<p>The protein preparations were separated on 10% (A) and 12% (B) NuPAGE BisTris gels, and stained by Coomassie Brilliant Blue R-250. The lanes on A were 1, molecular mass standards; 2, CS6 protein, and the lanes on B were 1, molecular mass standards; 2, CssA protein (with polyhistidine tag); 3, CssB protein (fused to glutathione-S-transferase (26 kDa) and with polyhistidine tag).</p
<p>(A) 1% agarose gel stained with ethidium bromide and (B) 15% acrylamide gel stained with Comassie...
<p>The electrophoresis showed a 40 kDa protein band. M: protein markers (lanes concentrations: 0.1∼0...
<p><b>A.</b> Purification of the protein expressed in the shaker. In the 10% polyacrylamide gel, wel...
<p>Purified protein extracts were separated in SDS–12.5% polyacrylamide gels and stained with Coomas...
<p>Expression and purification analysis of recombinant proteins Lsa46 <b>(A)</b> and Lsa77 <b>(E)</b...
<p>After purification steps, different elution fractions of purified N recombinant protein were sepa...
(A) Protein gel (left) and corresponding western blot (right) probed for GST showing purified 6 μg G...
Purified wild-type (WT) recombinant Nus-BB0562, single (S34A; S34T; S58A; S58T) and double mutant (S...
<p>Characterisation of over expressed recombinant fusion protein GST-MC084S and FPLC purified recomb...
<p>Samples were reduced and boiled prior to loading on a 15% SDS-PAGE gel, causing the TcpF chimera ...
<p>GST and GST-ST1, -ST2 and -ST3 fusions proteins were expressed in <i>E.coli</i>, extracted, and r...
<p>SDS-PAGE (10%) of purified recombinant proteins from <i>E.coli</i> BL-21 transformed with pGEX-<i...
<p>Lane 1: Purified recombinant SjTGR protein on SDS-PAGE gel stained with Commassie Blue. MW: Prote...
<p>The soluble fraction containing recombinant OlTGK1 (A) and OlTGK2 (B) proteins were purified usin...
(A) Purification of Cas9 by affinity chromatography using a Nickel-charged HiTrap Chelating HP. Grad...
<p>(A) 1% agarose gel stained with ethidium bromide and (B) 15% acrylamide gel stained with Comassie...
<p>The electrophoresis showed a 40 kDa protein band. M: protein markers (lanes concentrations: 0.1∼0...
<p><b>A.</b> Purification of the protein expressed in the shaker. In the 10% polyacrylamide gel, wel...
<p>Purified protein extracts were separated in SDS–12.5% polyacrylamide gels and stained with Coomas...
<p>Expression and purification analysis of recombinant proteins Lsa46 <b>(A)</b> and Lsa77 <b>(E)</b...
<p>After purification steps, different elution fractions of purified N recombinant protein were sepa...
(A) Protein gel (left) and corresponding western blot (right) probed for GST showing purified 6 μg G...
Purified wild-type (WT) recombinant Nus-BB0562, single (S34A; S34T; S58A; S58T) and double mutant (S...
<p>Characterisation of over expressed recombinant fusion protein GST-MC084S and FPLC purified recomb...
<p>Samples were reduced and boiled prior to loading on a 15% SDS-PAGE gel, causing the TcpF chimera ...
<p>GST and GST-ST1, -ST2 and -ST3 fusions proteins were expressed in <i>E.coli</i>, extracted, and r...
<p>SDS-PAGE (10%) of purified recombinant proteins from <i>E.coli</i> BL-21 transformed with pGEX-<i...
<p>Lane 1: Purified recombinant SjTGR protein on SDS-PAGE gel stained with Commassie Blue. MW: Prote...
<p>The soluble fraction containing recombinant OlTGK1 (A) and OlTGK2 (B) proteins were purified usin...
(A) Purification of Cas9 by affinity chromatography using a Nickel-charged HiTrap Chelating HP. Grad...
<p>(A) 1% agarose gel stained with ethidium bromide and (B) 15% acrylamide gel stained with Comassie...
<p>The electrophoresis showed a 40 kDa protein band. M: protein markers (lanes concentrations: 0.1∼0...
<p><b>A.</b> Purification of the protein expressed in the shaker. In the 10% polyacrylamide gel, wel...