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  • 99
    New England Biolabs mgcl2
    Mgcl2, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 9114 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/New England Biolabs
    Average 99 stars, based on 9114 article reviews
    Price from $9.99 to $1999.99
    mgcl2 - by Bioz Stars, 2020-12
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    99
    Thermo Fisher mgcl2
    Mgcl2, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 120039 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Thermo Fisher
    Average 99 stars, based on 120039 article reviews
    Price from $9.99 to $1999.99
    mgcl2 - by Bioz Stars, 2020-12
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    99
    Millipore mgcl2
    Mgcl2, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 50653 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Millipore
    Average 99 stars, based on 50653 article reviews
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    mgcl2 - by Bioz Stars, 2020-12
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    94
    Meridian Life Science mgcl2
    Multiple profiles established on short sediment cores.  For consistency, results for the three different sites are displayed vertically according to their water depths.  (A)  From left to right: Total organic carbon and total carbon (wt%); molar C org /N ratio measured in bulk sediments; calcium, magnesium, chloride, and sulfate concentrations (μM) measured in the pore water; potential sulfate reduction rates (nmol × cm -3  day -1 ) obtained after 24 h incubation experiments; ammonium concentrations (μM) in the pore water measured by cell dialysis.  (B)  From left to right: Cell counts in log scale (log 10  cells × cm -3 ); concentrations of extracellular DNA (gray dots) and total DNA (black squares) (μg × g wet sediment -1 ), with distance between the two curves corresponding to intracellular DNA concentrations; Shannon index established from bacterial and archaeal DGGE gel features, with eDNA (gray dots) and iDNA (black squares) displayed separately; range-weighted richness index for bacterial DNA (square) and archaeal DNA (dots), with eDNA (gray) and iDNA (black) displayed separately.
    Mgcl2, supplied by Meridian Life Science, used in various techniques. Bioz Stars score: 94/100, based on 6379 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Meridian Life Science
    Average 94 stars, based on 6379 article reviews
    Price from $9.99 to $1999.99
    mgcl2 - by Bioz Stars, 2020-12
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    97
    Promega mgcl2
    Multiple profiles established on short sediment cores.  For consistency, results for the three different sites are displayed vertically according to their water depths.  (A)  From left to right: Total organic carbon and total carbon (wt%); molar C org /N ratio measured in bulk sediments; calcium, magnesium, chloride, and sulfate concentrations (μM) measured in the pore water; potential sulfate reduction rates (nmol × cm -3  day -1 ) obtained after 24 h incubation experiments; ammonium concentrations (μM) in the pore water measured by cell dialysis.  (B)  From left to right: Cell counts in log scale (log 10  cells × cm -3 ); concentrations of extracellular DNA (gray dots) and total DNA (black squares) (μg × g wet sediment -1 ), with distance between the two curves corresponding to intracellular DNA concentrations; Shannon index established from bacterial and archaeal DGGE gel features, with eDNA (gray dots) and iDNA (black squares) displayed separately; range-weighted richness index for bacterial DNA (square) and archaeal DNA (dots), with eDNA (gray) and iDNA (black) displayed separately.
    Mgcl2, supplied by Promega, used in various techniques. Bioz Stars score: 97/100, based on 37407 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Promega
    Average 97 stars, based on 37407 article reviews
    Price from $9.99 to $1999.99
    mgcl2 - by Bioz Stars, 2020-12
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    99
    Thermo Fisher m mgcl2
    Multiple profiles established on short sediment cores.  For consistency, results for the three different sites are displayed vertically according to their water depths.  (A)  From left to right: Total organic carbon and total carbon (wt%); molar C org /N ratio measured in bulk sediments; calcium, magnesium, chloride, and sulfate concentrations (μM) measured in the pore water; potential sulfate reduction rates (nmol × cm -3  day -1 ) obtained after 24 h incubation experiments; ammonium concentrations (μM) in the pore water measured by cell dialysis.  (B)  From left to right: Cell counts in log scale (log 10  cells × cm -3 ); concentrations of extracellular DNA (gray dots) and total DNA (black squares) (μg × g wet sediment -1 ), with distance between the two curves corresponding to intracellular DNA concentrations; Shannon index established from bacterial and archaeal DGGE gel features, with eDNA (gray dots) and iDNA (black squares) displayed separately; range-weighted richness index for bacterial DNA (square) and archaeal DNA (dots), with eDNA (gray) and iDNA (black) displayed separately.
