<p>The purified proteins were separated on a 12.5% gel under reducing or non-reducing conditions: (A) SDS-PAGE analysis of the purified MBL under reducing conditions; (B) SDS-PAGE analysis of the purified MBL under non-reducing conditions; (C) WB analysis of the purified MBL under non-reducing conditions; (D) WB analysis of the purified MBL under reducing conditions.</p
Polyacrylamide gel electrophoresis is a simple yet powerful means of resolving complex mixtures of p...
<p>Lane M: Molecular weight markers. Lanes 1 to 7: Fractions of purified recombinant tM2e-MBP protei...
<p>Proteins were extracted from purified MLBs, solubilized with denaturation solutions, and run on a...
<p>Proteins (∼2 µg per lane) were reduced with 5% BME or loaded on a 12% gel in non-reducing conditi...
<p>Total proteins in cells treated with or without the MOL extract were measured. Equal amounts of t...
<p>SDS-PAGE showing purification of biotinylated MBP from a crude sample using SAVSBPM32 Affi-gel. M...
<p>A.SDS-PAGE analysis of purified mRANKL. The fusion mRANKL was cleaved by Factor Xa, purified by a...
<p>Proteins were separated by SDS-PAGE and stained using Coomassie Brilliant Blue. Lane 1, pooled fr...
A Comassie blue stained SDS PAGE gel demonstrating the purification of MBP::LysM1. Lane 1 contains m...
<p>(a) The gel stained with Coomassie Brilliant Blue R-250. Lane M: protein marker; Lane 1: purified...
<p>SDS-PAGE analysis of the purified recombinant Xyl3A. Lanes: 1, the purified recombinant Xyl3A aft...
Lanes in panel A: 1, Mtb cytosol; 2, MtM; 3, MtM-SMALPs; 4, SMA-insoluble MtM and 5, lyophilized MtM...
<p>XeHypBA1 (A), XeHypBA2 (B), XeHypAA (C). M, protein molecular weight marker; lane 1, soluble prot...
<p>Proteins (0.7 mg/ml) were incubated for 3 h without Abs (odd numbers), 0.03 mg/ml csf-IgG<sub>mix...
Polyacrylamide gel electrophoresis (PAGE) is a widely used technique for separating proteins. The mo...
Polyacrylamide gel electrophoresis is a simple yet powerful means of resolving complex mixtures of p...
<p>Lane M: Molecular weight markers. Lanes 1 to 7: Fractions of purified recombinant tM2e-MBP protei...
<p>Proteins were extracted from purified MLBs, solubilized with denaturation solutions, and run on a...
<p>Proteins (∼2 µg per lane) were reduced with 5% BME or loaded on a 12% gel in non-reducing conditi...
<p>Total proteins in cells treated with or without the MOL extract were measured. Equal amounts of t...
<p>SDS-PAGE showing purification of biotinylated MBP from a crude sample using SAVSBPM32 Affi-gel. M...
<p>A.SDS-PAGE analysis of purified mRANKL. The fusion mRANKL was cleaved by Factor Xa, purified by a...
<p>Proteins were separated by SDS-PAGE and stained using Coomassie Brilliant Blue. Lane 1, pooled fr...
A Comassie blue stained SDS PAGE gel demonstrating the purification of MBP::LysM1. Lane 1 contains m...
<p>(a) The gel stained with Coomassie Brilliant Blue R-250. Lane M: protein marker; Lane 1: purified...
<p>SDS-PAGE analysis of the purified recombinant Xyl3A. Lanes: 1, the purified recombinant Xyl3A aft...
Lanes in panel A: 1, Mtb cytosol; 2, MtM; 3, MtM-SMALPs; 4, SMA-insoluble MtM and 5, lyophilized MtM...
<p>XeHypBA1 (A), XeHypBA2 (B), XeHypAA (C). M, protein molecular weight marker; lane 1, soluble prot...
<p>Proteins (0.7 mg/ml) were incubated for 3 h without Abs (odd numbers), 0.03 mg/ml csf-IgG<sub>mix...
Polyacrylamide gel electrophoresis (PAGE) is a widely used technique for separating proteins. The mo...
Polyacrylamide gel electrophoresis is a simple yet powerful means of resolving complex mixtures of p...
<p>Lane M: Molecular weight markers. Lanes 1 to 7: Fractions of purified recombinant tM2e-MBP protei...
<p>Proteins were extracted from purified MLBs, solubilized with denaturation solutions, and run on a...