 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
journal menu
![[Figure 1]](rl5093fig1mag.jpg)
|
|
Figure 1
Protein characterization. (a) SDS–PAGE analysis of omalizumab, the omalizumab Fab, the recombinant IgE Fc and the Fab–Fc complex isolated by size-exclusion chromatography under nonreducing (left) and reducing (right) conditions. Lane M contains molecular-weight marker (labelled in kDa). (b) Immunoreactivity and functionality of the recombinant IgE Fc was assessed by ELISA using omalizumab, the Fab generated from omalizumab and a solubilized Fc∊RI fusion protein as the primary antibody and anti-human IgG, anti-human κ chain and anti-chicken IgY conjugated to alkaline phosphatase, respectively, for detection. (c) Biological activity of the recombinant IgE Fc in mediator-release assays. RBL-SX38 cells providing the human Fc∊RI were sensitized with IgE Fc. Degranulation was induced by the addition of anti-IgE and was monitored by the β-hexosaminidase activity released into the culture supernatants. Data are the mean ± standard deviation of triplicate measurements. (d) Analytical size-exclusion chromatography of the isolated omalizumab Fab IgE Fc proteins and their complex. For the latter, Fab and IgE Fc were mixed in a 2.1:1 molar ratio. |
![[Figure 1]](rl5093fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
