Recombinant Human Fibrinogen produced in HEK cells is comprised from the Aa chain (ACC# P02671), Bb chain (ACC# P02675) and g chain (ACC# P02679), having a total molecular weight of 340kDa. The Fibrinogen is purified by proprietary chromatographic techniques.
Fibrinogen is a blood-borne glycoprotein comprised of 3 pairs of nonidentical polypeptide chains. Fibrinogen is disulfide linked heterohexamer, which contains 2 sets of 3 non-identical chains (alpha, beta and gamma). Subsequent to vascular injury, fibrinogen is cleaved by thrombin to make fibrin which is the most abundant component of blood clots. Furthermore, different cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, exhibit vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Therefore, Fibrinogen has a double function: yielding monomers that polymerize into fibrin and functioning as a cofactor in platelet aggregation.
Sterile Filtered colorless solution.
The Fibrinogen solution (1mg/ml) contains 20mM Tris-HCl (pH7.4) and 154mM NaCl.
Store frozen at -20°C to -80°C for long periods of time. Avoid multiple freeze-thaw cycles.
>95% clottable. Clottability of the purified fibrinogens was determined as mixing human a-thrombin (final concentration 0.1 U/ml) and fibrinogen (final concentration 0.45 mg/ml) in 20mM Tris-HCl (pH7.4), 154mM NaCl, and 10mM CaCl2. Samples were incubated for 18 h at room temperature, and fibrin clot or fibrin aggregates were removed by centrifµgation at 13000
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