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  • 85
    Bio-Rad bio silect 250
    SGF-2 is a 1.1-MDa heteromeric complex. A , chromatography chart of SGF-2 activity passed through a Bio-Silect 250 gel filtration column.  B , EMSA was performed using the E site probe, and each fraction passed through a Bio-Silect 250 column.  Source Q fr
    Bio Silect 250, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Bio-Rad bio silect column
    SGF-2 is a 1.1-MDa heteromeric complex. A , chromatography chart of SGF-2 activity passed through a Bio-Silect 250 gel filtration column.  B , EMSA was performed using the E site probe, and each fraction passed through a Bio-Silect 250 column.  Source Q fr
    Bio Silect Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bio silect column/product/Bio-Rad
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    88
    Bio-Rad bio silect
    SGF-2 is a 1.1-MDa heteromeric complex. A , chromatography chart of SGF-2 activity passed through a Bio-Silect 250 gel filtration column.  B , EMSA was performed using the E site probe, and each fraction passed through a Bio-Silect 250 column.  Source Q fr
    Bio Silect, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 88/100, based on 117 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bio silect/product/Bio-Rad
    Average 88 stars, based on 117 article reviews
    Price from $9.99 to $1999.99
    bio silect - by Bioz Stars, 2020-08
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    85
    Bio-Rad bio silect sec250 column
    SGF-2 is a 1.1-MDa heteromeric complex. A , chromatography chart of SGF-2 activity passed through a Bio-Silect 250 gel filtration column.  B , EMSA was performed using the E site probe, and each fraction passed through a Bio-Silect 250 column.  Source Q fr
    Bio Silect Sec250 Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bio silect sec250 column/product/Bio-Rad
    Average 85 stars, based on 5 article reviews
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    bio silect sec250 column - by Bioz Stars, 2020-08
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    80
    Bio-Rad bio silect chromatography column
    Purification of the active component from pig brain cytosol. ( A ) Cibachrome blue 3GA: a step-eluted fraction from fast-flow <t>Q-Sepharose,</t> diluted to 50 mM salt, was passed over a 40 ml Cibachrome blue 3GA column, washed extensively, and eluted as shown in a continuous 25-300 μS salt gradient. Protein was monitored in line by absorbence at 280 nm, and salt concentration by conductivity, as shown. The activities of column fractions were assayed and plotted ( far left ordinate axis ) and the two activity peaks were pooled. ( B ) Phenyl–Sepharose: pooled fractions from A were applied to a 15-ml phenyl–Sepharose column and proteins eluted with a 300–25 μS salt gradient. ( C ) Q-Sepharose: pooled active fractions from B were diluted to 20 mM salt and chromatographed on a 5-ml Q-Sepharose column. Activity was eluted in a salt gradient to 200 μS. ( D ) 200 μl of the peak fraction from C was applied to a <t>Bio-Silect</t> gel filtration column with a rated separation range of 100–5 kD. The elution positions of molecular weight standards are indicated.
    Bio Silect Chromatography Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 80/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Bio-Rad bio silect 400 guard column
    Purification of the active component from pig brain cytosol. ( A ) Cibachrome blue 3GA: a step-eluted fraction from fast-flow <t>Q-Sepharose,</t> diluted to 50 mM salt, was passed over a 40 ml Cibachrome blue 3GA column, washed extensively, and eluted as shown in a continuous 25-300 μS salt gradient. Protein was monitored in line by absorbence at 280 nm, and salt concentration by conductivity, as shown. The activities of column fractions were assayed and plotted ( far left ordinate axis ) and the two activity peaks were pooled. ( B ) Phenyl–Sepharose: pooled fractions from A were applied to a 15-ml phenyl–Sepharose column and proteins eluted with a 300–25 μS salt gradient. ( C ) Q-Sepharose: pooled active fractions from B were diluted to 20 mM salt and chromatographed on a 5-ml Q-Sepharose column. Activity was eluted in a salt gradient to 200 μS. ( D ) 200 μl of the peak fraction from C was applied to a <t>Bio-Silect</t> gel filtration column with a rated separation range of 100–5 kD. The elution positions of molecular weight standards are indicated.
