Skip to main content
Figure 1 | BMC Biotechnology

Figure 1

From: One single method to produce native and Tat-fused recombinant human α-synuclein in Escherichia coli

Figure 1

Representative purification of recombinant native AS on HiTrap chelating column (5 mL). A) An amount of periplasmic sample corresponding to 2 L of fermentation broth was loaded and eluted in 20 mM sodium phosphate, pH 7.4, 1 M NaCl. Following two washing steps at 5 and 10% of elution buffer to remove proteins aspecifically bound to the column, AS was eluted with 500 mM imidazole in 20 mM sodium phosphate, pH 7.4 (elution buffer). B) SDS-PAGE analysis of fractions eluted from HiTrap chelating column. P and PS: cell pellet after osmotic shock and periplasmic space content (both corresponding to 0.2 mL of fermentation broth); 0%, 5% and 100%: fractions eluted at different percentage of elution buffer; M: molecular mass standard proteins (GE Healthcare). TAT-AS: purified TAT-AS recombinant protein eluted at 100% of elution buffer.

Back to article page