    M Mgcl2, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4068 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 4068 article reviews
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    m mgcl2 - by Bioz Stars, 2020-12
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    92
    Boehringer Mannheim mgcl2
    Multiple profiles established on short sediment cores.  For consistency, results for the three different sites are displayed vertically according to their water depths.  (A)  From left to right: Total organic carbon and total carbon (wt%); molar C org /N ratio measured in bulk sediments; calcium, magnesium, chloride, and sulfate concentrations (μM) measured in the pore water; potential sulfate reduction rates (nmol × cm -3  day -1 ) obtained after 24 h incubation experiments; ammonium concentrations (μM) in the pore water measured by cell dialysis.  (B)  From left to right: Cell counts in log scale (log 10  cells × cm -3 ); concentrations of extracellular DNA (gray dots) and total DNA (black squares) (μg × g wet sediment -1 ), with distance between the two curves corresponding to intracellular DNA concentrations; Shannon index established from bacterial and archaeal DGGE gel features, with eDNA (gray dots) and iDNA (black squares) displayed separately; range-weighted richness index for bacterial DNA (square) and archaeal DNA (dots), with eDNA (gray) and iDNA (black) displayed separately.
    Mgcl2, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 92/100, based on 3601 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Boehringer Mannheim
    Average 92 stars, based on 3601 article reviews
    Price from $9.99 to $1999.99
    mgcl2 - by Bioz Stars, 2020-12
    92/100 stars
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    99
    Bio-Rad mgcl2
    Multiple profiles established on short sediment cores.  For consistency, results for the three different sites are displayed vertically according to their water depths.  (A)  From left to right: Total organic carbon and total carbon (wt%); molar C org /N ratio measured in bulk sediments; calcium, magnesium, chloride, and sulfate concentrations (μM) measured in the pore water; potential sulfate reduction rates (nmol × cm -3  day -1 ) obtained after 24 h incubation experiments; ammonium concentrations (μM) in the pore water measured by cell dialysis.  (B)  From left to right: Cell counts in log scale (log 10  cells × cm -3 ); concentrations of extracellular DNA (gray dots) and total DNA (black squares) (μg × g wet sediment -1 ), with distance between the two curves corresponding to intracellular DNA concentrations; Shannon index established from bacterial and archaeal DGGE gel features, with eDNA (gray dots) and iDNA (black squares) displayed separately; range-weighted richness index for bacterial DNA (square) and archaeal DNA (dots), with eDNA (gray) and iDNA (black) displayed separately.
    Mgcl2, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 2331 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Bio-Rad
    Average 99 stars, based on 2331 article reviews
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    mgcl2 - by Bioz Stars, 2020-12
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    98
    TaKaRa mgcl2
    Multiple profiles established on short sediment cores.  For consistency, results for the three different sites are displayed vertically according to their water depths.  (A)  From left to right: Total organic carbon and total carbon (wt%); molar C org /N ratio measured in bulk sediments; calcium, magnesium, chloride, and sulfate concentrations (μM) measured in the pore water; potential sulfate reduction rates (nmol × cm -3  day -1 ) obtained after 24 h incubation experiments; ammonium concentrations (μM) in the pore water measured by cell dialysis.  (B)  From left to right: Cell counts in log scale (log 10  cells × cm -3 ); concentrations of extracellular DNA (gray dots) and total DNA (black squares) (μg × g wet sediment -1 ), with distance between the two curves corresponding to intracellular DNA concentrations; Shannon index established from bacterial and archaeal DGGE gel features, with eDNA (gray dots) and iDNA (black squares) displayed separately; range-weighted richness index for bacterial DNA (square) and archaeal DNA (dots), with eDNA (gray) and iDNA (black) displayed separately.
