atp  (Jena Bioscience)


Bioz Verified Symbol Jena Bioscience is a verified supplier
Bioz Manufacturer Symbol Jena Bioscience manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94
    Name:
    ATP Solution
    Description:
    Ultrapure ATP supplied as clear aqueous solution
    Catalog Number:
    nu-1010
    Price:
    34.61
    Applications:
    ATP-sensitive calcium channels[1] V-ATPases (cellular proton pumps)[2] ATP-coupled chromatin remodelling[3] ATP-binding cassette transporters[4] ATP-grasp enzymes[5] Agonistic ligand, mainly for nucleoside receptor A1 Nucleoside-triphosphates can be converted by different membrane-bound phosphatases into nucleosides acting as nucleoside receptor ligands.
    Purity:
    ≥ 99 % (HPLC)
    Category:
    Nucleotides Nucleosides
    Buy from Supplier


    Structured Review

    Jena Bioscience atp
    <t>ATP</t> dependency of ATP waiting times measured by GNP tracking and fluorescent ATP experiments. a A plot of the ATP binding rate against ATP concentrations. The ATP binding rate was fit to a straight line with a slope of 0.0038 ± 0.0001 s −1 nM −1 and an intercept of 0.17 ± 0.07 s −1 . The ATP binding rates indicated by green were calculated from the GNP tracking experiments. The ATP binding rates indicated by red were calculated from the fluorescent ATP turnover 53 , 54 . See Methods for details. Error bars indicate standard deviations. The points were obtained by the cumulative frequency plots in Supplementary Fig. 6 . Data were obtained from at least three independent experiments for each ATP concentration. b A schematic of the ATP waiting time measurement and a representative time course of the fluorescence intensity. A scattering image of GNP was used to decide the position of the myosin head. At the position, the time course of the fluorescence intensity from <t>Cy3-labeled</t> ATP (Cy3ATP) was monitored. Each spike indicates a binding event of Cy3ATP to a myosin head. The time between spikes corresponds to ATP waiting time.
    Ultrapure ATP supplied as clear aqueous solution
    https://www.bioz.com/result/atp/product/Jena Bioscience
    Average 94 stars, based on 26 article reviews
    Price from $9.99 to $1999.99
    atp - by Bioz Stars, 2020-07
    94/100 stars

    Images

    1) Product Images from "Direct visualization of human myosin II force generation using DNA origami-based thick filaments"

    Article Title: Direct visualization of human myosin II force generation using DNA origami-based thick filaments

    Journal: Communications Biology

    doi: 10.1038/s42003-019-0683-0

    ATP dependency of ATP waiting times measured by GNP tracking and fluorescent ATP experiments. a A plot of the ATP binding rate against ATP concentrations. The ATP binding rate was fit to a straight line with a slope of 0.0038 ± 0.0001 s −1 nM −1 and an intercept of 0.17 ± 0.07 s −1 . The ATP binding rates indicated by green were calculated from the GNP tracking experiments. The ATP binding rates indicated by red were calculated from the fluorescent ATP turnover 53 , 54 . See Methods for details. Error bars indicate standard deviations. The points were obtained by the cumulative frequency plots in Supplementary Fig. 6 . Data were obtained from at least three independent experiments for each ATP concentration. b A schematic of the ATP waiting time measurement and a representative time course of the fluorescence intensity. A scattering image of GNP was used to decide the position of the myosin head. At the position, the time course of the fluorescence intensity from Cy3-labeled ATP (Cy3ATP) was monitored. Each spike indicates a binding event of Cy3ATP to a myosin head. The time between spikes corresponds to ATP waiting time.
    Figure Legend Snippet: ATP dependency of ATP waiting times measured by GNP tracking and fluorescent ATP experiments. a A plot of the ATP binding rate against ATP concentrations. The ATP binding rate was fit to a straight line with a slope of 0.0038 ± 0.0001 s −1 nM −1 and an intercept of 0.17 ± 0.07 s −1 . The ATP binding rates indicated by green were calculated from the GNP tracking experiments. The ATP binding rates indicated by red were calculated from the fluorescent ATP turnover 53 , 54 . See Methods for details. Error bars indicate standard deviations. The points were obtained by the cumulative frequency plots in Supplementary Fig. 6 . Data were obtained from at least three independent experiments for each ATP concentration. b A schematic of the ATP waiting time measurement and a representative time course of the fluorescence intensity. A scattering image of GNP was used to decide the position of the myosin head. At the position, the time course of the fluorescence intensity from Cy3-labeled ATP (Cy3ATP) was monitored. Each spike indicates a binding event of Cy3ATP to a myosin head. The time between spikes corresponds to ATP waiting time.

