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  • 96
    Millipore gel filtration markers kit
    Gel Filtration Markers Kit, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 417 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad size exclusion chromatography gel filtration
    Size Exclusion Chromatography Gel Filtration, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad gel filtration chromatography gel filtration chromatography
    Elution patterns of gintonin prepared from ginseng root by <t>gel</t> <t>chromatography.</t> Gel <t>filtration</t> chromatograms on Superdex 75 column with phosphate buffered saline (pH 7.2) of edible gintonin prepared from ginseng root. Analysis through gel filtration chromatograms showed one main peak and other minor peaks. The main peak was active for the activation of Ca 2+ -activated Cl - channel.
    Gel Filtration Chromatography Gel Filtration Chromatography, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 55 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bio-Rad gel permeation chromatography
    Elution patterns of gintonin prepared from ginseng root by <t>gel</t> <t>chromatography.</t> Gel <t>filtration</t> chromatograms on Superdex 75 column with phosphate buffered saline (pH 7.2) of edible gintonin prepared from ginseng root. Analysis through gel filtration chromatograms showed one main peak and other minor peaks. The main peak was active for the activation of Ca 2+ -activated Cl - channel.
    Gel Permeation Chromatography, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 50 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    GE Healthcare hplc size exclusion gel filtration chromatography
    Elution patterns of gintonin prepared from ginseng root by <t>gel</t> <t>chromatography.</t> Gel <t>filtration</t> chromatograms on Superdex 75 column with phosphate buffered saline (pH 7.2) of edible gintonin prepared from ginseng root. Analysis through gel filtration chromatograms showed one main peak and other minor peaks. The main peak was active for the activation of Ca 2+ -activated Cl - channel.
    Hplc Size Exclusion Gel Filtration Chromatography, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare size exclusion chromatography gel filtration
    <t>Size</t> <t>exclusion</t> <t>chromatography</t> and SDS-PAGE analyses on AbHemL, HemA-HemL complex and AbHemA. Elution profiles of Ab HemL (A) , fractions from Ab HemA-HemL complex corresponding to lane 2 of Figure 2B and lane 3 from Figure 2C and Ab HemA (D) . Rigth panels are the SDS-PAGE of the same samples analyzed on SEC (S) and fractions from SEC at 8, 14, and 15 ml elution volume. In right panel (B) , the black line indicates that the image was assembled from two different gels. White lines on right panels (C,D) separate different parts of the same <t>gel</t> that were combined, excluding lanes which were not of interest. Original gels from which panels were assembled are shown in the Supplementary Materials .
    Size Exclusion Chromatography Gel Filtration, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 89/100, based on 162 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare gel filtration size exclusion chromatography
    Fractionation of IMAC-purified recombinant Pr78 Gag protein by <t>size</t> <t>exclusion</t> <t>chromatography.</t> ( a ) Absorbance versus elution time chromatogram plotted from the data obtained from a Superdex 200 column showing peak fractions with maximum absorbance containing purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1. ( b ) Coomassie Brilliant Blue-stained SDS-polyacrylamide <t>gel</t> showing the resolution of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1 in fractions 18–26. ( c ) Western blot analysis of pooled peak fractions (22–24) of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein analyzed with anti-Pr78 Gag polyserum, and ( d ) anti-6x-His monoclonal antibody, respectively.
    Gel Filtration Size Exclusion Chromatography, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 2845 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Malvern Panalytical size exclusion chromatography gel filtration
    Fractionation of IMAC-purified recombinant Pr78 Gag protein by <t>size</t> <t>exclusion</t> <t>chromatography.</t> ( a ) Absorbance versus elution time chromatogram plotted from the data obtained from a Superdex 200 column showing peak fractions with maximum absorbance containing purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1. ( b ) Coomassie Brilliant Blue-stained SDS-polyacrylamide <t>gel</t> showing the resolution of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1 in fractions 18–26. ( c ) Western blot analysis of pooled peak fractions (22–24) of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein analyzed with anti-Pr78 Gag polyserum, and ( d ) anti-6x-His monoclonal antibody, respectively.
    Size Exclusion Chromatography Gel Filtration, supplied by Malvern Panalytical, used in various techniques. Bioz Stars score: 89/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Tosoh Corporation gel permeation chromatography
    Fractionation of IMAC-purified recombinant Pr78 Gag protein by <t>size</t> <t>exclusion</t> <t>chromatography.</t> ( a ) Absorbance versus elution time chromatogram plotted from the data obtained from a Superdex 200 column showing peak fractions with maximum absorbance containing purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1. ( b ) Coomassie Brilliant Blue-stained SDS-polyacrylamide <t>gel</t> showing the resolution of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1 in fractions 18–26. ( c ) Western blot analysis of pooled peak fractions (22–24) of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein analyzed with anti-Pr78 Gag polyserum, and ( d ) anti-6x-His monoclonal antibody, respectively.
    Gel Permeation Chromatography, supplied by Tosoh Corporation, used in various techniques. Bioz Stars score: 92/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Phenomenex size exclusion chromatography
    Fractionation of IMAC-purified recombinant Pr78 Gag protein by <t>size</t> <t>exclusion</t> <t>chromatography.</t> ( a ) Absorbance versus elution time chromatogram plotted from the data obtained from a Superdex 200 column showing peak fractions with maximum absorbance containing purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1. ( b ) Coomassie Brilliant Blue-stained SDS-polyacrylamide <t>gel</t> showing the resolution of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1 in fractions 18–26. ( c ) Western blot analysis of pooled peak fractions (22–24) of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein analyzed with anti-Pr78 Gag polyserum, and ( d ) anti-6x-His monoclonal antibody, respectively.
    Size Exclusion Chromatography, supplied by Phenomenex, used in various techniques. Bioz Stars score: 93/100, based on 379 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore size exclusion chromatography
    Fractionation of IMAC-purified recombinant Pr78 Gag protein by <t>size</t> <t>exclusion</t> <t>chromatography.</t> ( a ) Absorbance versus elution time chromatogram plotted from the data obtained from a Superdex 200 column showing peak fractions with maximum absorbance containing purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1. ( b ) Coomassie Brilliant Blue-stained SDS-polyacrylamide <t>gel</t> showing the resolution of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1 in fractions 18–26. ( c ) Western blot analysis of pooled peak fractions (22–24) of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein analyzed with anti-Pr78 Gag polyserum, and ( d ) anti-6x-His monoclonal antibody, respectively.
    Size Exclusion Chromatography, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 589 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Elution patterns of gintonin prepared from ginseng root by gel chromatography. Gel filtration chromatograms on Superdex 75 column with phosphate buffered saline (pH 7.2) of edible gintonin prepared from ginseng root. Analysis through gel filtration chromatograms showed one main peak and other minor peaks. The main peak was active for the activation of Ca 2+ -activated Cl - channel.

