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Fig.1 Construction of pET-28a-CD19scFv-IL-10R1 plasmid
Fig.2 Identification of PCR products of CD19scFv and IL-10R1 gene fragments(a) Agarose gel electrophoresis analysis of PCR product of CD19scFv (b) Agarose gel electrophoresis analysis of PCR product of IL-10R1
Fig.3 Identification of pET-28a-CD19scFv plasmid (a)and pET-28a-CD19scv-IL-10R1 plasmid (b)(a) pET-28a-CD19-scfv plasmid was treated with BamHI and HindIII 1: pET-28a; 2: Digestion with BamHI and HindIII (b) 1: pET-28a; 2: Digestion with BamHⅠ and XhoⅠ
Fig.4 Expression of CD19scFv protein at 25℃
Fig.5 Expression of CD19scFv-IL-10R1 protein at different temperatures and different IPTG concentrations(a) CD19scfv-IL-10R1 was expressed at 30 ℃ and (0.4mmol/L~2mmol/L) IPTG concentrations (b) CD19scfv-IL-10R1 was expressed at 25 ℃ and (0.4mmol/L~2mmol/L) IPTG concentrations (c) CD19scfv-IL-10R1 was expressed at 16 ℃ and (0.4mmol/L~2mmol/L) IPTG concentrations (d) CD19scfv-IL-10R1 was expressed at 4 ℃ and (0.4mmol/L~2mmol/L) IPTG concentrations
Fig.6 Determination of purified CD19scFv and CD19scFv-IL-10R1 recombinant protein by SDS PAGE and Western blot(a) SDS PAGE (b) Western blot
Fig.7 CD19-scfv-IL-10R1 binds to both CD19 and IL-10CD19scfv-IL-10R1/ CD19scFv-beads were incubated with cell lysate from LPS-treated B splenocytes. After washing the beads, Western blot was performed to identify the proteins captured by CD19scfv-IL-10R1/ CD19scFv-beads
Fig.1 Purine metabolism and cAMP synthesis pathway in Saccharomyces cerevisiae
Table 1 Xylose and glucose transport systems in yeast
Fig.1 Xylose transportation and fermentation in yeast
Table 2 Kinetics parameters of fungal transporters
Table 3 Kinetic parameters of yeast xylose transporters
Table 1 Primers for fragments amplification
Fig.1 Construction of expression vectors(a)The expression cassettes of designed expression plasmids (b) Identification of recombinant plasmids by SphⅠ & Xho I 1: pET-28a’; 2: pET-ELP₃₀; 3: pET-ELP₃₀-eGFP;4: pET-ELP₃₀-intein1-eGFP;5: pET-eGFP-intein2-ELP₃₀
Fig.2 Purification of ELP₃₀ and ELP₃₀-eGFPM: Protein maker; 1: Uninduced cell extract; 2: Purification of ELP₃₀ via ELP₃₀-tag;3: Purification of ELP₃₀-eGFP via ELP₃₀-tag; 4: Purification of ELP₃₀-eGFP via His-tag
Fig.3 Detection of fluorescence activity of recombinant proteinsA: PBS(used as negative control); B: ELP₃₀-eGFP;C: ELP₃₀-intein1-eGFP; D: eGFP-intein2-ELP₃₀. White scale bar represents 1 mm
Fig.4 Purification and cleavage of ELP₃₀-intein1-eGFPM: Protein maker; 1: Uninduced cell extract; 2:Supernatant of lysate of ELP₃₀-intein1-eGFP, 3: ELP₃₀-intein1-eGFP purification via ELP₃₀-tag; 4: Cleavage products of ELP₃₀-intein1-eGFP induced by pH shift; 5: Eluate gained by another ITC operation after the cleavage
Fig.5 Purification and cleavage of eGFP-intein2-ELP₃₀M: Protein maker; 1: Uninduced cell extract; 2: Supernatant of lysate of eGFP-intein2-ELP₃₀, 3: eGFP-intein2-ELP₃₀purification via ELP₃₀-tag; 4: Cleavage products of eGFP-intein2-ELP₃₀ induced by DTT; 5: Eluate gained by another ITC operation after the cleavage
Table 2 Recovery rate analysis of recombinant proteins
Table 1 Enrichment of phages in biopanning

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