American Society of Hematology

Fig. 1.

$Fig. 1. Purification of sIL-11R. (A) Western blot of CHO sIL-11R eluates from anti-FLAG M2 affinity column. Numbers above represent fractions (0.5 mL) eluted with FLAG peptide (50 μg/mL). SM, starting material; BT, breakthrough when loaded onto affinity column. Blots probed with anti-FLAG antibody. Samples prepared by mixing with equal volume of 2× nonreducing (left side of gel) or reducing (right side of gel) sample buffer and run on 8% to 25% SDS-PAGE. Molecular weights on left side (kD). (B) Chromatogram of Superdex 75 gel filtration (Pharmacia) of pooled fractions 4 to 6. (C) Silver stain of nonreducing SDS-PAGE of fractions 40 through 44 from gel filtration. (D) Silver stain gel of pooled fractions before (lane 1) and after (lane 2) deglycosylation with N-glycanase F as described in experimental methods.$

Purification of sIL-11R. (A) Western blot of CHO sIL-11R eluates from anti-FLAG M2 affinity column. Numbers above represent fractions (0.5 mL) eluted with FLAG peptide (50 μg/mL). SM, starting material; BT, breakthrough when loaded onto affinity column. Blots probed with anti-FLAG antibody. Samples prepared by mixing with equal volume of 2× nonreducing (left side of gel) or reducing (right side of gel) sample buffer and run on 8% to 25% SDS-PAGE. Molecular weights on left side (kD). (B) Chromatogram of Superdex 75 gel filtration (Pharmacia) of pooled fractions 4 to 6. (C) Silver stain of nonreducing SDS-PAGE of fractions 40 through 44 from gel filtration. (D) Silver stain gel of pooled fractions before (lane 1) and after (lane 2) deglycosylation with N-glycanase F as described in experimental methods.

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