<p>Artificial cysteine-mutant scFv-C<sub>kappa</sub> fusion protein PEG conjugates were subjected to 4–12% (w/v) SDS-polyacrylamide gel electrophoresis without the addition of a reducing agent. After electrophoresis, the gel was stained with Coomassie Blue (A) or barium iodide (I<sub>2</sub>) (B). An artificial cysteine-mutant scFv-C<sub>kappa</sub> fusion protein not conjugated with PEG and the original scFv-C<sub>kappa</sub> fusion protein were used as controls.</p
Coomassie blue staining of all the recombinant sA28 mutant proteins after purification (for ITC anal...
(A). Analyses of purified WT and mutant sA28 proteins using gel filtration chromatography. Gel-filtr...
<p>Native gel electrophoresis (3–12% gel) and subsequent western blotting of cleared lysates. UT; Un...
<p>(A) Sixteen charge-variant artificial cysteine-mutant scFvs were prepared as scFv-PIII fusion pro...
<p>The binding activity of four charge-variant artificial cysteine-mutant scFv-C<sub>kappa</sub> fus...
<p>12% SDS-PAGE gel of the purified protein of hAS3MT mutants were stained with Coomassie blue.</p
<p><b>(A)</b> SDS-PAGE analysis of purified SK1-383C-PEG20 (C-terminal truncated cysteine mutant PEG...
<p>Coomassie blue stained 12% SDS-PAGE gel of the purified protein of hAS3MT mutants.</p
Molecular imaging employing fluorescent proteins has been widely used to highlight specific reaction...
<p>The binding activity of 157 cysteine-mutants in the form of scFv-pIII displayed on phage was test...
Molecular imaging employing fluorescent proteins has been widely used to highlight specific reaction...
<p>Immunoblotted SDS-polyacrylamide 7.5% gels with 10 μg of membrane protein run in each lane. Lanes...
The formation of oligomeric complexes is a crucial prerequisite for the proper structure and functio...
SDS-PAGE represents a quick and simple method for qualitative and quantitative analysis of protein...
<p>Samples were reduced and boiled prior to loading on a 15% SDS-PAGE gel, causing the TcpF chimera ...
Coomassie blue staining of all the recombinant sA28 mutant proteins after purification (for ITC anal...
(A). Analyses of purified WT and mutant sA28 proteins using gel filtration chromatography. Gel-filtr...
<p>Native gel electrophoresis (3–12% gel) and subsequent western blotting of cleared lysates. UT; Un...
<p>(A) Sixteen charge-variant artificial cysteine-mutant scFvs were prepared as scFv-PIII fusion pro...
<p>The binding activity of four charge-variant artificial cysteine-mutant scFv-C<sub>kappa</sub> fus...
<p>12% SDS-PAGE gel of the purified protein of hAS3MT mutants were stained with Coomassie blue.</p
<p><b>(A)</b> SDS-PAGE analysis of purified SK1-383C-PEG20 (C-terminal truncated cysteine mutant PEG...
<p>Coomassie blue stained 12% SDS-PAGE gel of the purified protein of hAS3MT mutants.</p
Molecular imaging employing fluorescent proteins has been widely used to highlight specific reaction...
<p>The binding activity of 157 cysteine-mutants in the form of scFv-pIII displayed on phage was test...
Molecular imaging employing fluorescent proteins has been widely used to highlight specific reaction...
<p>Immunoblotted SDS-polyacrylamide 7.5% gels with 10 μg of membrane protein run in each lane. Lanes...
The formation of oligomeric complexes is a crucial prerequisite for the proper structure and functio...
SDS-PAGE represents a quick and simple method for qualitative and quantitative analysis of protein...
<p>Samples were reduced and boiled prior to loading on a 15% SDS-PAGE gel, causing the TcpF chimera ...
Coomassie blue staining of all the recombinant sA28 mutant proteins after purification (for ITC anal...
(A). Analyses of purified WT and mutant sA28 proteins using gel filtration chromatography. Gel-filtr...
<p>Native gel electrophoresis (3–12% gel) and subsequent western blotting of cleared lysates. UT; Un...