mantadp  (Jena Bioscience)


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  • 93
    Name:
    Mant ADP
    Description:

    Catalog Number:
    nu-201l
    Price:
    343.57
    Applications:
    MYOSIN-ATPase cycle[1] SecA cycle[2] Dissociation kinetic proteinkinase A[3] FRET: kinesin[4], myosin[5, 1] Conformational dynamic: DnaC-protein[6]
    Purity:
    ≥ 95 % (HPLC)
    Category:
    Nucleotides Nucleosides
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    Structured Review

    Jena Bioscience mantadp
    Determination of unlabeled nucleotide affinity in the absence of Mg 2+ by kinetic competition with <t>mantADP</t> and yield apparent affinities: K D(−Mg) = 0.8 ± 0.1 mM and K T(−Mg) = 15 ± 4 mM. Uncertainty bars represent standard errors of the fits and are contained within the data points.

    https://www.bioz.com/result/mantadp/product/Jena Bioscience
    Average 93 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    mantadp - by Bioz Stars, 2020-08
    93/100 stars

    Images

    1) Product Images from "Nup159 weakens Gle1 binding to Dbp5 but does not accelerate ADP release"

    Article Title: Nup159 weakens Gle1 binding to Dbp5 but does not accelerate ADP release

    Journal: Journal of molecular biology

    doi: 10.1016/j.jmb.2018.05.025

    Determination of unlabeled nucleotide affinity in the absence of Mg 2+ by kinetic competition with mantADP and yield apparent affinities: K D(−Mg) = 0.8 ± 0.1 mM and K T(−Mg) = 15 ± 4 mM. Uncertainty bars represent standard errors of the fits and are contained within the data points.
    Figure Legend Snippet: Determination of unlabeled nucleotide affinity in the absence of Mg 2+ by kinetic competition with mantADP and yield apparent affinities: K D(−Mg) = 0.8 ± 0.1 mM and K T(−Mg) = 15 ± 4 mM. Uncertainty bars represent standard errors of the fits and are contained within the data points.

    Techniques Used:

    Nup159 minimally affects mantADP(±Mg 2+ ) dissociation kinetics (A) Time courses of irreversible Mg 2+ mantADP dissociation from a pre-incubated solution of Dbp5 (2 μM) and Mg 2+ mantADP (20 μM) upon mixing with 3 mM Mg 2+ ADP and (from lower to upper) 0, 1.5, 4.5, or 10 μM Nup159 in assay buffer containing excess MgCl 2 , yielding K N(+Mg)HmD of 0.3 ± 0.8 μM, k −mD(+Mg) = 2.7 ± 0.1 s −1 and k −mD(+Mg),N = 2.0 ± 0.2 s −1 . (C) Time courses of FRET signal change after mixing pre-equilibrated solutions of 1 μM Dbp5 and 40 μM mantADP with an equal volume of (lower to upper) 0, 3 or 9 μM Nup159 and 10 mM ADP in assay buffer containing excess EDTA (ca. 27 nM [Mg 2+ ] free after mixing). The concentrations are final after mixing. Continuous lines through the data represent best fits to a single exponential. (D) [Nup159]-dependence of the mantADP dissociation observed rate constants obtained from exponential fits in C. ANOVA analysis suggests that the dependence is insignificant and the average dissociation rate constant is ~ 11 s −1 indicated by a horizontal dashed line. Uncertainty bars represent standard error of the fits and are contained within the data points.
    Figure Legend Snippet: Nup159 minimally affects mantADP(±Mg 2+ ) dissociation kinetics (A) Time courses of irreversible Mg 2+ mantADP dissociation from a pre-incubated solution of Dbp5 (2 μM) and Mg 2+ mantADP (20 μM) upon mixing with 3 mM Mg 2+ ADP and (from lower to upper) 0, 1.5, 4.5, or 10 μM Nup159 in assay buffer containing excess MgCl 2 , yielding K N(+Mg)HmD of 0.3 ± 0.8 μM, k −mD(+Mg) = 2.7 ± 0.1 s −1 and k −mD(+Mg),N = 2.0 ± 0.2 s −1 . (C) Time courses of FRET signal change after mixing pre-equilibrated solutions of 1 μM Dbp5 and 40 μM mantADP with an equal volume of (lower to upper) 0, 3 or 9 μM Nup159 and 10 mM ADP in assay buffer containing excess EDTA (ca. 27 nM [Mg 2+ ] free after mixing). The concentrations are final after mixing. Continuous lines through the data represent best fits to a single exponential. (D) [Nup159]-dependence of the mantADP dissociation observed rate constants obtained from exponential fits in C. ANOVA analysis suggests that the dependence is insignificant and the average dissociation rate constant is ~ 11 s −1 indicated by a horizontal dashed line. Uncertainty bars represent standard error of the fits and are contained within the data points.

