hepes  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc hepes
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    Gold Biotechnology Inc hepes
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    krebs ringer hepes  (Gold Biotechnology Inc)


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    hydroxyethyl 1 piperazineethanesulfonic acid hepes  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc hepes
    a Confocal microscopy images of droplets of 50 μM tau with 80 nM 12mer arrays (1 μM equivalent of mononucleosomes), 1 μM mononucleosomes, or 80 nM 2.1 kbp DNA (1 μM equivalent of ‘601’ DNA sites), visualized with 5% Cy5-tau (scale bar = 50 μm). Studies were conducted in 20 mM <t>HEPES</t> buffer, 25 <t>mM</t> <t>NaCl,</t> 0.5 mM TCEP, pH 7.2. b FRAP analysis of 50 μM tau droplets with different LLPS inducers in the same low salt buffer. The standard deviation and the best monoexponential fit curve are plotted for each data set. Quantification of maximum recovery (%) and half-life (s) are tabulated in Table . c Turbidity at A 600 of tau solutions with different LLPS inducers in the same low salt buffer. Individual replicates are shown, and the line indicates the mean. d Schematic of the compaction behavior of 12mer arrays in the presence of cations, including physiological salt. e Confocal microscopy images of 50 μM tau (with 5% Cy5-labelled tau) with 80 nM 12mer arrays at 150 mM NaCl (scale bar = 50 μm) in the same buffer. YOYO-1 was added to visualize the arrays. f EMSA of 4 nM 12mer arrays with and without tau, in 20 mM HEPES buffer, 150 mM NaCl, 0.5 mM TCEP, 0.1% Tween, pH 7.2. MN – mononucleosomes.
    Hepes, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Phosphorylation regulates tau’s phase separation behavior and interactions with chromatin"

    Article Title: Phosphorylation regulates tau’s phase separation behavior and interactions with chromatin

    Journal: Communications Biology

    doi: 10.1038/s42003-024-05920-4

    a Confocal microscopy images of droplets of 50 μM tau with 80 nM 12mer arrays (1 μM equivalent of mononucleosomes), 1 μM mononucleosomes, or 80 nM 2.1 kbp DNA (1 μM equivalent of ‘601’ DNA sites), visualized with 5% Cy5-tau (scale bar = 50 μm). Studies were conducted in 20 mM HEPES buffer, 25 mM NaCl, 0.5 mM TCEP, pH 7.2. b FRAP analysis of 50 μM tau droplets with different LLPS inducers in the same low salt buffer. The standard deviation and the best monoexponential fit curve are plotted for each data set. Quantification of maximum recovery (%) and half-life (s) are tabulated in Table . c Turbidity at A 600 of tau solutions with different LLPS inducers in the same low salt buffer. Individual replicates are shown, and the line indicates the mean. d Schematic of the compaction behavior of 12mer arrays in the presence of cations, including physiological salt. e Confocal microscopy images of 50 μM tau (with 5% Cy5-labelled tau) with 80 nM 12mer arrays at 150 mM NaCl (scale bar = 50 μm) in the same buffer. YOYO-1 was added to visualize the arrays. f EMSA of 4 nM 12mer arrays with and without tau, in 20 mM HEPES buffer, 150 mM NaCl, 0.5 mM TCEP, 0.1% Tween, pH 7.2. MN – mononucleosomes.
    Figure Legend Snippet: a Confocal microscopy images of droplets of 50 μM tau with 80 nM 12mer arrays (1 μM equivalent of mononucleosomes), 1 μM mononucleosomes, or 80 nM 2.1 kbp DNA (1 μM equivalent of ‘601’ DNA sites), visualized with 5% Cy5-tau (scale bar = 50 μm). Studies were conducted in 20 mM HEPES buffer, 25 mM NaCl, 0.5 mM TCEP, pH 7.2. b FRAP analysis of 50 μM tau droplets with different LLPS inducers in the same low salt buffer. The standard deviation and the best monoexponential fit curve are plotted for each data set. Quantification of maximum recovery (%) and half-life (s) are tabulated in Table . c Turbidity at A 600 of tau solutions with different LLPS inducers in the same low salt buffer. Individual replicates are shown, and the line indicates the mean. d Schematic of the compaction behavior of 12mer arrays in the presence of cations, including physiological salt. e Confocal microscopy images of 50 μM tau (with 5% Cy5-labelled tau) with 80 nM 12mer arrays at 150 mM NaCl (scale bar = 50 μm) in the same buffer. YOYO-1 was added to visualize the arrays. f EMSA of 4 nM 12mer arrays with and without tau, in 20 mM HEPES buffer, 150 mM NaCl, 0.5 mM TCEP, 0.1% Tween, pH 7.2. MN – mononucleosomes.

