Figure 1From: Fully recombinant IgG2a Fc multimers (stradomers) effectively treat collagen-induced arthritis and prevent idiopathic thrombocytopenic purpura in miceStradomers form highly ordered multimers, which can be fractionated by size. (A) Stradomers consist of the murine IgG2a hinge, CH2, and CH3 domains (abbreviated as 2A), linked to a multimerization domain (MD) at the carboxy (C) or amino (N) terminus. The MD is either the human IgG2 hinge (2H) or an isoleucine zipper (ILZ). (B) SDS-PAGE of the stradomer proteins. Homodimeric 2A-2HC bands have a molecular mass of 55 kDa. Multimeric bands have a mass of 150 kDa or more. (C) The 2A-2HC protein was fractionated on a GE Highload Phenyl Sepharose High-Performance column (GE 17-1066-01) by using a standard protocol. The sample was run at a rate of 3 ml/min, and 2-ml fractions were collected. UV spectrometry at 280 nm was used to quantify protein in each fraction, yielding a histogram readout characterized by peaks representing the different fractions. (D) SDS-PAGE of unfractionated 2A-2HC, fraction I, fraction II, and fraction III. Homodimeric 2A-2HC bands have a mass of 55 kDa. Multimeric bands are higher at ≥ 100 kDa.Back to article page