    Bio Silect 400 Guard Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 80/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bio silect 400 guard column/product/Bio-Rad
    Average 80 stars, based on 4 article reviews
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    85
    Bio-Rad bio silect 250 gel filtration column
    Purification of the active component from pig brain cytosol. ( A ) Cibachrome blue 3GA: a step-eluted fraction from fast-flow <t>Q-Sepharose,</t> diluted to 50 mM salt, was passed over a 40 ml Cibachrome blue 3GA column, washed extensively, and eluted as shown in a continuous 25-300 μS salt gradient. Protein was monitored in line by absorbence at 280 nm, and salt concentration by conductivity, as shown. The activities of column fractions were assayed and plotted ( far left ordinate axis ) and the two activity peaks were pooled. ( B ) Phenyl–Sepharose: pooled fractions from A were applied to a 15-ml phenyl–Sepharose column and proteins eluted with a 300–25 μS salt gradient. ( C ) Q-Sepharose: pooled active fractions from B were diluted to 20 mM salt and chromatographed on a 5-ml Q-Sepharose column. Activity was eluted in a salt gradient to 200 μS. ( D ) 200 μl of the peak fraction from C was applied to a <t>Bio-Silect</t> gel filtration column with a rated separation range of 100–5 kD. The elution positions of molecular weight standards are indicated.
    Bio Silect 250 Gel Filtration Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bio silect 250 gel filtration column/product/Bio-Rad
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    85
    Bio-Rad bio silect sec 250 5 column
    Purification of the active component from pig brain cytosol. ( A ) Cibachrome blue 3GA: a step-eluted fraction from fast-flow <t>Q-Sepharose,</t> diluted to 50 mM salt, was passed over a 40 ml Cibachrome blue 3GA column, washed extensively, and eluted as shown in a continuous 25-300 μS salt gradient. Protein was monitored in line by absorbence at 280 nm, and salt concentration by conductivity, as shown. The activities of column fractions were assayed and plotted ( far left ordinate axis ) and the two activity peaks were pooled. ( B ) Phenyl–Sepharose: pooled fractions from A were applied to a 15-ml phenyl–Sepharose column and proteins eluted with a 300–25 μS salt gradient. ( C ) Q-Sepharose: pooled active fractions from B were diluted to 20 mM salt and chromatographed on a 5-ml Q-Sepharose column. Activity was eluted in a salt gradient to 200 μS. ( D ) 200 μl of the peak fraction from C was applied to a <t>Bio-Silect</t> gel filtration column with a rated separation range of 100–5 kD. The elution positions of molecular weight standards are indicated.
    Bio Silect Sec 250 5 Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bio silect sec 250 5 column/product/Bio-Rad
    Average 85 stars, based on 11 article reviews
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    85
    Bio-Rad biosilect sec400
    Purification of the active component from pig brain cytosol. ( A ) Cibachrome blue 3GA: a step-eluted fraction from fast-flow <t>Q-Sepharose,</t> diluted to 50 mM salt, was passed over a 40 ml Cibachrome blue 3GA column, washed extensively, and eluted as shown in a continuous 25-300 μS salt gradient. Protein was monitored in line by absorbence at 280 nm, and salt concentration by conductivity, as shown. The activities of column fractions were assayed and plotted ( far left ordinate axis ) and the two activity peaks were pooled. ( B ) Phenyl–Sepharose: pooled fractions from A were applied to a 15-ml phenyl–Sepharose column and proteins eluted with a 300–25 μS salt gradient. ( C ) Q-Sepharose: pooled active fractions from B were diluted to 20 mM salt and chromatographed on a 5-ml Q-Sepharose column. Activity was eluted in a salt gradient to 200 μS. ( D ) 200 μl of the peak fraction from C was applied to a <t>Bio-Silect</t> gel filtration column with a rated separation range of 100–5 kD. The elution positions of molecular weight standards are indicated.
    Biosilect Sec400, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biosilect sec400/product/Bio-Rad
    Average 85 stars, based on 1 article reviews
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    85
    Bio-Rad biosilect 400 s column
    Purification of the active component from pig brain cytosol. ( A ) Cibachrome blue 3GA: a step-eluted fraction from fast-flow <t>Q-Sepharose,</t> diluted to 50 mM salt, was passed over a 40 ml Cibachrome blue 3GA column, washed extensively, and eluted as shown in a continuous 25-300 μS salt gradient. Protein was monitored in line by absorbence at 280 nm, and salt concentration by conductivity, as shown. The activities of column fractions were assayed and plotted ( far left ordinate axis ) and the two activity peaks were pooled. ( B ) Phenyl–Sepharose: pooled fractions from A were applied to a 15-ml phenyl–Sepharose column and proteins eluted with a 300–25 μS salt gradient. ( C ) Q-Sepharose: pooled active fractions from B were diluted to 20 mM salt and chromatographed on a 5-ml Q-Sepharose column. Activity was eluted in a salt gradient to 200 μS. ( D ) 200 μl of the peak fraction from C was applied to a <t>Bio-Silect</t> gel filtration column with a rated separation range of 100–5 kD. The elution positions of molecular weight standards are indicated.
    Biosilect 400 S Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Bio-Rad biosilect 125 5 column
    Purification of the active component from pig brain cytosol. ( A ) Cibachrome blue 3GA: a step-eluted fraction from fast-flow <t>Q-Sepharose,</t> diluted to 50 mM salt, was passed over a 40 ml Cibachrome blue 3GA column, washed extensively, and eluted as shown in a continuous 25-300 μS salt gradient. Protein was monitored in line by absorbence at 280 nm, and salt concentration by conductivity, as shown. The activities of column fractions were assayed and plotted ( far left ordinate axis ) and the two activity peaks were pooled. ( B ) Phenyl–Sepharose: pooled fractions from A were applied to a 15-ml phenyl–Sepharose column and proteins eluted with a 300–25 μS salt gradient. ( C ) Q-Sepharose: pooled active fractions from B were diluted to 20 mM salt and chromatographed on a 5-ml Q-Sepharose column. Activity was eluted in a salt gradient to 200 μS. ( D ) 200 μl of the peak fraction from C was applied to a <t>Bio-Silect</t> gel filtration column with a rated separation range of 100–5 kD. The elution positions of molecular weight standards are indicated.
    Biosilect 125 5 Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biosilect 125 5 column/product/Bio-Rad
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    85
    Bio-Rad biosilect sec400 gel filtration column
    Gel filtration of KI extract by <t>BioSilect</t> <t>SEC400</t> column. (A) KI extract from KCl-treated axonemes was loaded on a gel filtration column (300 × 7.8 mm) and separated at a flow rate of 1.0 ml/min. Fractions (200 μl) were collected. The numbers above the chromatogram indicate the fraction number. Arrows show the elution positions of molecular mass markers as follows: thyroglobulin (670 kDa), immunoglobulin G (150 kDa), ovalbumin (44 kDa), and myoglobin (17 kDa). (B) Proteins in the fraction 4–25 were separated by 10% SDS-PAGE and immunoblotted by anti-LRR37 and anti-RSP3 antibodies. Both proteins were coeluted at around the position with molecular mass of 1300 kDa.
    Biosilect Sec400 Gel Filtration Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biosilect sec400 gel filtration column/product/Bio-Rad
    Average 85 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
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    Image Search Results


