Fig. 2
From: Phase separation propensity of the intrinsically disordered AB region of human RXRβ
Purification of AB_hRXRB. A Ion exchange (IEX) chromatography using a MonoS 5/50 GL column. The absorbance was monitored at 280 nm. The green line corresponds to the gradient of the NaCl concentration. Fractions from the II peak, containing pure AB_hRXRB, were combined, concentrated and used for further analysis. B SDS–PAGE analysis of the expression and purification of AB_hRXRB. The gel was stained with Coomassie Brilliant Blue R250. Lanes 1 and 8, molecular mass standard; Lane 2, the fraction of insoluble proteins obtained after cell lysis; Lane 3, the fraction of soluble proteins obtained after cell lysis; Lane 4, the fraction of proteins unbound to Talon® Metal Affinity Resin; Lanes 5 and 6, fraction of proteins eluted with buffers A and C, respectively; Lane 7, the combined fraction after digestion and elution with buffer C; Lane 9, fraction of protein impurities separated during IEX chromatography (peak I); Lane 10, combined fractions of pure AB_hRXRB eluted from the MonoS 5/50 GL column (peak II). The arrowhead marks the position of a band corresponding to AB_hRXRB