    Journal: Journal of Ginseng Research

    Article Title: An Edible Gintonin Preparation from Ginseng

    doi: 10.5142/jgr.2011.35.4.471

    Figure Lengend Snippet: Elution patterns of gintonin prepared from ginseng root by gel chromatography. Gel filtration chromatograms on Superdex 75 column with phosphate buffered saline (pH 7.2) of edible gintonin prepared from ginseng root. Analysis through gel filtration chromatograms showed one main peak and other minor peaks. The main peak was active for the activation of Ca 2+ -activated Cl - channel.

    Article Snippet: Gel filtration chromatography Gel filtration chromatography of the gintonin fraction obtained from ginseng root was carried out by a Superdex 75 column (10×300 mm) equilibrated with PBS on BioLogic DuoFlow chromatography systems (Bio-Rad).

    Techniques: Chromatography, Filtration, Activation Assay

    Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of each gintonin prepared from ginseng root. SDS-PAGE of edible gintonin obtained from anion exchange chromatography as shown in Fig. 1 . Coomassie Brilliant Blue staining was used to stain protein moieties of gintonin. Crude gintonin prepared from ginseng root in SDS-PAGE showed that apparent molecular weight of gintonin was about 13 kDa.

    Journal: Journal of Ginseng Research

    Article Title: An Edible Gintonin Preparation from Ginseng

    doi: 10.5142/jgr.2011.35.4.471

    Figure Lengend Snippet: Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of each gintonin prepared from ginseng root. SDS-PAGE of edible gintonin obtained from anion exchange chromatography as shown in Fig. 1 . Coomassie Brilliant Blue staining was used to stain protein moieties of gintonin. Crude gintonin prepared from ginseng root in SDS-PAGE showed that apparent molecular weight of gintonin was about 13 kDa.

    Article Snippet: Gel filtration chromatography Gel filtration chromatography of the gintonin fraction obtained from ginseng root was carried out by a Superdex 75 column (10×300 mm) equilibrated with PBS on BioLogic DuoFlow chromatography systems (Bio-Rad).

