Recombinant Mouse FGA/Fibrinogen A protein (His tag)

Fibrinogen is a 340 kDa, secreted glycoprotein complex that is found in blood at concentrations of 150-400 mg/dL. It is secreted primarily by hepatocytes, but is also reported to be expressed by fibroblasts, type I alveolar epithelium, intestinal epithelium and some tumor cells. Fibrinogen is a homodimer that is composed of two, three-polypeptide chain subunits. Fibrinogen plays a central role in clot formation. Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon- (gamma-glutamyl) lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. Fibrinogen is also a component of the ECM and binds to cell surface molecules on inflammatory cells. Mature mouse alpha, beta and gamma-chains share 67%, 85% and 83% aa identity with human alpha, beta and gamma-chains, respectively.

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.