<p>A chromatogram showing the two steps used in the purification of Xf-VapD: Xf-VapD fused with a trx-tag was obtained first, and then trypsin cleavage was used to remove the trx-tag. On the right, a 12.5% SDS-PAGE is shown for the Xf-VapD purification process. The lanes are as follows: M, protein marker; 1, Xf-VapD fused to trx-tag (31 kDa); 2, Xf-VapD and trx-tag after cleavage with trypsin; 3, totally purified Xf-VapD (16.5 kDa); and 4, trx-tag (~13 kDa). The gel was stained using Coomassie brilliant blue.</p
The “Strep tag” is a nine amino acid peptide with intrinsic streptavidin-binding activity. If this s...
Key assays in enzymology for the biochemical characterization of proteins in vitro necessitate high ...
a<p>Protein concentration was determined by Bradford assay.</p>b<p>Protein purity was determined by ...
<p>A two-step purification procedure was used to purify the proteins after being labeled with either...
<p>Purified F proteins were mock treated (−) or treated with increasing amounts of TPCK-Trypsin (T; ...
Proteins, which have inherent biorecognition properties, have long been used as therapeutic agents f...
<p>(A) Overview of the purification steps. (B) Coomassie blue stained SDS-PAGE gel and in gel fluore...
Protein purification is a crucial procedure in order to analyze the behavior, structure, and functio...
<p>(<b>A</b>) Imperial stained SDS-PAGE showing the purity of purified recombinant human full length...
The technique of three-phase partitioning (TPP) was used to purify the green fluorescent protein (GF...
The efficient removal of a N- or C-terminal purification tag from a fusion protein is necessary to o...
The efficient removal of a N-or C-terminal purification tag from a fusion protein is necessary to ob...
A. Agarose gel of pET28a-VvFrsA plasmid. M: DNA marker; 1: pET28a-VvFrsA plasmid after digestion wit...
<p>(A) Proteins were separated on an 18% SDS gel. M: molecular mass standard; P: cell-free expressed...
<p>The soluble fraction containing recombinant OlTGK1 (A) and OlTGK2 (B) proteins were purified usin...
The “Strep tag” is a nine amino acid peptide with intrinsic streptavidin-binding activity. If this s...
Key assays in enzymology for the biochemical characterization of proteins in vitro necessitate high ...
a<p>Protein concentration was determined by Bradford assay.</p>b<p>Protein purity was determined by ...
<p>A two-step purification procedure was used to purify the proteins after being labeled with either...
<p>Purified F proteins were mock treated (−) or treated with increasing amounts of TPCK-Trypsin (T; ...
Proteins, which have inherent biorecognition properties, have long been used as therapeutic agents f...
<p>(A) Overview of the purification steps. (B) Coomassie blue stained SDS-PAGE gel and in gel fluore...
Protein purification is a crucial procedure in order to analyze the behavior, structure, and functio...
<p>(<b>A</b>) Imperial stained SDS-PAGE showing the purity of purified recombinant human full length...
The technique of three-phase partitioning (TPP) was used to purify the green fluorescent protein (GF...
The efficient removal of a N- or C-terminal purification tag from a fusion protein is necessary to o...
The efficient removal of a N-or C-terminal purification tag from a fusion protein is necessary to ob...
A. Agarose gel of pET28a-VvFrsA plasmid. M: DNA marker; 1: pET28a-VvFrsA plasmid after digestion wit...
<p>(A) Proteins were separated on an 18% SDS gel. M: molecular mass standard; P: cell-free expressed...
<p>The soluble fraction containing recombinant OlTGK1 (A) and OlTGK2 (B) proteins were purified usin...
The “Strep tag” is a nine amino acid peptide with intrinsic streptavidin-binding activity. If this s...
Key assays in enzymology for the biochemical characterization of proteins in vitro necessitate high ...
a<p>Protein concentration was determined by Bradford assay.</p>b<p>Protein purity was determined by ...