    Techniques Used: Incubation

    Mg 2+ slows mantADP dissociation from Dbp5 (A) Time courses of FRET signal changes in pre-equilibrated solutions of Dbp5 and mantADP with 2 mM MgCl 2 (Mg 2+ curve) or 4 mM EDTA (EDTA curve) upon rapid mixing with an equal volume of 20 mM ADP in assay buffer containing either 2 mM [MgCl 2 ] free (Mg 2+ curve) or 0 mM [MgCl 2 ] free (EDTA curve). Continuous lines through the data represent best fits to single exponentials, yielding k −mD(−Mg) = 10.0 ± 0.4 s −1 and k −mD(+Mg) = 2.4 ± 0.009 s −1 . (B) [Mg 2+ ] free dependence of the observed rate constants of mantADP dissociation from a pre-formed Dbp5-mantADP (no Mg 2+ , filled circles) or Dbp5-Mg 2+ mantADP complex (open circles). The solid and dashed lines through the data represent the best fits of the data starting with Dbp5-mantADP (filled circles) or Dbp5-Mg 2+ , yielding the two K Mg(HmD) values (160 ± 40 – filled circles and 165 ± 26 μM – open circles) for Mg 2+ binding to Dbp5-mantADP complex as well as the fundamental dissociation rate constants for mantADP (k −mD(-Mg) ≈ 10 and 9 s −1 , no Mg 2+ ) or Mg 2+ mantADP (k −mD(+Mg) ≈ 2.4 and 2.2 s −1 , saturating Mg 2+ ). Uncertainty bars represent standard errors of the fits and are contained within the data points.
    Figure Legend Snippet: Mg 2+ slows mantADP dissociation from Dbp5 (A) Time courses of FRET signal changes in pre-equilibrated solutions of Dbp5 and mantADP with 2 mM MgCl 2 (Mg 2+ curve) or 4 mM EDTA (EDTA curve) upon rapid mixing with an equal volume of 20 mM ADP in assay buffer containing either 2 mM [MgCl 2 ] free (Mg 2+ curve) or 0 mM [MgCl 2 ] free (EDTA curve). Continuous lines through the data represent best fits to single exponentials, yielding k −mD(−Mg) = 10.0 ± 0.4 s −1 and k −mD(+Mg) = 2.4 ± 0.009 s −1 . (B) [Mg 2+ ] free dependence of the observed rate constants of mantADP dissociation from a pre-formed Dbp5-mantADP (no Mg 2+ , filled circles) or Dbp5-Mg 2+ mantADP complex (open circles). The solid and dashed lines through the data represent the best fits of the data starting with Dbp5-mantADP (filled circles) or Dbp5-Mg 2+ , yielding the two K Mg(HmD) values (160 ± 40 – filled circles and 165 ± 26 μM – open circles) for Mg 2+ binding to Dbp5-mantADP complex as well as the fundamental dissociation rate constants for mantADP (k −mD(-Mg) ≈ 10 and 9 s −1 , no Mg 2+ ) or Mg 2+ mantADP (k −mD(+Mg) ≈ 2.4 and 2.2 s −1 , saturating Mg 2+ ). Uncertainty bars represent standard errors of the fits and are contained within the data points.

    Techniques Used: Binding Assay

    Nup159 does not accelerate mantADP release from Dbp5
    Figure Legend Snippet: Nup159 does not accelerate mantADP release from Dbp5

    Techniques Used:

    Related Articles

    other:

    Article Title: Kinetic adaptation of human Myo19 for active mitochondrial transport to growing filopodia tips
    Article Snippet: The N-methylanthraniloyl (mant) derivatives of the nucleotides, 3′-mant-2′-deoxy-ATP (mT), 2′/3′-mantADP (mD) were purchased from Jena Bioscience (Jena, Germany) and their concentrations was determined by absorbance at 259 nm using ε255 of 23,300 M−1 cm−1 .

    Article Title: Nup159 weakens Gle1 binding to Dbp5 but does not accelerate ADP release
    Article Snippet: ATP (Sigma, A7699) and ADP (Sigma, 01879) concentrations were determined by absorbance using ε259 = 15,400 M−1 cm−1 . mantATP (Jena Biosciences, NU-202 and Invitrogen, ) and mantADP (Jena Biosciences, NU-201 and Invitrogen, ) concentrations were determined by absorbance using ε255 = 23,300 M−1 cm−1 .

