Reactivity
Human
(tested or 100% immunogen sequence identity)
Specificity
Recognizes human fibrinogen, a complex ~340kD hetero-hexameric (di-trimeric) glycoprotein consisting of 3 pairs of alpha, beta and gamma chains linked by a series of 29 disulphide bonds. The six chains are arranged in such a way that all the N-Terminal ends adjoin to form a central with two trimeric coiled coil structures connecting to outer D domains. Fibrinogen plays an important role in the coagulation process with the D and E domains interacting via the C-Terminal ends of the alpha chains during fibrin clot cross-linking. Shows minimal cross-reactivity with related serum proteins. Fibrinogen has been identified as a ferritin binding protein in the horse. Has been successfully as a capture reagent for ferritin - anti ferritin IgG complexes in horse plasma to evaluate the antibody response to ferritin by ELISA.