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  • 94
    Valiant mgcl2
    Mgcl2, supplied by Valiant, used in various techniques. Bioz Stars score: 94/100, based on 1135 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Valiant
    Average 94 stars, based on 1135 article reviews
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    mgcl2 - by Bioz Stars, 2021-02
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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
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    mgcl2 - by Bioz Stars, 2021-02
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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
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    mgcl2 - by Bioz Stars, 2021-02
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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
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    Average 99 stars, based on 50653 article reviews
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    mgcl2 - by Bioz Stars, 2021-02
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    97
    Millipore m mgcl2
    M Mgcl2, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 4183 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/m mgcl2/product/Millipore
    Average 97 stars, based on 4183 article reviews
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    m mgcl2 - by Bioz Stars, 2021-02
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    Thermo Fisher m mgcl2
    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
    https://www.bioz.com/result/m mgcl2/product/Thermo Fisher
    Average 99 stars, based on 4068 article reviews
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    m mgcl2 - by Bioz Stars, 2021-02
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    97
    Promega mgcl2
    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
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    mgcl2 - by Bioz Stars, 2021-02
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    92
    Boehringer Mannheim mgcl2
    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
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    mgcl2 - by Bioz Stars, 2021-02
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    99
    Bio-Rad mgcl2
    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
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    98
    TaKaRa mgcl2
    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, 2021-02
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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, 2021-02
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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, 2021-02
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    92
    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: 92/100, based on 1246 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Merck & Co
    Average 92 stars, based on 1246 article reviews
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    mgcl2 - by Bioz Stars, 2021-02
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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, 2021-02
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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
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    mgcl2 - by Bioz Stars, 2021-02
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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
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    mgcl2 - by Bioz Stars, 2021-02
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    92
    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.
    Mgcl2, supplied by Carl Roth GmbH, used in various techniques. Bioz Stars score: 92/100, based on 504 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl2/product/Carl Roth GmbH
    Average 92 stars, based on 504 article reviews
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    mgcl2 - by Bioz Stars, 2021-02
    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
    https://www.bioz.com/result/mgcl2/product/Stratagene
    Average 92 stars, based on 1242 article reviews
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    mgcl2 - by Bioz Stars, 2021-02
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    92
    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
    https://www.bioz.com/result/mgcl2/product/Solis BioDyne
    Average 92 stars, based on 1339 article reviews
    Price from $9.99 to $1999.99
    mgcl2 - by Bioz Stars, 2021-02
    92/100 stars
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    99
    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.
    Pcr Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2561 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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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    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