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  • 93
    Jena Bioscience mantadp
    Determination of unlabeled nucleotide affinity in the absence of Mg 2+ by kinetic competition with <t>mantADP</t> and yield apparent affinities: K D(−Mg) = 0.8 ± 0.1 mM and K T(−Mg) = 15 ± 4 mM. Uncertainty bars represent standard errors of the fits and are contained within the data points.
    Mantadp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mantadp/product/Jena Bioscience
    Average 93 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    mantadp - by Bioz Stars, 2020-08
    93/100 stars
      Buy from Supplier

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    Determination of unlabeled nucleotide affinity in the absence of Mg 2+ by kinetic competition with mantADP and yield apparent affinities: K D(−Mg) = 0.8 ± 0.1 mM and K T(−Mg) = 15 ± 4 mM. Uncertainty bars represent standard errors of the fits and are contained within the data points.

    Journal: Journal of molecular biology

    Article Title: Nup159 weakens Gle1 binding to Dbp5 but does not accelerate ADP release

    doi: 10.1016/j.jmb.2018.05.025

    Figure Lengend Snippet: Determination of unlabeled nucleotide affinity in the absence of Mg 2+ by kinetic competition with mantADP and yield apparent affinities: K D(−Mg) = 0.8 ± 0.1 mM and K T(−Mg) = 15 ± 4 mM. Uncertainty bars represent standard errors of the fits and are contained within the data points.

    Article Snippet: ATP (Sigma, A7699) and ADP (Sigma, 01879) concentrations were determined by absorbance using ε259 = 15,400 M−1 cm−1 . mantATP (Jena Biosciences, NU-202 and Invitrogen, ) and mantADP (Jena Biosciences, NU-201 and Invitrogen, ) concentrations were determined by absorbance using ε255 = 23,300 M−1 cm−1 .

    Techniques:

    Nup159 minimally affects mantADP(±Mg 2+ ) dissociation kinetics (A) Time courses of irreversible Mg 2+ mantADP dissociation from a pre-incubated solution of Dbp5 (2 μM) and Mg 2+ mantADP (20 μM) upon mixing with 3 mM Mg 2+ ADP and (from lower to upper) 0, 1.5, 4.5, or 10 μM Nup159 in assay buffer containing excess MgCl 2 , yielding K N(+Mg)HmD of 0.3 ± 0.8 μM, k −mD(+Mg) = 2.7 ± 0.1 s −1 and k −mD(+Mg),N = 2.0 ± 0.2 s −1 . (C) Time courses of FRET signal change after mixing pre-equilibrated solutions of 1 μM Dbp5 and 40 μM mantADP with an equal volume of (lower to upper) 0, 3 or 9 μM Nup159 and 10 mM ADP in assay buffer containing excess EDTA (ca. 27 nM [Mg 2+ ] free after mixing). The concentrations are final after mixing. Continuous lines through the data represent best fits to a single exponential. (D) [Nup159]-dependence of the mantADP dissociation observed rate constants obtained from exponential fits in C. ANOVA analysis suggests that the dependence is insignificant and the average dissociation rate constant is ~ 11 s −1 indicated by a horizontal dashed line. Uncertainty bars represent standard error of the fits and are contained within the data points.

    Journal: Journal of molecular biology

    Article Title: Nup159 weakens Gle1 binding to Dbp5 but does not accelerate ADP release

    doi: 10.1016/j.jmb.2018.05.025

    Figure Lengend Snippet: Nup159 minimally affects mantADP(±Mg 2+ ) dissociation kinetics (A) Time courses of irreversible Mg 2+ mantADP dissociation from a pre-incubated solution of Dbp5 (2 μM) and Mg 2+ mantADP (20 μM) upon mixing with 3 mM Mg 2+ ADP and (from lower to upper) 0, 1.5, 4.5, or 10 μM Nup159 in assay buffer containing excess MgCl 2 , yielding K N(+Mg)HmD of 0.3 ± 0.8 μM, k −mD(+Mg) = 2.7 ± 0.1 s −1 and k −mD(+Mg),N = 2.0 ± 0.2 s −1 . (C) Time courses of FRET signal change after mixing pre-equilibrated solutions of 1 μM Dbp5 and 40 μM mantADP with an equal volume of (lower to upper) 0, 3 or 9 μM Nup159 and 10 mM ADP in assay buffer containing excess EDTA (ca. 27 nM [Mg 2+ ] free after mixing). The concentrations are final after mixing. Continuous lines through the data represent best fits to a single exponential. (D) [Nup159]-dependence of the mantADP dissociation observed rate constants obtained from exponential fits in C. ANOVA analysis suggests that the dependence is insignificant and the average dissociation rate constant is ~ 11 s −1 indicated by a horizontal dashed line. Uncertainty bars represent standard error of the fits and are contained within the data points.

    Article Snippet: ATP (Sigma, A7699) and ADP (Sigma, 01879) concentrations were determined by absorbance using ε259 = 15,400 M−1 cm−1 . mantATP (Jena Biosciences, NU-202 and Invitrogen, ) and mantADP (Jena Biosciences, NU-201 and Invitrogen, ) concentrations were determined by absorbance using ε255 = 23,300 M−1 cm−1 .

