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. 2019 Oct 31;12(21):3576. doi: 10.3390/ma12213576

Figure 2.

Figure 2

Specificity of OX26-monoclonal antibodies (MAbs). (A) Elution diagram of collected OX-MAbs. X-axis: Elution fraction number; y-axis: Absorbance at 280 nm. (B) Coomasie Blue-stained SDS gel. Lane L, protein ladder (kDa). Lane 0, sample of antibody suspension before running on affinity column. Lane 1, sample from flow-through when loading affinity column with antibody suspension. Lane 2, sample of flow-through immediately before elution of antibodies. Lanes 3–9, elution fractions containing the expected 25 and 55 kDa bands representing components of OX26-MAbs. Lanes 5–7 contain the majority of OX26-MAbs corresponding to the high absorbance in A. The absence of 25 and 55 kDa bands in lane 1 indicates that OX26-MAbs were well adsorbed to the affinity column. (C–E) Merged images captured from RBE4 cells labeled with OX26-MAbs (C), commercial anti-CD71 (D), or secondary antibody alone (E). (F) The detection of OX26 in brain sections following the intravenous administration of 300 µg OX26-MAbs. (G–H) HeLa cells transfected with cDNA encoding rat transferrin receptor protein. Detection of the rat transferrin receptor protein using OX26-MAbs using FITC-conjugated secondary antibody (green) in transfected cells (G) and non-transfected cells (H), indicative of the affinity of OX26-MAbs for the rat transferrin receptor. Cellular nuclei stained with To-Pro3 (red). Scale bars = 20 µm (C–E), 20 µm (F), and 10 µm (G–H).