    Techniques: Polyacrylamide Gel Electrophoresis, SDS Page, Chromatography, Staining, Molecular Weight

    The majority of cytosolic Ku70 is found in high molecule weight complexes. a Cytosolic SH-SY5Y cell extracts were analyzed by Superdex 600 HR 10/30 gel filtration chromatography. Twenty microliter of each fraction (0.5 ml) was separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and the blot was probed with Ku70, Bax, or Ku80 antibodies. b Cytosolic extracts were cross-linked using DC4 (0, 0.1, 0.2, 0.4, 0.8, 1.6 mM) as shown. Cross-linked proteins were separated by 10 % SDS-PAGE, and the blot was probed with Ku70, Ku80, or Bax antibodies

    Journal: Tumour Biology

    Article Title: Cytosolic Ku70 regulates Bax-mediated cell death

    doi: 10.1007/s13277-016-5202-z

    Figure Lengend Snippet: The majority of cytosolic Ku70 is found in high molecule weight complexes. a Cytosolic SH-SY5Y cell extracts were analyzed by Superdex 600 HR 10/30 gel filtration chromatography. Twenty microliter of each fraction (0.5 ml) was separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and the blot was probed with Ku70, Bax, or Ku80 antibodies. b Cytosolic extracts were cross-linked using DC4 (0, 0.1, 0.2, 0.4, 0.8, 1.6 mM) as shown. Cross-linked proteins were separated by 10 % SDS-PAGE, and the blot was probed with Ku70, Ku80, or Bax antibodies

    Article Snippet: Gel filtration Gel filtration chromatography was carried out using a Bio-Rad Biologic DueFlow system with a Superdex 200 HR 10/30 column at a flow rate of 0.5 ml per min. One milligram of cytosolic extracts was injected into the column.

    Techniques: Filtration, Chromatography, Polyacrylamide Gel Electrophoresis, SDS Page

    Ku70-depletion sensitive or insensitive cells have similar levels of Ku70, Ku80, or Bax, but they differ in their response to HDACI-induced cell death. a Cytosolic extracts or whole cell extracts of SH-SY5Y, SHEP-1, ES2, A2780, and HEK-293T cells were separated by SDA-PAGE and blotted with Ku70, Ku80, or Bax antibodies. β-Tubulin was used as a loading control. b Cytosolic HEK-293T or A2780 cell extracts were analyzed by Superdex 600 HR 10/30 gel filtration chromatography. Twenty microliters of each fraction (0.5 ml) were separated by SDA-PAGE, and the blot was probed with Ku70 or Bax antibodies. c Cells were plated into 96-well plates. One day later, they were treated with various concentrations of suberoylanilide hydroxamic acid (SAHA) as shown. There were at least three wells per concentration. Forty-eight hours following SAHA treatment, cell viability was determined by MTT assay. The results of the MTT assay were expressed as percent of DMSO-treated control (mean ± SD)

    Journal: Tumour Biology

    Article Title: Cytosolic Ku70 regulates Bax-mediated cell death

    doi: 10.1007/s13277-016-5202-z

    Figure Lengend Snippet: Ku70-depletion sensitive or insensitive cells have similar levels of Ku70, Ku80, or Bax, but they differ in their response to HDACI-induced cell death. a Cytosolic extracts or whole cell extracts of SH-SY5Y, SHEP-1, ES2, A2780, and HEK-293T cells were separated by SDA-PAGE and blotted with Ku70, Ku80, or Bax antibodies. β-Tubulin was used as a loading control. b Cytosolic HEK-293T or A2780 cell extracts were analyzed by Superdex 600 HR 10/30 gel filtration chromatography. Twenty microliters of each fraction (0.5 ml) were separated by SDA-PAGE, and the blot was probed with Ku70 or Bax antibodies. c Cells were plated into 96-well plates. One day later, they were treated with various concentrations of suberoylanilide hydroxamic acid (SAHA) as shown. There were at least three wells per concentration. Forty-eight hours following SAHA treatment, cell viability was determined by MTT assay. The results of the MTT assay were expressed as percent of DMSO-treated control (mean ± SD)

    Article Snippet: Gel filtration Gel filtration chromatography was carried out using a Bio-Rad Biologic DueFlow system with a Superdex 200 HR 10/30 column at a flow rate of 0.5 ml per min. One milligram of cytosolic extracts was injected into the column.

