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. 2018 Jun 14;13(6):e0197971. doi: 10.1371/journal.pone.0197971

Fig 1. SDS-PAGE analysis of the recombinant Sola l 4.02 protein.

Fig 1

(A) Purification from soluble protein fraction, SDS-PAGE under reducing condition with ß-mercaptoethanol (A1 crude extract; A2 flow through; A3 washing; A4 elution 1; A5 elution 2; A6 elution 3). (B) insoluble protein fractions, SDS-PAGE under non-reducing conditions (B1 denaturation; B2 refolding; B3 flow through; B4 elution 1; B5 elution 2; B6 elution 3). (C) insoluble protein fraction (C1 pooled elution 1–3). Under non-reducing conditions, (B) two distinct protein bands were visible in the elution fractions at 18 kDa and 36 kDa. Under reducing condition with ß-mercaptoethanol (A, C) only one band at approximately 18 kDa appeared. Five μg protein per lane were visualized by Coomassie Brilliant Blue G250. M: PageRuler Plus Prestained Protein Ladder.