    Mgcl2, supplied by TaKaRa, used in various techniques. Bioz Stars score: 98/100, based on 15312 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/TaKaRa
    Average 98 stars, based on 15312 article reviews
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    mgcl2 - by Bioz Stars, 2020-12
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    92
    Fisher Scientific mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
    Mgcl2, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 92/100, based on 1122 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Fisher Scientific
    Average 92 stars, based on 1122 article reviews
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    mgcl2 - by Bioz Stars, 2020-12
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    94
    Eppendorf AG mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
    Mgcl2, supplied by Eppendorf AG, used in various techniques. Bioz Stars score: 94/100, based on 1687 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Eppendorf AG
    Average 94 stars, based on 1687 article reviews
    Price from $9.99 to $1999.99
    mgcl2 - by Bioz Stars, 2020-12
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    99
    GE Healthcare mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
    Mgcl2, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 11018 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/GE Healthcare
    Average 99 stars, based on 11018 article reviews
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    mgcl2 - by Bioz Stars, 2020-12
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    94
    Merck & Co mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
    Mgcl2, supplied by Merck & Co, used in various techniques. Bioz Stars score: 94/100, based on 1246 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Merck & Co
    Average 94 stars, based on 1246 article reviews
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    mgcl2 - by Bioz Stars, 2020-12
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    92
    CinnaGen Co mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
    Mgcl2, supplied by CinnaGen Co, used in various techniques. Bioz Stars score: 92/100, based on 1702 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/CinnaGen Co
    Average 92 stars, based on 1702 article reviews
    Price from $9.99 to $1999.99
    mgcl2 - by Bioz Stars, 2020-12
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    92
    Merck KGaA mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
    Mgcl2, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 92/100, based on 891 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Merck KGaA
    Average 92 stars, based on 891 article reviews
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    mgcl2 - by Bioz Stars, 2020-12
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    92
    Kaneka Corp mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
    Mgcl2, supplied by Kaneka Corp, used in various techniques. Bioz Stars score: 92/100, based on 1111 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Kaneka Corp
    Average 92 stars, based on 1111 article reviews
    Price from $9.99 to $1999.99
    mgcl2 - by Bioz Stars, 2020-12
    92/100 stars
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    92
    Stratagene mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
    Mgcl2, supplied by Stratagene, used in various techniques. Bioz Stars score: 92/100, based on 1242 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    R&D Systems mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
    Mgcl2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 99/100, based on 888 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Solis BioDyne mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
    Mgcl2, supplied by Solis BioDyne, used in various techniques. Bioz Stars score: 92/100, based on 1339 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Carl Roth GmbH mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
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    Valiant mgcl2
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
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    Millipore pcr buffer
    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), <t>MgCl2</t> (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.
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    Image Search Results