    Techniques: Polyacrylamide Gel Electrophoresis, Filtration, Chromatography, Concentration Assay, MTT Assay

    Size exclusion chromatography and SDS-PAGE analyses on AbHemL, HemA-HemL complex and AbHemA. Elution profiles of Ab HemL (A) , fractions from Ab HemA-HemL complex corresponding to lane 2 of Figure 2B and lane 3 from Figure 2C and Ab HemA (D) . Rigth panels are the SDS-PAGE of the same samples analyzed on SEC (S) and fractions from SEC at 8, 14, and 15 ml elution volume. In right panel (B) , the black line indicates that the image was assembled from two different gels. White lines on right panels (C,D) separate different parts of the same gel that were combined, excluding lanes which were not of interest. Original gels from which panels were assembled are shown in the Supplementary Materials .

    Journal: Frontiers in Molecular Biosciences

    Article Title: Isolation of a Complex Formed Between Acinetobacter baumannii HemA and HemL, Key Enzymes of Tetrapyrroles Biosynthesis

    doi: 10.3389/fmolb.2019.00006

    Figure Lengend Snippet: Size exclusion chromatography and SDS-PAGE analyses on AbHemL, HemA-HemL complex and AbHemA. Elution profiles of Ab HemL (A) , fractions from Ab HemA-HemL complex corresponding to lane 2 of Figure 2B and lane 3 from Figure 2C and Ab HemA (D) . Rigth panels are the SDS-PAGE of the same samples analyzed on SEC (S) and fractions from SEC at 8, 14, and 15 ml elution volume. In right panel (B) , the black line indicates that the image was assembled from two different gels. White lines on right panels (C,D) separate different parts of the same gel that were combined, excluding lanes which were not of interest. Original gels from which panels were assembled are shown in the Supplementary Materials .

    Article Snippet: Size Exclusion Chromatography Gel filtration of Ab HemA/L was performed on a Superdex 200 10/300 GL column (GE Healthcare, Little Chalfont, UK) at room temperature and at a flow rate of 0.5 mL/min in 50 mM Na phosphate buffer pH 8.0, containing 100 mM NaCl.

    Techniques: Size-exclusion Chromatography, SDS Page

    Effects of citrate on the AbHemA-HemL complex. (A) Native gel on Ab HemA (A), Ab HemL (L) and a mixture of same amounts (0.7 μg/μL) of Ab HemA and Ab HemL (A+L) in the presence of HemA ligands: 0.1 mM NADP + , 10 mM glutamate benzyl-ester (BENZYL-Glu), 10 mM glutamate methyl-ester (METHYL-Glu), 10 mM sodium citrate and 0.1 mM tRNA. The black line indicates that the image was assembled from two different gels. The original gels from which the panel was assembled are shown in the Supplementary Materials . (B) Size exclusion chromatography of Ab HemA-HemL complex in the presence (red line) or absence (black line) of 0.1 M sodium citrate. (C) SDS-PAGE analysis of fractions from SEC (sample 1 and 2) at 8 ml elution volume. (D) Affinity chromatography elution profiles obtained in different purification procedures of co-expressed Ab HemA and Ab HemL, carried out in the absence (black line) or the presence (red line) of 0.1 M sodium citrate. (E) Size exclusion chromatography of the Ab HemA-HemL sample purified in the presence of 0.1 M sodium citrate.

    Journal: Frontiers in Molecular Biosciences

    Article Title: Isolation of a Complex Formed Between Acinetobacter baumannii HemA and HemL, Key Enzymes of Tetrapyrroles Biosynthesis

    doi: 10.3389/fmolb.2019.00006

    Figure Lengend Snippet: Effects of citrate on the AbHemA-HemL complex. (A) Native gel on Ab HemA (A), Ab HemL (L) and a mixture of same amounts (0.7 μg/μL) of Ab HemA and Ab HemL (A+L) in the presence of HemA ligands: 0.1 mM NADP + , 10 mM glutamate benzyl-ester (BENZYL-Glu), 10 mM glutamate methyl-ester (METHYL-Glu), 10 mM sodium citrate and 0.1 mM tRNA. The black line indicates that the image was assembled from two different gels. The original gels from which the panel was assembled are shown in the Supplementary Materials . (B) Size exclusion chromatography of Ab HemA-HemL complex in the presence (red line) or absence (black line) of 0.1 M sodium citrate. (C) SDS-PAGE analysis of fractions from SEC (sample 1 and 2) at 8 ml elution volume. (D) Affinity chromatography elution profiles obtained in different purification procedures of co-expressed Ab HemA and Ab HemL, carried out in the absence (black line) or the presence (red line) of 0.1 M sodium citrate. (E) Size exclusion chromatography of the Ab HemA-HemL sample purified in the presence of 0.1 M sodium citrate.

