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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 1702 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/buffer 100 mm kcl/product/Bio-Rad
Average 96 stars, based on 1702 article reviews

buffer 100 mm kcl - by Bioz Stars, 2026-05

96/100 stars

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buffer 100 mm kcl (Bio-Rad)

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lysis buffer containing 25 mm tris-hcl, ph 8.0, 137 mm nacl, 2.7 mm kcl, 1% triton x-100 and protease inhibitor mixture (Thermo Fisher)

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Lysis Buffer Containing 25 Mm Tris Hcl, Ph 8.0, 137 Mm Nacl, 2.7 Mm Kcl, 1% Triton X 100 And Protease Inhibitor Mixture, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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saline phosphate buffer (pbs) consisting of a 100 mm sodium phosphate buffer of ph 7.4 supplemented with 2.0 g nacl and 50.25 mg kcl (Scharlau Group)

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Saline Phosphate Buffer (Pbs) Consisting Of A 100 Mm Sodium Phosphate Buffer Of Ph 7.4 Supplemented With 2.0 G Nacl And 50.25 Mg Kcl, supplied by Scharlau Group, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Protein Extraction Buffer (20 Mm Hepes–Koh Ph 7.9; 100 Mm Kcl; 20% (V/V) Glycerol; 0.2 Mm Edta, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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coacervate buffer (20 mm hepes, 100 mm kcl, ph 7.5, freshly prepared with 100 µm tris(2-carboxyethyl)phosphine (tcep) (Fisher Scientific)

Fisher Scientific coacervate buffer (20 mm hepes, 100 mm kcl, ph 7.5, freshly prepared with 100 µm tris(2-carboxyethyl)phosphine (tcep)

a Schematic overview of affinity-based uptake of a client peptide of the 14-3-3 hub protein in a specific <t>coacervate</t> 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.

Coacervate Buffer (20 Mm Hepes, 100 Mm Kcl, Ph 7.5, Freshly Prepared With 100 µm Tris(2 Carboxyethyl)phosphine (Tcep), supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews

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rip buffer (25 mm tris-hcl (ph 7.5), 150 mm kcl, 5 mm edta, 0.5 mm dtt, 0.5% np40, 100 u/ml superase in rnase inhibitor (Thermo Fisher)

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ni_a buffer (25 mm hepes ph 7.6, 100 mm nacl, 100 mm kcl, 10% glycerol, 10 mm mgcl 2 , 0.5 mm edta, and 20 mm imidazole) (Millipore)

Millipore ni_a buffer (25 mm hepes ph 7.6, 100 mm nacl, 100 mm kcl, 10% glycerol, 10 mm mgcl 2 , 0.5 mm edta, and 20 mm imidazole)

Ni A Buffer (25 Mm Hepes Ph 7.6, 100 Mm Nacl, 100 Mm Kcl, 10% Glycerol, 10 Mm Mgcl 2 , 0.5 Mm Edta, And 20 Mm Imidazole), supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews

ni_a buffer (25 mm hepes ph 7.6, 100 mm nacl, 100 mm kcl, 10% glycerol, 10 mm mgcl 2 , 0.5 mm edta, and 20 mm imidazole) - by Bioz Stars, 2026-05

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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.

Techniques: Binding Assay, Imaging, Comparison