - knot domain.
All proteins are accompanied by certificates of analysis which determine the appropriate storage conditions. In order for us to guarantee the stability of the product, it is imperative that the storage conditions are respected. A brief centrifugation of the zymogens in their original packaging will completely recover the sample at the bottom of the tube. Never allow protein solutions to sit at room temperature for excessive periods of time. High temperatures can increase the rate of protein degradation. Avoid storing or maintaining diluted protein samples for a long period of time. In general, purified proteins are inherently more stable in concentrated form. Many proteins are “sticky” by nature. To avoid protein loss due to adsorption, highly concentrated protein samples should be prepared in buffers containing excipients such as bovine serum albumin, polyethylene glycol, Prionex, or gelatin.
Vial containing at least 5 mg of purified human fibrinogen. Main band of 340,000 daltons on SDS-PAGE.
This fibrinogen has a coagulability ≥ 98%