    Article Snippet: Size Exclusion Chromatography Gel filtration of Ab HemA/L was performed on a Superdex 200 10/300 GL column (GE Healthcare, Little Chalfont, UK) at room temperature and at a flow rate of 0.5 mL/min in 50 mM Na phosphate buffer pH 8.0, containing 100 mM NaCl.

    Techniques: Size-exclusion Chromatography, SDS Page, Affinity Chromatography, Purification

    Fractionation of IMAC-purified recombinant Pr78 Gag protein by size exclusion chromatography. ( a ) Absorbance versus elution time chromatogram plotted from the data obtained from a Superdex 200 column showing peak fractions with maximum absorbance containing purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1. ( b ) Coomassie Brilliant Blue-stained SDS-polyacrylamide gel showing the resolution of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1 in fractions 18–26. ( c ) Western blot analysis of pooled peak fractions (22–24) of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein analyzed with anti-Pr78 Gag polyserum, and ( d ) anti-6x-His monoclonal antibody, respectively.

    Journal: Scientific Reports

    Article Title: Expression, purification, and characterization of biologically active full-length Mason-Pfizer monkey virus (MPMV) Pr78Gag

    doi: 10.1038/s41598-018-30142-0

    Figure Lengend Snippet: Fractionation of IMAC-purified recombinant Pr78 Gag protein by size exclusion chromatography. ( a ) Absorbance versus elution time chromatogram plotted from the data obtained from a Superdex 200 column showing peak fractions with maximum absorbance containing purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1. ( b ) Coomassie Brilliant Blue-stained SDS-polyacrylamide gel showing the resolution of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein expressed from FN1 in fractions 18–26. ( c ) Western blot analysis of pooled peak fractions (22–24) of purified recombinant full-length MPMV Pr78 Gag -His 6 -tag fusion protein analyzed with anti-Pr78 Gag polyserum, and ( d ) anti-6x-His monoclonal antibody, respectively.

    Article Snippet: Following HisTRAPTM column elution, Pr78Gag -His6 -tag protein was concentrated using Amicon® Ultra 15 (30,000 molecular weight cut-off membrane) and was further fractionated by gel filtration/size exclusion chromatography using a Superdex 200 10/300 GL column (GE Healthcare) previously equilibrated with 50 mM Tris-HCl (pH 8.0) and 1.0 M NaCl.

    Techniques: Fractionation, Purification, Recombinant, Size-exclusion Chromatography, Staining, Western Blot

    Laboratory-Scale Purification of AAV9-dsEGFP by Quaternary Ammonium Anion-Exchange Column and Size-Exclusion Chromatography (A) The AAV9-dsEGFP preparations were analyzed by 5%–20% (v/v) gradient gel SDS-PAGE and stained with Oriole fluorescent gel stain before and after chromatography purification using a HiPrep Q XL 16/10 column. The white arrowhead indicates a 200-kDa impurity. Lane 1, pre-TFF; lane 2, post-TFF; lane 3, after heat treatment; lane 4, 1/3→1/2 AS; lane 5, diluted 1/3→1/2 AS; lane 6, pass-through fraction; lane 7, wash-out fraction; lane 8, column-bound and eluted fraction. (B) The pass-through fraction was subsequently subjected to size-exclusion chromatography using a HiLoad 16/60 Superdex 200 preparation-grade column using an ÄKTA Explorer 100 HPLC system equipped with a 10-mL sample loop, with MHN buffer (pH 6.5) containing 300 mM NaCl and 0.01% (w/v) Pluronic F-68 as the mobile phase. y axis, 280 nm absorbance; x axis, fraction number. The black arrowhead indicates the peak fractions of the rAAV9 (corresponding to lanes 2–14 in C). (C) The elution fraction was analyzed by two 5%–20% (v/v) gradient SDS-PAGE gels with Oriole fluorescent staining; the left gel is from lanes 1–12, and the right gel is from lanes 13–23. Lanes 1–18, fractions 14–31; lane 19, fraction 33; lane 20, fraction 35; lane 21, fraction 37; lane 22, fraction 39; lane 23, fraction 41. Peak fractions (fractions 15–27) were collected to obtain the final product. (D–G) The final AAV9-dsEGFP product was analyzed by 5%–20% (v/v) gradient gel SDS-PAGE with Oriole fluorescent staining (D), western blotting (E, anti-AAV capsid monoclonal antibody B1), EM (F, negative staining), and analytical ultracentrifugation (AUC, G). Shown are the peak fractions of (i) empty particles (68.6 S, 25.7%), (ii) intermediate particles (88.8 S, 32.4%), and (iii) fully packaged virions (102.6 S, 38.8%). The goodness of fit (RMSD) was 0.004635. y axis, continuous-size C(S) distribution; x axis, sedimentation coefficient. Lane 1 and lane 2, the final rAAV9 product. The three bands represent the AAV9 capsid proteins VP1 (82 kDa), VP2 (67 kDa), and VP3 (60 kDa).