    Techniques Used: Confocal Microscopy, Standard Deviation

    a EMSA of 20 nM 177 bp mononucleosomes and 147 bp ‘linker-free’ mononucleosomes with various concentrations of tau, in 20 mM HEPES buffer, 10 mM NaCl, 0.5 mM TCEP, 0.1% Tween, pH 7.2. b EMSA of 20 nM 177 bp DNA with various concentrations of tau, in the same low salt buffer. c Quantification of binding propensity based on the intensity of the unbound DNA or mononucleosome bands in Fig. 2a, b. Individual replicates are shown, and curves were fitted to a one-site-specific binding with Hill Slope equation. 177 bp DNA, 147 bp mononucleosomes, and 177 bp mononucleosomes were quantified for the following data points: 0, 125, 250, 500, and 1000 nM. 16–62 nM data points were excluded for the mononucleosome binding due to the smearing and complex bands overlapping with the unbound probe. MN – mononucleosomes.
    Figure Legend Snippet: a EMSA of 20 nM 177 bp mononucleosomes and 147 bp ‘linker-free’ mononucleosomes with various concentrations of tau, in 20 mM HEPES buffer, 10 mM NaCl, 0.5 mM TCEP, 0.1% Tween, pH 7.2. b EMSA of 20 nM 177 bp DNA with various concentrations of tau, in the same low salt buffer. c Quantification of binding propensity based on the intensity of the unbound DNA or mononucleosome bands in Fig. 2a, b. Individual replicates are shown, and curves were fitted to a one-site-specific binding with Hill Slope equation. 177 bp DNA, 147 bp mononucleosomes, and 177 bp mononucleosomes were quantified for the following data points: 0, 125, 250, 500, and 1000 nM. 16–62 nM data points were excluded for the mononucleosome binding due to the smearing and complex bands overlapping with the unbound probe. MN – mononucleosomes.

    Techniques Used: Binding Assay

    a TEM images and schematic of cation-induced compaction of 12mer arrays (11.3 nM of 12mer array which is equivalent to 136 nM of mononucleosomes) with MgCl 2 , as compaction control, and increasing concentrations of tau (0.136 μM and 1.36 μM), conducted in 20 mM HEPES buffer, 10 mM NaCl, 0.5 mM TCEP, pH 7.2. b (left) Schematic of the chromatin oligomerization assay. 12mer arrays were incubated in different buffer conditions, subjected to low-speed centrifugation, and the A260 of the supernatant was measured. The soluble fraction reflects the degree of self-association of the 12mer arrays. (right) Increasing concentrations of tau were incubated with 30 nM 12mer arrays (for an A260 ~ 1) in different salt conditions in the same buffer. Individual replicates are shown, and the line indicates the mean. c (left) Schematic of the MNase digestion assay to probe for DNA protection within 12mer arrays. (right) Time course of MNase digestion of 2 nM 12mer arrays with varying concentrations of tau and MgCl 2 , in the same buffer. All lanes contain a band at ~150 bp which results from a small amount of MMTV nucleosomes present in the sample.
    Figure Legend Snippet: a TEM images and schematic of cation-induced compaction of 12mer arrays (11.3 nM of 12mer array which is equivalent to 136 nM of mononucleosomes) with MgCl 2 , as compaction control, and increasing concentrations of tau (0.136 μM and 1.36 μM), conducted in 20 mM HEPES buffer, 10 mM NaCl, 0.5 mM TCEP, pH 7.2. b (left) Schematic of the chromatin oligomerization assay. 12mer arrays were incubated in different buffer conditions, subjected to low-speed centrifugation, and the A260 of the supernatant was measured. The soluble fraction reflects the degree of self-association of the 12mer arrays. (right) Increasing concentrations of tau were incubated with 30 nM 12mer arrays (for an A260 ~ 1) in different salt conditions in the same buffer. Individual replicates are shown, and the line indicates the mean. c (left) Schematic of the MNase digestion assay to probe for DNA protection within 12mer arrays. (right) Time course of MNase digestion of 2 nM 12mer arrays with varying concentrations of tau and MgCl 2 , in the same buffer. All lanes contain a band at ~150 bp which results from a small amount of MMTV nucleosomes present in the sample.

