The characterization of proteins was performed by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) under non-reducing conditions (8% polyacrylamide gel) and reducing conditions (10% polyacrylamide gel), followed by a Western blot analysis developed with a rabbit anti-human fibrinogen antibody (DAKO, Carpinteria, CA, USA) and horseradish peroxidase-conjugated goat anti-rabbit IgG antibody (Medical and Biological Laboratories Ltd, Nagoya, Japan), a mouse monoclonal antibody against the human fibrinogen -chain (2G10, specific for 15-35; Accurate Chemical and Scientific, Westbury, NY, USA) and horseradish peroxidase-conjugated goat anti-mouse IgG antibody (Medical and Biological Laboratories Ltd), or an anti-'-chain monoclonal antibody (specific for '408-427; Upstate, Lake Placid, NY, USA) and horseradish peroxidase-conjugated goat anti-mouse IgG antibody (Medical and Biological Laboratories Ltd), and enhanced with chemiluminescence detection reagents (Amersham Pharmacia Biotech, Buckinghamshire, UK). Blots were exposed on Hyperfilm-ECL (Amersham Pharmacia Biotech, Buckinghamshire, UK) [14] .
Mukai S., Nagata K., Ikeda M., Arai S., Sugano M., Honda T, & Okumura N. (2016). Genetic analyses of novel compound heterozygous hypodysfibrinogenemia, Tsukuba I: FGG c.1129+62_65 del AATA and FGG c.1299+4 del A. Thrombosis research, 148.
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