    Multiple profiles established on short sediment cores.  For consistency, results for the three different sites are displayed vertically according to their water depths.  (A)  From left to right: Total organic carbon and total carbon (wt%); molar C org /N ratio measured in bulk sediments; calcium, magnesium, chloride, and sulfate concentrations (μM) measured in the pore water; potential sulfate reduction rates (nmol × cm -3  day -1 ) obtained after 24 h incubation experiments; ammonium concentrations (μM) in the pore water measured by cell dialysis.  (B)  From left to right: Cell counts in log scale (log 10  cells × cm -3 ); concentrations of extracellular DNA (gray dots) and total DNA (black squares) (μg × g wet sediment -1 ), with distance between the two curves corresponding to intracellular DNA concentrations; Shannon index established from bacterial and archaeal DGGE gel features, with eDNA (gray dots) and iDNA (black squares) displayed separately; range-weighted richness index for bacterial DNA (square) and archaeal DNA (dots), with eDNA (gray) and iDNA (black) displayed separately.

    Journal: Frontiers in Microbiology

    Article Title: Geomicrobiological Features of Ferruginous Sediments from Lake Towuti, Indonesia

    doi: 10.3389/fmicb.2016.01007

    Figure Lengend Snippet: Multiple profiles established on short sediment cores. For consistency, results for the three different sites are displayed vertically according to their water depths. (A) From left to right: Total organic carbon and total carbon (wt%); molar C org /N ratio measured in bulk sediments; calcium, magnesium, chloride, and sulfate concentrations (μM) measured in the pore water; potential sulfate reduction rates (nmol × cm -3 day -1 ) obtained after 24 h incubation experiments; ammonium concentrations (μM) in the pore water measured by cell dialysis. (B) From left to right: Cell counts in log scale (log 10 cells × cm -3 ); concentrations of extracellular DNA (gray dots) and total DNA (black squares) (μg × g wet sediment -1 ), with distance between the two curves corresponding to intracellular DNA concentrations; Shannon index established from bacterial and archaeal DGGE gel features, with eDNA (gray dots) and iDNA (black squares) displayed separately; range-weighted richness index for bacterial DNA (square) and archaeal DNA (dots), with eDNA (gray) and iDNA (black) displayed separately.

    Article Snippet: PCR was performed with 2.5 μL of DNA template, 12.5 μL of MangoMix (Bioline, Life Science Company, London, UK), 0.5 μmol L-1 of each of the primers, 1 μL of MgCl2 (25 mM) and 8 μL of Ultra-pure 18.2 Mω PCR Water (Bioline).

    Techniques: Incubation, Denaturing Gradient Gel Electrophoresis

    EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.

    Journal: Biochemistry

    Article Title: Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1

    doi: 10.1021/acs.biochem.6b00401

    Figure Lengend Snippet: EGCG binding to the E·(PAP)2 Complex. A.) The Binding-Reaction Progress Curve . Binding-induced fluorescence changes were monitored using a stopped-flow fluorimeter (λ ex = 290 nm, λ em ≥ 325 nm (cutoff filter). Reactions were initiated by rapidly mixing (1:1 v/v) a solution containing SULT1A1 (0.25μM, active sites), PAP (0.50 mM), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C with a solution that was identical except that it lacked SULT1A1 and contained EGCG. The curve through the data (red line) is the behavior predicted by the best fit to a double-exponential model. The insert shows the residuals from a single- (black) and doubleexponential (red) fit. The single-exponential model deviates substantially from the data, while the bi-phasic model provides an excellent fit. B.) k obs vs [EGCG] for the First (Fast) Phase . kobs values were obtained at the four indicated EGCG concentrations under the conditions given in Panel A. Each value is the average of three independent determinations. The reactions were pseudo-first-order in EGCG in all cases. C.) EGCG Dissociation from E·(PAP) 2 ·(EGCG) 2 Complex . A pulse solution containing SULT1A1 (20 μM, monomer), EGCG (24 μM (4.0 μM free, 100 × Kd)), and PAP (500 μM, 16 ▪ K d low affinity site ), MgCl2 (5.0 mM), NaPO4 (50 mM), pH 7.5, 25 ± 2°C, was diluted 200:1 into a chase solution containing 75 μM 4-hydroxytamoxifen (TAM, 100 ▪ K d cap open form ), PAP (0.50 mM, 16 ▪ K d low affinity site ), NaPO4 (50 mM), MgCl2 (5.0 mM), pH 7.5, 25 ± 2°C. The final EGCG concentration is 0.12 μM (0.20 ▪ K d cap open form ). Dissociation was monitored by a change in SULT1A1 fluorescence (λ ex = 290 nm, λ em = 370 nm). Three progress curves (black dots) are superposed. The curve through the data is the behavior predicted by a best-fit, single-exponential model.

    Article Snippet: Ampicillin, HEPES, KCl, KOH, MgCl2 , NaCl and phenylmethylsulfonyl fluoride (PMSF) were purchased from Fisher Scientific.

    Techniques: Binding Assay, Fluorescence, Flow Cytometry, Concentration Assay