    Techniques Used: Incubation, Centrifugation

    a Gel analysis of tau phosphorylation using PKA, GSK or both (full gel image presented in Fig. ). b Abundance of different masses corresponding to the number of phosphates for each phosphorylated form as detected by intact MS analysis. Mass values were binned to the nearest whole number of phosphates. Error bars reflect standard deviation resulting from independent phosphorylation reactions. Individual replicates and non-binned values can be found in Fig. . c Turbidity (A 600 ) analysis of wild-type and phosphorylated tau constructs, with LLPS induced by 10% PEG-6000, in 20 mM HEPES buffer, 25 mM NaCl, 0.5 mM TCEP, pH 7.2. Individual replicates are shown, and the error bars reflect the standard deviation. d Confocal microscopy images of liquid droplets of 50 μM PKA, GSK or PKA-GSK phosphorylated tau with 12mer arrays, spiked with 5% Cy5-tau (control) or Cy5-ptau (phosphorylated samples), in the same low salt buffer. YOYO-1 was added to visualize the 12mer arrays (scale bar = 50 μm). e A 600 turbidity measurements of the phase separation of PKA, GSK or PKA-GSK phosphorylated tau with 12mer arrays as function of tau concentration. Studies were conducted in the same low-salt buffer. Individual replicates are shown and the line indicates the mean. f (left) EMSA to assess the binding propensity of PKA-GSK phosphorylated tau with 20 nM 177 bp DNA, or mononucleosomes in the same buffer containing 10 mM NaCl. Representative gel images from three independent experiments are shown. (right) Quantification of binding propensity based on the intensity of the unbound DNA or mononucleosome bands. Individual replicates are shown, and curves were fitted to a one-site-specific binding with Hill Slope equation. g MNase digestion of 12mer array samples containing varying concentrations of wild-type or PKA-GSK phosphorylated tau. (-) is an undigested control, the lane with Mg 2+ controls for the effect of compaction, and (+) is a positive control for complete digestion. Protein concentrations used in the gradient are 5, 10, 25, and 50 μM. Studies were conducted in the same buffer containing 10 mM NaCl. h TEM image of 12mer arrays (11.3 nM, or 136 nM equivalent of mononucleosomes) with 1.36 μM PKA-GSK phosphorylated tau, in the same buffer containing 10 mM NaCl. MN mononucleosomes, PG PKA-GSK phosphorylated tau, MW molecular weight.
    Figure Legend Snippet: a Gel analysis of tau phosphorylation using PKA, GSK or both (full gel image presented in Fig. ). b Abundance of different masses corresponding to the number of phosphates for each phosphorylated form as detected by intact MS analysis. Mass values were binned to the nearest whole number of phosphates. Error bars reflect standard deviation resulting from independent phosphorylation reactions. Individual replicates and non-binned values can be found in Fig. . c Turbidity (A 600 ) analysis of wild-type and phosphorylated tau constructs, with LLPS induced by 10% PEG-6000, in 20 mM HEPES buffer, 25 mM NaCl, 0.5 mM TCEP, pH 7.2. Individual replicates are shown, and the error bars reflect the standard deviation. d Confocal microscopy images of liquid droplets of 50 μM PKA, GSK or PKA-GSK phosphorylated tau with 12mer arrays, spiked with 5% Cy5-tau (control) or Cy5-ptau (phosphorylated samples), in the same low salt buffer. YOYO-1 was added to visualize the 12mer arrays (scale bar = 50 μm). e A 600 turbidity measurements of the phase separation of PKA, GSK or PKA-GSK phosphorylated tau with 12mer arrays as function of tau concentration. Studies were conducted in the same low-salt buffer. Individual replicates are shown and the line indicates the mean. f (left) EMSA to assess the binding propensity of PKA-GSK phosphorylated tau with 20 nM 177 bp DNA, or mononucleosomes in the same buffer containing 10 mM NaCl. Representative gel images from three independent experiments are shown. (right) Quantification of binding propensity based on the intensity of the unbound DNA or mononucleosome bands. Individual replicates are shown, and curves were fitted to a one-site-specific binding with Hill Slope equation. g MNase digestion of 12mer array samples containing varying concentrations of wild-type or PKA-GSK phosphorylated tau. (-) is an undigested control, the lane with Mg 2+ controls for the effect of compaction, and (+) is a positive control for complete digestion. Protein concentrations used in the gradient are 5, 10, 25, and 50 μM. Studies were conducted in the same buffer containing 10 mM NaCl. h TEM image of 12mer arrays (11.3 nM, or 136 nM equivalent of mononucleosomes) with 1.36 μM PKA-GSK phosphorylated tau, in the same buffer containing 10 mM NaCl. MN mononucleosomes, PG PKA-GSK phosphorylated tau, MW molecular weight.

