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The Anti-Fibrinogen Protein A Scaffold molecule was selected against human fibrinogen. Cross reactivity with other species has not been tested. The Anti-Fibrinogen Protein A Scaffold molecule works very well for purification and depletion of fibrinogen from plasma. The Anti-Fibrinogen Protein A Scaffold molecule is modified with a unique C-terminal cysteine for directed single-point chemical modification, facilitating coupling to matrices.
Anti-Fibrinogen Protein A scaffold molecule binds to human fibrinogen. Cross reactivity with other species has not been tested.
At +4°C is recommended for lyophilized protein. For reconstituted protein in physiological buffer, short-term storage at +4°C is recommended. For long-term storage, the protein solution should first be aliquoted and stored frozen at -20°C. There is no dec
Fibrinogen is a globular and fibrous plasma protein of 340 kDa. It is essential for platelet aggregation and platelet plug formation (clotting) at the site of damage. Fibrinogen is a dimeric protein composed of three pairs of non- identical polypeptide chains held together by disulfide bonds. The polypeptide chains that are designated as the alpha, beta and gamma chains are 63, 56 and 47 kDa, respectively. Fibrinogen is synthesized exclusively in the liver by hepatic parenchymal cells and the level in circulation is maintained at 2.5-3.2 mg/ml. It belongs to the family of acute phase proteins and the levels rises up to seven-fold in response to trauma or inflammation. Individuals with hypofibrinogenimia may have a predisposition for bleeding whereas a complete absence of fibrinogen usually is fatal.
Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.