<p>The soluble fraction containing recombinant OlTGK1 (A) and OlTGK2 (B) proteins were purified using metal ion affinity-gel and size exclusion chromatography. Each sample was subjected to 7.5% SDS-PAGE following Coomassie Brilliant Blue staining: lane 1; applied samples for affinity chromatography, lane 2; flow-through fractions, lane 3; washed fractions, lane 4; eluted fractions, lane 5; the peak fractions from the size separation performed using Superdex-200 increase. M: molecular mass marker.</p
<p><b>(A)</b> The recombinant protein was analyzed by SDS-PAGE using 10% (v/v) polyacrylamide gels u...
New methods for the chromatographic isolation of inclusion bodies directly from crude Escherichia co...
The major purpose of this work was to determine if a protein i.e. Green Fluorescent Protein (GFP) co...
<p>(top left panel) SDS-PAGE with Coomassie staining and (remaining panels) size-exclusion chromatog...
Lane M, Molecular Marker (Color Prestained Protein Standard, Broad Range, NEB); lane 1, culture supe...
<p>The upper part of the figure shows a scheme of the purification steps followed to prepare the thr...
Protein purification is a complex and non-standardized process; the fact that proteins have differen...
<p>(A) Construction of the recombinant plasmid pGEX-5X-1-ERK8(28aa) which contains a GST-tag. (B) GS...
<p>Lane 1: Purified recombinant SjTGR protein on SDS-PAGE gel stained with Commassie Blue. MW: Prote...
<p>(A) Size exclusion chromatography using a HiLoad 16/600 Superdex 200 prep grade column. The absor...
<p>DDM solubilized supernatant was subjected to purification in buffer containing DDM (a and b) or L...
<p>A.SDS-PAGE analysis of purified mRANKL. The fusion mRANKL was cleaved by Factor Xa, purified by a...
<p>Lane (1) protein makers (kDa); Lane (2) 10 µg of soluble protein from uninduced cells; Lane (3) 1...
A Comassie blue stained SDS PAGE gel demonstrating the purification of MBP::LysM1. Lane 1 contains m...
The gene for a protein domain, derived from a tumor marker, fused to His tag codons and under contro...
<p><b>(A)</b> The recombinant protein was analyzed by SDS-PAGE using 10% (v/v) polyacrylamide gels u...
New methods for the chromatographic isolation of inclusion bodies directly from crude Escherichia co...
The major purpose of this work was to determine if a protein i.e. Green Fluorescent Protein (GFP) co...
<p>(top left panel) SDS-PAGE with Coomassie staining and (remaining panels) size-exclusion chromatog...
Lane M, Molecular Marker (Color Prestained Protein Standard, Broad Range, NEB); lane 1, culture supe...
<p>The upper part of the figure shows a scheme of the purification steps followed to prepare the thr...
Protein purification is a complex and non-standardized process; the fact that proteins have differen...
<p>(A) Construction of the recombinant plasmid pGEX-5X-1-ERK8(28aa) which contains a GST-tag. (B) GS...
<p>Lane 1: Purified recombinant SjTGR protein on SDS-PAGE gel stained with Commassie Blue. MW: Prote...
<p>(A) Size exclusion chromatography using a HiLoad 16/600 Superdex 200 prep grade column. The absor...
<p>DDM solubilized supernatant was subjected to purification in buffer containing DDM (a and b) or L...
<p>A.SDS-PAGE analysis of purified mRANKL. The fusion mRANKL was cleaved by Factor Xa, purified by a...
<p>Lane (1) protein makers (kDa); Lane (2) 10 µg of soluble protein from uninduced cells; Lane (3) 1...
A Comassie blue stained SDS PAGE gel demonstrating the purification of MBP::LysM1. Lane 1 contains m...
The gene for a protein domain, derived from a tumor marker, fused to His tag codons and under contro...
<p><b>(A)</b> The recombinant protein was analyzed by SDS-PAGE using 10% (v/v) polyacrylamide gels u...
New methods for the chromatographic isolation of inclusion bodies directly from crude Escherichia co...
The major purpose of this work was to determine if a protein i.e. Green Fluorescent Protein (GFP) co...