    Techniques Used: Standard Deviation, Construct, Confocal Microscopy, Concentration Assay, Binding Assay, Positive Control, Molecular Weight

    a Confocal microscopy images of droplets of 50 μM tau and 50 μM pHP1α, with and without 80 nM 12mer arrays, imaged using 5% Cy5-tau, 5% Cy3-pHP1α, and YOYO-1 (scale bar = 50 μm), in 20 mM HEPES buffer, 25 mM NaCl, 0.5 mM TCEP, pH 7.2. b Co-localization of tau, pHP1α, and 12mer arrays in the same buffer containing 150 mM NaCl. See Fig. for the full overlay. c FRAP analysis of tau mobility in samples containing 50 μM tau with pHP1α alone (purple) or pHP1α and 12mer arrays (blue) in the same low salt buffer. The standard deviation and the best monoexponential fit curve are plotted for each data set. Quantification of maximum recovery (%) and half-life (s) are tabulated in Table . d Confocal microscopy images of 50 μM pHP1α and 50 μM PKA, GSK or PKA-GSK phosphorylated tau (top) and 50 μM pHP1α, 50 μM phosphorylated tau, and 80 nM 12mer arrays (bottom), in the same low salt buffer.
    Figure Legend Snippet: a Confocal microscopy images of droplets of 50 μM tau and 50 μM pHP1α, with and without 80 nM 12mer arrays, imaged using 5% Cy5-tau, 5% Cy3-pHP1α, and YOYO-1 (scale bar = 50 μm), in 20 mM HEPES buffer, 25 mM NaCl, 0.5 mM TCEP, pH 7.2. b Co-localization of tau, pHP1α, and 12mer arrays in the same buffer containing 150 mM NaCl. See Fig. for the full overlay. c FRAP analysis of tau mobility in samples containing 50 μM tau with pHP1α alone (purple) or pHP1α and 12mer arrays (blue) in the same low salt buffer. The standard deviation and the best monoexponential fit curve are plotted for each data set. Quantification of maximum recovery (%) and half-life (s) are tabulated in Table . d Confocal microscopy images of 50 μM pHP1α and 50 μM PKA, GSK or PKA-GSK phosphorylated tau (top) and 50 μM pHP1α, 50 μM phosphorylated tau, and 80 nM 12mer arrays (bottom), in the same low salt buffer.

    Techniques Used: Confocal Microscopy, Standard Deviation

    hepes  (Gold Biotechnology Inc)


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