    Journal: Molecular Therapy. Methods & Clinical Development

    Article Title: Highly Efficient Ultracentrifugation-free Chromatographic Purification of Recombinant AAV Serotype 9

    doi: 10.1016/j.omtm.2018.10.015

    Figure Lengend Snippet: Laboratory-Scale Purification of AAV9-dsEGFP by Quaternary Ammonium Anion-Exchange Column and Size-Exclusion Chromatography (A) The AAV9-dsEGFP preparations were analyzed by 5%–20% (v/v) gradient gel SDS-PAGE and stained with Oriole fluorescent gel stain before and after chromatography purification using a HiPrep Q XL 16/10 column. The white arrowhead indicates a 200-kDa impurity. Lane 1, pre-TFF; lane 2, post-TFF; lane 3, after heat treatment; lane 4, 1/3→1/2 AS; lane 5, diluted 1/3→1/2 AS; lane 6, pass-through fraction; lane 7, wash-out fraction; lane 8, column-bound and eluted fraction. (B) The pass-through fraction was subsequently subjected to size-exclusion chromatography using a HiLoad 16/60 Superdex 200 preparation-grade column using an ÄKTA Explorer 100 HPLC system equipped with a 10-mL sample loop, with MHN buffer (pH 6.5) containing 300 mM NaCl and 0.01% (w/v) Pluronic F-68 as the mobile phase. y axis, 280 nm absorbance; x axis, fraction number. The black arrowhead indicates the peak fractions of the rAAV9 (corresponding to lanes 2–14 in C). (C) The elution fraction was analyzed by two 5%–20% (v/v) gradient SDS-PAGE gels with Oriole fluorescent staining; the left gel is from lanes 1–12, and the right gel is from lanes 13–23. Lanes 1–18, fractions 14–31; lane 19, fraction 33; lane 20, fraction 35; lane 21, fraction 37; lane 22, fraction 39; lane 23, fraction 41. Peak fractions (fractions 15–27) were collected to obtain the final product. (D–G) The final AAV9-dsEGFP product was analyzed by 5%–20% (v/v) gradient gel SDS-PAGE with Oriole fluorescent staining (D), western blotting (E, anti-AAV capsid monoclonal antibody B1), EM (F, negative staining), and analytical ultracentrifugation (AUC, G). Shown are the peak fractions of (i) empty particles (68.6 S, 25.7%), (ii) intermediate particles (88.8 S, 32.4%), and (iii) fully packaged virions (102.6 S, 38.8%). The goodness of fit (RMSD) was 0.004635. y axis, continuous-size C(S) distribution; x axis, sedimentation coefficient. Lane 1 and lane 2, the final rAAV9 product. The three bands represent the AAV9 capsid proteins VP1 (82 kDa), VP2 (67 kDa), and VP3 (60 kDa).

    Article Snippet: The pass-through fraction was purified by size-exclusion (gel filtration) chromatography using a HiLoad 16/60 Superdex 200 preparation-grade column (GE Healthcare) and an ÄKTA Explorer 100 HPLC system (GE Healthcare) equipped with a 10-mL sample loop running the MHN buffer (pH 6.5) containing 300 mM NaCl and 0.01% (w/v) Pluronic F-68.

    Techniques: Purification, Size-exclusion Chromatography, SDS Page, Staining, Chromatography, High Performance Liquid Chromatography, Western Blot, Negative Staining, Sedimentation

    Purification and molecular weight analysis of free recombinant Usp. ( A ) Purity analysis of purified free recombinant Usp. Free Usp was purified from E . coli BL21(DE3) over-expressing Usp and OrfU1-His as described under Methods. Lane 1, marker; lane 2, total cell proteins extracted from E . coli BL21(DE3) cells over-expressing Usp and OrfU1-His and lane 3, free Usp eluted with 6 M guanidine HCl. ( B ) Elution profile of purified free recombinant Usp from gel filtration column. Free Usp which was dialyzed against 50 mM sodium phosphate buffer was separated by gel filtration column. Opened triangles indicate elution positions of molecular weight markers. Calculated molecular weight was indicated on each peak.

    Journal: Gut Pathogens

    Article Title: Uropathogenic specific protein gene, highly distributed in extraintestinal uropathogenic Escherichia coli, encodes a new member of H-N-H nuclease superfamily

    doi: 10.1186/1757-4749-5-13

    Figure Lengend Snippet: Purification and molecular weight analysis of free recombinant Usp. ( A ) Purity analysis of purified free recombinant Usp. Free Usp was purified from E . coli BL21(DE3) over-expressing Usp and OrfU1-His as described under Methods. Lane 1, marker; lane 2, total cell proteins extracted from E . coli BL21(DE3) cells over-expressing Usp and OrfU1-His and lane 3, free Usp eluted with 6 M guanidine HCl. ( B ) Elution profile of purified free recombinant Usp from gel filtration column. Free Usp which was dialyzed against 50 mM sodium phosphate buffer was separated by gel filtration column. Opened triangles indicate elution positions of molecular weight markers. Calculated molecular weight was indicated on each peak.

    Article Snippet: Analytical gel filtration Gel filtration chromatography was used to determine the molecular weight of free Usp. The purified free Usp and 5 standard proteins from Gel Filtration LMW Calibration Kit (GE Healthcare Life Sciences) were dialyzed against sodium phosphate buffer (0.05 M NaH2 PO4 , 0.05 M Na2 HPO4 , 0.2 M NaCl pH 8.0), and separated on the Superdex 75 10/300 GL Column (GE Healthcare Life Sciences) equilibrated with the same buffer.

    Techniques: Purification, Molecular Weight, Recombinant, Expressing, Marker, Filtration

    ANX1 and ANX2 share a common ectodomain architecture. ( a ) Ribbon diagrams of ANX1 (left) and ANX2 (right) show a strong degree of structural conservation (r.m.s.d. of ∼0.6 Å comparing 375 corresponding C α atoms between ANX1 and ANX2) with a similar orientation of their mal-N and mal-C domains (colours are as in Fig. 1 ▸ ). The N-glycan structures observed in ANX1 and ANX2 are highlighted in yellow (in bond representation). ( b ) Structural superposition of the ANX1 (C α trace, magenta) and ANX2 (blue) ectodomains (right) and a ribbon diagram of the ANX1 ectodomain with C α atoms coloured according to their crystallographic temperature factors, from blue to red (left). Note that the N- and C-termini as well as several loop structures assembled around the ‘cleft’ region appear to be flexible. ( c ) The corresponding the1-1 and the1-2 alleles (shown as orange spheres) are mapped into the ANX1 structure. ( d ) Analytical size-exclusion chromatography reveals that the ANX1 extracellular domain elutes as a monomer (red line), as do the isolated THE1 (black line), HERK1 (blue line) and ANX2 (green line) ectodomains. The void volume ( V 0 ) and total volume ( V t ) are shown, together with elution volumes for molecular-mass standards ( A , thyroglobulin, 669 000 Da; B , ferritin, 440 000 Da; C , aldolase, 158 000 Da; D , conalbumin, 75 000 Da; E , ovalbumin, 44 000 Da; F , carbonic anhydrase, 29 000 Da; G , ribonuclease A, 13 700 Da.). The molecular masses of purified ANX1, THE1 and HERK1 ectodomains analysed by MS-MALDI-TOF are 58, 63 and 53.5 kDa, respectively. An SDS–PAGE analysis of the purified ectodomains is shown alongside.