    Techniques Used: Binding Assay, Concentration Assay, Fluorescence, Labeling

    2) Product Images from "Disruption of Heat Shock Protein 90 (Hsp90)-Protein Kinase Cδ (PKCδ) Interaction by (−)-Maackiain Suppresses Histamine H1 Receptor Gene Transcription in HeLa Cells *"

    Article Title: Disruption of Heat Shock Protein 90 (Hsp90)-Protein Kinase Cδ (PKCδ) Interaction by (−)-Maackiain Suppresses Histamine H1 Receptor Gene Transcription in HeLa Cells *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M115.657023

    (−)-Maackiain binds to Hsp90 and disrupts Hsp90-PKCδ interaction. A and B , pull-down assay. Whole cell extracts were incubated with (−)-maackiain-immobilized beads ( A ) or ATP-immobilized agarose ( B ), and Hsp90 was detected by immunoblot
    Figure Legend Snippet: (−)-Maackiain binds to Hsp90 and disrupts Hsp90-PKCδ interaction. A and B , pull-down assay. Whole cell extracts were incubated with (−)-maackiain-immobilized beads ( A ) or ATP-immobilized agarose ( B ), and Hsp90 was detected by immunoblot

    Techniques Used: Pull Down Assay, Incubation

    3) Product Images from "AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase"

    Article Title: AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase

    Journal: Retrovirology

    doi: 10.1186/s12977-015-0147-7

    HSQC spectra of RTshort-WT, RTshort- mt4 and RTshort- mt4 -T345S . Overlays of 1 H/ 15 N-HSQC spectra of RTshort proteins in the absence of ATP (black) and in the presence of 21 mM ATP (red) in binding buffer with 10% D 2 O at a sample temperature of 298 K. (A) black: 460 μM RTshort-WT without ATP; red: 363 μM RTshort-WT with a 58 fold ATP excess. (B) black: 550 μM RTshort- mt4 without ATP; red: 434 μM RTshort with a 48 fold ATP excess. (C) black: RTshort- mt4 -T345S without ATP; red: 355 μM RTshort- mt4 -T345S with a 59 fold ATP excess
    Figure Legend Snippet: HSQC spectra of RTshort-WT, RTshort- mt4 and RTshort- mt4 -T345S . Overlays of 1 H/ 15 N-HSQC spectra of RTshort proteins in the absence of ATP (black) and in the presence of 21 mM ATP (red) in binding buffer with 10% D 2 O at a sample temperature of 298 K. (A) black: 460 μM RTshort-WT without ATP; red: 363 μM RTshort-WT with a 58 fold ATP excess. (B) black: 550 μM RTshort- mt4 without ATP; red: 434 μM RTshort with a 48 fold ATP excess. (C) black: RTshort- mt4 -T345S without ATP; red: 355 μM RTshort- mt4 -T345S with a 59 fold ATP excess

    Techniques Used: Binding Assay

    Titration of RTshort- mt4 with ATP . (A) Overlay of TROSY- 1 H/ 15 N-HSQC spectra of 205 μM RTshort- mt4 recorded at a sample temperature of 288 K during the titration with different ATP/protein ratios. Key: black: 0; red: 15; green: 48; cyan: 92; blue: 142; pink: 195. Blow-ups of the framed areas (a) and (b ) are shown underneath the spectra and represent examples of significant chemical shift changes with RTshort- mt4 and ATP. (B) Determination of the mean K D -value for ATP with RTshort- mt4 . Seven fits for normalized chemical shift changes of seven shifting residues encircled in (A) were used to calculate the mean K D -value with standard deviation. Exemplified, fitted curves for three signal changes depicted in boxes (a) and (b) are shown as a function of the [ATP]/[RTshort- mt4 ] ratio.
    Figure Legend Snippet: Titration of RTshort- mt4 with ATP . (A) Overlay of TROSY- 1 H/ 15 N-HSQC spectra of 205 μM RTshort- mt4 recorded at a sample temperature of 288 K during the titration with different ATP/protein ratios. Key: black: 0; red: 15; green: 48; cyan: 92; blue: 142; pink: 195. Blow-ups of the framed areas (a) and (b ) are shown underneath the spectra and represent examples of significant chemical shift changes with RTshort- mt4 and ATP. (B) Determination of the mean K D -value for ATP with RTshort- mt4 . Seven fits for normalized chemical shift changes of seven shifting residues encircled in (A) were used to calculate the mean K D -value with standard deviation. Exemplified, fitted curves for three signal changes depicted in boxes (a) and (b) are shown as a function of the [ATP]/[RTshort- mt4 ] ratio.