    Techniques: Incubation

    Mg 2+ slows mantADP dissociation from Dbp5 (A) Time courses of FRET signal changes in pre-equilibrated solutions of Dbp5 and mantADP with 2 mM MgCl 2 (Mg 2+ curve) or 4 mM EDTA (EDTA curve) upon rapid mixing with an equal volume of 20 mM ADP in assay buffer containing either 2 mM [MgCl 2 ] free (Mg 2+ curve) or 0 mM [MgCl 2 ] free (EDTA curve). Continuous lines through the data represent best fits to single exponentials, yielding k −mD(−Mg) = 10.0 ± 0.4 s −1 and k −mD(+Mg) = 2.4 ± 0.009 s −1 . (B) [Mg 2+ ] free dependence of the observed rate constants of mantADP dissociation from a pre-formed Dbp5-mantADP (no Mg 2+ , filled circles) or Dbp5-Mg 2+ mantADP complex (open circles). The solid and dashed lines through the data represent the best fits of the data starting with Dbp5-mantADP (filled circles) or Dbp5-Mg 2+ , yielding the two K Mg(HmD) values (160 ± 40 – filled circles and 165 ± 26 μM – open circles) for Mg 2+ binding to Dbp5-mantADP complex as well as the fundamental dissociation rate constants for mantADP (k −mD(-Mg) ≈ 10 and 9 s −1 , no Mg 2+ ) or Mg 2+ mantADP (k −mD(+Mg) ≈ 2.4 and 2.2 s −1 , saturating Mg 2+ ). Uncertainty bars represent standard errors of the fits and are contained within the data points.

    Journal: Journal of molecular biology

    Article Title: Nup159 weakens Gle1 binding to Dbp5 but does not accelerate ADP release

    doi: 10.1016/j.jmb.2018.05.025

    Figure Lengend Snippet: Mg 2+ slows mantADP dissociation from Dbp5 (A) Time courses of FRET signal changes in pre-equilibrated solutions of Dbp5 and mantADP with 2 mM MgCl 2 (Mg 2+ curve) or 4 mM EDTA (EDTA curve) upon rapid mixing with an equal volume of 20 mM ADP in assay buffer containing either 2 mM [MgCl 2 ] free (Mg 2+ curve) or 0 mM [MgCl 2 ] free (EDTA curve). Continuous lines through the data represent best fits to single exponentials, yielding k −mD(−Mg) = 10.0 ± 0.4 s −1 and k −mD(+Mg) = 2.4 ± 0.009 s −1 . (B) [Mg 2+ ] free dependence of the observed rate constants of mantADP dissociation from a pre-formed Dbp5-mantADP (no Mg 2+ , filled circles) or Dbp5-Mg 2+ mantADP complex (open circles). The solid and dashed lines through the data represent the best fits of the data starting with Dbp5-mantADP (filled circles) or Dbp5-Mg 2+ , yielding the two K Mg(HmD) values (160 ± 40 – filled circles and 165 ± 26 μM – open circles) for Mg 2+ binding to Dbp5-mantADP complex as well as the fundamental dissociation rate constants for mantADP (k −mD(-Mg) ≈ 10 and 9 s −1 , no Mg 2+ ) or Mg 2+ mantADP (k −mD(+Mg) ≈ 2.4 and 2.2 s −1 , saturating Mg 2+ ). Uncertainty bars represent standard errors of the fits and are contained within the data points.

    Article Snippet: ATP (Sigma, A7699) and ADP (Sigma, 01879) concentrations were determined by absorbance using ε259 = 15,400 M−1 cm−1 . mantATP (Jena Biosciences, NU-202 and Invitrogen, ) and mantADP (Jena Biosciences, NU-201 and Invitrogen, ) concentrations were determined by absorbance using ε255 = 23,300 M−1 cm−1 .

    Techniques: Binding Assay

    Nup159 does not accelerate mantADP release from Dbp5

    Journal: Journal of molecular biology

    Article Title: Nup159 weakens Gle1 binding to Dbp5 but does not accelerate ADP release

    doi: 10.1016/j.jmb.2018.05.025

    Figure Lengend Snippet: Nup159 does not accelerate mantADP release from Dbp5

    Article Snippet: ATP (Sigma, A7699) and ADP (Sigma, 01879) concentrations were determined by absorbance using ε259 = 15,400 M−1 cm−1 . mantATP (Jena Biosciences, NU-202 and Invitrogen, ) and mantADP (Jena Biosciences, NU-201 and Invitrogen, ) concentrations were determined by absorbance using ε255 = 23,300 M−1 cm−1 .

    Techniques: