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buffer 100 mm kcl  (Bio-Rad)


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    Bio-Rad buffer 100 mm kcl
    Buffer 100 Mm Kcl, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1714 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/buffer+100+mm+kcl/Protein+Standard+II/pmc12852091-183-50-54
    Average 96 stars, based on 1714 article reviews
    buffer 100 mm kcl - by Bioz Stars, 2026-09
    96/100 stars

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    Related Articles

    Purification:

    Article Title: Intrinsically disordered regions in the yeast transcriptional regulator Ixr1 support prion-like behavior
    Article Snippet: The molecular weight and Stokes radius of Ixr1 protein were determined by size-exclusion chromatography.The molecular weight and Stokes radius of Ixr1 protein were determined by size-exclusion chromatography.. The chromatographic separation was done on a Superdex 200 increase 3.2/300 column (GE Healthcare, United States) connected to a ÄKTA-prime purifier system (GE Healthcare, United States), pre-equilibrated with running buffer (50 mM potassium phosphate buffer pH 6.9, 100 mM KCl, 2 mM dithiothreitol and 1 mM EDTA) and calibrated using the protein standards from Bio-Rad, United States (bovine thyroglobulin bovine (670 kDa; Stokes radius: 7.8 Å); bovine γ-globulin (158 kDa; 51 Å); chicken ovalbumin (44 kDa; Stokes radius: 31.2 Å); equine myoglobin (17 kDa; Stokes radius: 19 Å); Vitamin B12 (1.35 kDa; Stokes radius: 8.5 Å).. Blue dextran (≈ 2 MDa) was used to determine the void volume (V 0 ) of the column.Blue dextran (≈ 2 MDa) was used to determine the void volume (V 0 ) of the column.

    Filtration:

    Article Title: Intrinsically disordered regions in the yeast transcriptional regulator Ixr1 support prion-like behavior
    Article Snippet: The molecular weight and Stokes radius of Ixr1 protein were determined by size-exclusion chromatography.The molecular weight and Stokes radius of Ixr1 protein were determined by size-exclusion chromatography.. The chromatographic separation was done on a Superdex 200 increase 3.2/300 column (GE Healthcare, United States) connected to a ÄKTA-prime purifier system (GE Healthcare, United States), pre-equilibrated with running buffer (50 mM potassium phosphate buffer pH 6.9, 100 mM KCl, 2 mM dithiothreitol and 1 mM EDTA) and calibrated using the protein standards from Bio-Rad, United States (bovine thyroglobulin bovine (670 kDa; Stokes radius: 7.8 Å); bovine γ-globulin (158 kDa; 51 Å); chicken ovalbumin (44 kDa; Stokes radius: 31.2 Å); equine myoglobin (17 kDa; Stokes radius: 19 Å); Vitamin B12 (1.35 kDa; Stokes radius: 8.5 Å).. Blue dextran (≈ 2 MDa) was used to determine the void volume (V 0 ) of the column.Blue dextran (≈ 2 MDa) was used to determine the void volume (V 0 ) of the column.

    Chromatography:

    Article Title: Intrinsically disordered regions in the yeast transcriptional regulator Ixr1 support prion-like behavior
    Article Snippet: The molecular weight and Stokes radius of Ixr1 protein were determined by size-exclusion chromatography.The molecular weight and Stokes radius of Ixr1 protein were determined by size-exclusion chromatography.. The chromatographic separation was done on a Superdex 200 increase 3.2/300 column (GE Healthcare, United States) connected to a ÄKTA-prime purifier system (GE Healthcare, United States), pre-equilibrated with running buffer (50 mM potassium phosphate buffer pH 6.9, 100 mM KCl, 2 mM dithiothreitol and 1 mM EDTA) and calibrated using the protein standards from Bio-Rad, United States (bovine thyroglobulin bovine (670 kDa; Stokes radius: 7.8 Å); bovine γ-globulin (158 kDa; 51 Å); chicken ovalbumin (44 kDa; Stokes radius: 31.2 Å); equine myoglobin (17 kDa; Stokes radius: 19 Å); Vitamin B12 (1.35 kDa; Stokes radius: 8.5 Å).. Blue dextran (≈ 2 MDa) was used to determine the void volume (V 0 ) of the column.Blue dextran (≈ 2 MDa) was used to determine the void volume (V 0 ) of the column.



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    Image Search Results


    a Schematic overview of affinity-based uptake of a client peptide of the 14-3-3 hub protein in a specific coacervate population. Two isoforms of His-tagged 14-3-3 are anchored in separate terpolymer-stabilized coacervates by means of their interaction with Ni-NTA-amylose in the coacervates. b Schematic overview of inter-coacervate signaling based on 14-3-3 interactions. PKA phosphorylates a phosphorylation-dependent and coacervate-anchored client protein (competitor, gray), which displaces an initially bound, but mobile, client protein (moderate binder, green) and facilitates the release of the mobile client protein into bulk solution. Subsequently, the green client protein is taken up into the receiver population of coacervates. 14-3-3, PKA, and the phosphorylation-dependent client protein are immobilized in the coacervates by means of interactions between their His-tag and Ni-NTA-amyloses.

    Journal: Communications Chemistry

    Article Title: Competitive protein recruitment in artificial cells

    doi: 10.1038/s42004-024-01229-9

    Figure Lengend Snippet: a Schematic overview of affinity-based uptake of a client peptide of the 14-3-3 hub protein in a specific coacervate population. Two isoforms of His-tagged 14-3-3 are anchored in separate terpolymer-stabilized coacervates by means of their interaction with Ni-NTA-amylose in the coacervates. b Schematic overview of inter-coacervate signaling based on 14-3-3 interactions. PKA phosphorylates a phosphorylation-dependent and coacervate-anchored client protein (competitor, gray), which displaces an initially bound, but mobile, client protein (moderate binder, green) and facilitates the release of the mobile client protein into bulk solution. Subsequently, the green client protein is taken up into the receiver population of coacervates. 14-3-3, PKA, and the phosphorylation-dependent client protein are immobilized in the coacervates by means of interactions between their His-tag and Ni-NTA-amyloses.

    Article Snippet: The combined fractions were extensively dialyzed against coacervate buffer (20 mM HEPES, 100 mM KCl, pH 7.5, freshly prepared with 100 µM tris(2-carboxyethyl)phosphine (TCEP) using membrane tubing with a molecular weight cut-off (MWCO) of 12–14 kDa (Fisher Scientific).

    Techniques:

    a Schematic overview of binding of the FITC-c-Raf pS peptide to 14-3-3 isoforms and uptake of FITC-c-Raf pS in individual populations of coacervates containing either the weak 14-3-3σ isoform or the strong 14-3-3γ isoform. b Confocal micrographs showing the uptake of FITC-c-Raf pS in individual populations in the absence or presence of different 14-3-3 isoforms. Scale bar: 25 µm. Uncropped images are available in Supplementary Fig . c Schematic overview of competitive uptake of FITC-c-Raf pS into the coacervates containing two 14-3-3 isoforms with different affinity. d Confocal micrograph of competitive FITC-c-Raf pS uptake in a mixed coacervate sample containing coacervates loaded with either 14-3-3σ or with 14-3-3γ. Scale bar: 25 µm. Uncropped images are available in Supplementary Fig. . e , f Quantification of the FITC-c-Raf pS signal from micrographs of individual populations ( e ) or mixed ( f ) coacervate populations containing different 14-3-3 isoforms. Statistical differences were analyzed by nonparametric Dunn’s test with correction for multiple comparisons, with N ≥ 21 coacervates across multiple imaging positions in the same sample. P values are shown above the comparison. Dashed lines represent the median and dotted lines represent the upper and lower quartiles. ns: no statistical difference. The fold difference is given as the fold difference between the means.

    Journal: Communications Chemistry

    Article Title: Competitive protein recruitment in artificial cells

    doi: 10.1038/s42004-024-01229-9

    Figure Lengend Snippet: a Schematic overview of binding of the FITC-c-Raf pS peptide to 14-3-3 isoforms and uptake of FITC-c-Raf pS in individual populations of coacervates containing either the weak 14-3-3σ isoform or the strong 14-3-3γ isoform. b Confocal micrographs showing the uptake of FITC-c-Raf pS in individual populations in the absence or presence of different 14-3-3 isoforms. Scale bar: 25 µm. Uncropped images are available in Supplementary Fig . c Schematic overview of competitive uptake of FITC-c-Raf pS into the coacervates containing two 14-3-3 isoforms with different affinity. d Confocal micrograph of competitive FITC-c-Raf pS uptake in a mixed coacervate sample containing coacervates loaded with either 14-3-3σ or with 14-3-3γ. Scale bar: 25 µm. Uncropped images are available in Supplementary Fig. . e , f Quantification of the FITC-c-Raf pS signal from micrographs of individual populations ( e ) or mixed ( f ) coacervate populations containing different 14-3-3 isoforms. Statistical differences were analyzed by nonparametric Dunn’s test with correction for multiple comparisons, with N ≥ 21 coacervates across multiple imaging positions in the same sample. P values are shown above the comparison. Dashed lines represent the median and dotted lines represent the upper and lower quartiles. ns: no statistical difference. The fold difference is given as the fold difference between the means.

    Article Snippet: The combined fractions were extensively dialyzed against coacervate buffer (20 mM HEPES, 100 mM KCl, pH 7.5, freshly prepared with 100 µM tris(2-carboxyethyl)phosphine (TCEP) using membrane tubing with a molecular weight cut-off (MWCO) of 12–14 kDa (Fisher Scientific).

    Techniques: Binding Assay, Imaging, Comparison