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Fig. 3. SDS-PAGE of expressed and purified recombinant proteins of the two types of medaka Wap65, mWap65-1 and mWap65-2. (A) Purification of recombinant mWap65-1 (rWap65-1). Lane 1, control total cell lysates of Escherichia coli BL21 used as host cell; lane 2, total cell lysate after induction; lane 3, soluble fraction; lane 4, insoluble fraction; lane 5, the fraction containing solubilized rWap65-1; lane 6, eluate after GSTrap affinity purification. (B) Purification of recombinant mWap65-2 (rWap65-2). Lane 7, control total cell lysates of E. coli BL21 (DE3) used as host cell; lane 8, total cell lysate after induction; lane 9, periplasm fraction; lane 10, soluble fraction; lane 11, insoluble fraction; lane 12, eluate after HiTrap affinity purification. 10–20 µg of protein were loaded in lanes 1–8, 10 and 11, and 5 µg in lanes 9 and 12. M, molecular mass standards (kDa). The positions of rWap65-1 and rWap65-2 in SDS-PAGE gels are marked by black and white arrowheads, respectively.