    SGF-2 is a 1.1-MDa heteromeric complex. A , chromatography chart of SGF-2 activity passed through a Bio-Silect 250 gel filtration column.  B , EMSA was performed using the E site probe, and each fraction passed through a Bio-Silect 250 column.  Source Q fr

    Journal: The Journal of Biological Chemistry

    Article Title: Silk Gland Factor-2, Involved in Fibroin Gene Transcription, Consists of LIM Homeodomain, LIM-interacting, and Single-stranded DNA-binding Proteins *

    doi: 10.1074/jbc.M113.514471

    Figure Lengend Snippet: SGF-2 is a 1.1-MDa heteromeric complex. A , chromatography chart of SGF-2 activity passed through a Bio-Silect 250 gel filtration column. B , EMSA was performed using the E site probe, and each fraction passed through a Bio-Silect 250 column. Source Q fr

    Article Snippet: The total eluate (0.15 mg, 2.1 ml) was dialyzed against TEMGTK100 and loaded onto a column of Bio-Silect 250 (Bio-Rad) equilibrated with TEMGTK100 .

    Techniques: Multiple Displacement Amplification, Chromatography, Activity Assay, Filtration

    Purification of the active component from pig brain cytosol. ( A ) Cibachrome blue 3GA: a step-eluted fraction from fast-flow Q-Sepharose, diluted to 50 mM salt, was passed over a 40 ml Cibachrome blue 3GA column, washed extensively, and eluted as shown in a continuous 25-300 μS salt gradient. Protein was monitored in line by absorbence at 280 nm, and salt concentration by conductivity, as shown. The activities of column fractions were assayed and plotted ( far left ordinate axis ) and the two activity peaks were pooled. ( B ) Phenyl–Sepharose: pooled fractions from A were applied to a 15-ml phenyl–Sepharose column and proteins eluted with a 300–25 μS salt gradient. ( C ) Q-Sepharose: pooled active fractions from B were diluted to 20 mM salt and chromatographed on a 5-ml Q-Sepharose column. Activity was eluted in a salt gradient to 200 μS. ( D ) 200 μl of the peak fraction from C was applied to a Bio-Silect gel filtration column with a rated separation range of 100–5 kD. The elution positions of molecular weight standards are indicated.

    Journal: The Journal of Cell Biology

    Article Title: Rho- and Rac-dependent Assembly of Focal Adhesion Complexes and Actin Filaments in Permeabilized Fibroblasts: An Essential Role for Ezrin/Radixin/Moesin Proteins

    doi:

    Figure Lengend Snippet: Purification of the active component from pig brain cytosol. ( A ) Cibachrome blue 3GA: a step-eluted fraction from fast-flow Q-Sepharose, diluted to 50 mM salt, was passed over a 40 ml Cibachrome blue 3GA column, washed extensively, and eluted as shown in a continuous 25-300 μS salt gradient. Protein was monitored in line by absorbence at 280 nm, and salt concentration by conductivity, as shown. The activities of column fractions were assayed and plotted ( far left ordinate axis ) and the two activity peaks were pooled. ( B ) Phenyl–Sepharose: pooled fractions from A were applied to a 15-ml phenyl–Sepharose column and proteins eluted with a 300–25 μS salt gradient. ( C ) Q-Sepharose: pooled active fractions from B were diluted to 20 mM salt and chromatographed on a 5-ml Q-Sepharose column. Activity was eluted in a salt gradient to 200 μS. ( D ) 200 μl of the peak fraction from C was applied to a Bio-Silect gel filtration column with a rated separation range of 100–5 kD. The elution positions of molecular weight standards are indicated.

    Article Snippet: For gel filtration, a 200-μl aliquot of the activity peak from the final Q-Sepharose column was applied to a 6-ml Bio-Silect chromatography column (Bio Rad Laboratories: rated fractionation range 100–5 kD) and protein was eluted in DK150, sampling 0.25-ml fractions.

    Techniques: Purification, Flow Cytometry, Concentration Assay, Activity Assay, Filtration, Molecular Weight

    Gel filtration of KI extract by BioSilect SEC400 column. (A) KI extract from KCl-treated axonemes was loaded on a gel filtration column (300 × 7.8 mm) and separated at a flow rate of 1.0 ml/min. Fractions (200 μl) were collected. The numbers above the chromatogram indicate the fraction number. Arrows show the elution positions of molecular mass markers as follows: thyroglobulin (670 kDa), immunoglobulin G (150 kDa), ovalbumin (44 kDa), and myoglobin (17 kDa). (B) Proteins in the fraction 4–25 were separated by 10% SDS-PAGE and immunoblotted by anti-LRR37 and anti-RSP3 antibodies. Both proteins were coeluted at around the position with molecular mass of 1300 kDa.

    Journal: Molecular Biology of the Cell

    Article Title: Identification of a Novel Leucine-rich Repeat Protein as a Component of Flagellar Radial Spoke in the Ascidian Ciona intestinalis

    doi: 10.1091/mbc.02-06-0089

    Figure Lengend Snippet: Gel filtration of KI extract by BioSilect SEC400 column. (A) KI extract from KCl-treated axonemes was loaded on a gel filtration column (300 × 7.8 mm) and separated at a flow rate of 1.0 ml/min. Fractions (200 μl) were collected. The numbers above the chromatogram indicate the fraction number. Arrows show the elution positions of molecular mass markers as follows: thyroglobulin (670 kDa), immunoglobulin G (150 kDa), ovalbumin (44 kDa), and myoglobin (17 kDa). (B) Proteins in the fraction 4–25 were separated by 10% SDS-PAGE and immunoblotted by anti-LRR37 and anti-RSP3 antibodies. Both proteins were coeluted at around the position with molecular mass of 1300 kDa.

    Article Snippet: The supernatant was separated on a BioSilect SEC400 gel filtration column (300 × 7.8 mm; Bio-Rad , Hercules, CA) at a flow rate of 1.0 ml/min.

    Techniques: Filtration, Flow Cytometry, SDS Page