    Journal: Acta Crystallographica. Section D, Structural Biology

    Article Title: Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction

    doi: 10.1107/S205979831800774X

    Figure Lengend Snippet: ANX1 and ANX2 share a common ectodomain architecture. ( a ) Ribbon diagrams of ANX1 (left) and ANX2 (right) show a strong degree of structural conservation (r.m.s.d. of ∼0.6 Å comparing 375 corresponding C α atoms between ANX1 and ANX2) with a similar orientation of their mal-N and mal-C domains (colours are as in Fig. 1 ▸ ). The N-glycan structures observed in ANX1 and ANX2 are highlighted in yellow (in bond representation). ( b ) Structural superposition of the ANX1 (C α trace, magenta) and ANX2 (blue) ectodomains (right) and a ribbon diagram of the ANX1 ectodomain with C α atoms coloured according to their crystallographic temperature factors, from blue to red (left). Note that the N- and C-termini as well as several loop structures assembled around the ‘cleft’ region appear to be flexible. ( c ) The corresponding the1-1 and the1-2 alleles (shown as orange spheres) are mapped into the ANX1 structure. ( d ) Analytical size-exclusion chromatography reveals that the ANX1 extracellular domain elutes as a monomer (red line), as do the isolated THE1 (black line), HERK1 (blue line) and ANX2 (green line) ectodomains. The void volume ( V 0 ) and total volume ( V t ) are shown, together with elution volumes for molecular-mass standards ( A , thyroglobulin, 669 000 Da; B , ferritin, 440 000 Da; C , aldolase, 158 000 Da; D , conalbumin, 75 000 Da; E , ovalbumin, 44 000 Da; F , carbonic anhydrase, 29 000 Da; G , ribonuclease A, 13 700 Da.). The molecular masses of purified ANX1, THE1 and HERK1 ectodomains analysed by MS-MALDI-TOF are 58, 63 and 53.5 kDa, respectively. An SDS–PAGE analysis of the purified ectodomains is shown alongside.

    Article Snippet: Size-exclusion chromatography Analytical gel-filtration experiments were performed using a Superdex 200 Increase 10/300 GL column (GE Healthcare) pre-equilibrated in 20 mM citric acid pH 5.0, 100 mM NaCl.

    Techniques: Size-exclusion Chromatography, Isolation, Purification, Mass Spectrometry, SDS Page

    Gel filtration chromatography of the NgoL-CTD wild type and NgoL–CTD-L480E-L487E. The wild-type and mutant protein were both subjected to gel filtration chromatography to determine their oligomeric status. Elution profile of (A) NgoL-CTD wild type and (B) NgoL-CTD-L480E-L487E (C) SDS-PAGE analysis of fractions for (B): Fraction no.'s 3, 6 and 9-11 correspond to peak no.'s I (Rv = 8.0 ml), II (Rv = 13.1 ml) and III (Rv = 17.8 ml), respectively. Peak III was reinjected and the corresponding chromatography and gel analysis profiles are shown as inset figure in (B). (D) The standard curve log molecular weight versus Ve / Vo was derived from the elution profiles of the standard molecular weight markers with Ve corresponding to the peak elution volume of the protein and Vo representing the void volume of the column determined using Blue dextran. The peak positions of wild type NgoL-CTD and NgoL-CTD-L480E-L487E are indicated by dotted and solid lines, respectively.

    Journal: PLoS ONE

    Article Title: The C-Terminal Domain of the MutL Homolog from Neisseria gonorrhoeae Forms an Inverted Homodimer

    doi: 10.1371/journal.pone.0013726

    Figure Lengend Snippet: Gel filtration chromatography of the NgoL-CTD wild type and NgoL–CTD-L480E-L487E. The wild-type and mutant protein were both subjected to gel filtration chromatography to determine their oligomeric status. Elution profile of (A) NgoL-CTD wild type and (B) NgoL-CTD-L480E-L487E (C) SDS-PAGE analysis of fractions for (B): Fraction no.'s 3, 6 and 9-11 correspond to peak no.'s I (Rv = 8.0 ml), II (Rv = 13.1 ml) and III (Rv = 17.8 ml), respectively. Peak III was reinjected and the corresponding chromatography and gel analysis profiles are shown as inset figure in (B). (D) The standard curve log molecular weight versus Ve / Vo was derived from the elution profiles of the standard molecular weight markers with Ve corresponding to the peak elution volume of the protein and Vo representing the void volume of the column determined using Blue dextran. The peak positions of wild type NgoL-CTD and NgoL-CTD-L480E-L487E are indicated by dotted and solid lines, respectively.

    Article Snippet: Molecular size-exclusion chromatography Gel-filtration experiments were performed using a Superose 6 HR 10/30 column (GE Healthcare).

    Techniques: Filtration, Chromatography, Mutagenesis, SDS Page, Molecular Weight, Derivative Assay