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. Author manuscript; available in PMC: 2016 Sep 1.
Published in final edited form as: Exp Eye Res. 2015 Jul 2;138:134–144. doi: 10.1016/j.exer.2015.06.027

Fig. 1.

Fig. 1

SDS-PAGE gel showing the purification of sNEP. The NEP extracellular catalytic domain was expressed as a soluble secreted protein in the Pichia expression system. sNEP was purified from conditioned media by first fractionating the conditioned media with ammonium sulfate followed by affinity chromatography on a Ni-NTA column. Left lane: molecular weight standards. Lane 1: ammonium sulfate fraction. Lane 2: flow-through from the Ni-NTA column. Lane 3: sNEP eluted from the Ni-NTA column. Protein bands were visualized by Coomassie Blue staining.