    Techniques Used: Titration, Standard Deviation

    4) Product Images from "Direct visualization of human myosin II force generation using DNA origami-based thick filaments"

    Article Title: Direct visualization of human myosin II force generation using DNA origami-based thick filaments

    Journal: Communications Biology

    doi: 10.1038/s42003-019-0683-0

    ATP dependency of ATP waiting times measured by GNP tracking and fluorescent ATP experiments. a A plot of the ATP binding rate against ATP concentrations. The ATP binding rate was fit to a straight line with a slope of 0.0038 ± 0.0001 s −1 nM −1 and an intercept of 0.17 ± 0.07 s −1 . The ATP binding rates indicated by green were calculated from the GNP tracking experiments. The ATP binding rates indicated by red were calculated from the fluorescent ATP turnover 53 , 54 . See Methods for details. Error bars indicate standard deviations. The points were obtained by the cumulative frequency plots in Supplementary Fig. 6 . Data were obtained from at least three independent experiments for each ATP concentration. b A schematic of the ATP waiting time measurement and a representative time course of the fluorescence intensity. A scattering image of GNP was used to decide the position of the myosin head. At the position, the time course of the fluorescence intensity from Cy3-labeled ATP (Cy3ATP) was monitored. Each spike indicates a binding event of Cy3ATP to a myosin head. The time between spikes corresponds to ATP waiting time.
    Figure Legend Snippet: ATP dependency of ATP waiting times measured by GNP tracking and fluorescent ATP experiments. a A plot of the ATP binding rate against ATP concentrations. The ATP binding rate was fit to a straight line with a slope of 0.0038 ± 0.0001 s −1 nM −1 and an intercept of 0.17 ± 0.07 s −1 . The ATP binding rates indicated by green were calculated from the GNP tracking experiments. The ATP binding rates indicated by red were calculated from the fluorescent ATP turnover 53 , 54 . See Methods for details. Error bars indicate standard deviations. The points were obtained by the cumulative frequency plots in Supplementary Fig. 6 . Data were obtained from at least three independent experiments for each ATP concentration. b A schematic of the ATP waiting time measurement and a representative time course of the fluorescence intensity. A scattering image of GNP was used to decide the position of the myosin head. At the position, the time course of the fluorescence intensity from Cy3-labeled ATP (Cy3ATP) was monitored. Each spike indicates a binding event of Cy3ATP to a myosin head. The time between spikes corresponds to ATP waiting time.

    Techniques Used: Binding Assay, Concentration Assay, Fluorescence, Labeling

    5) Product Images from "Biochemical characterization of a multi-drug resistant HIV-1 subtype AG reverse transcriptase: antagonism of AZT discrimination and excision pathways and sensitivity to RNase H inhibitors"

    Article Title: Biochemical characterization of a multi-drug resistant HIV-1 subtype AG reverse transcriptase: antagonism of AZT discrimination and excision pathways and sensitivity to RNase H inhibitors

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkw060

    AZTMP excision. AZTMP excision reactions with the CRF02_AG WT and MR RTs were performed with 20 nM of a 5′ [ 32 P] end-labeled and AZTMP terminated [ 32 P]-P 30-AZTMP /T 50 substrate in the presence of 5 mM ATP, 0.01 U/μl of pyrophosphatase and 600 nM RT as indicated. Reactions were started by RT addition and stopped after 5 min at 37°C. After separation of the reaction products and educt by denaturing gel electrophoresis, the bands were quantified densitometrically. The total amount of AZTMP-terminated primer per lane was set to 100% to calculate the percentage of excised AZTMP. Each diagram depicts the mean values and standard deviations (black bars) of three independent experiments. P -values ≤ 0.05 represent statistically significant differences to the WT protein (*** P -value ≤ 0.001).
    Figure Legend Snippet: AZTMP excision. AZTMP excision reactions with the CRF02_AG WT and MR RTs were performed with 20 nM of a 5′ [ 32 P] end-labeled and AZTMP terminated [ 32 P]-P 30-AZTMP /T 50 substrate in the presence of 5 mM ATP, 0.01 U/μl of pyrophosphatase and 600 nM RT as indicated. Reactions were started by RT addition and stopped after 5 min at 37°C. After separation of the reaction products and educt by denaturing gel electrophoresis, the bands were quantified densitometrically. The total amount of AZTMP-terminated primer per lane was set to 100% to calculate the percentage of excised AZTMP. Each diagram depicts the mean values and standard deviations (black bars) of three independent experiments. P -values ≤ 0.05 represent statistically significant differences to the WT protein (*** P -value ≤ 0.001).

    Techniques Used: Labeling, Nucleic Acid Electrophoresis

    6) Product Images from "AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase"

    Article Title: AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase

    Journal: Retrovirology

    doi: 10.1186/s12977-015-0147-7

    Polymerization activity and AZT resistance of SFVmac PR-RT variants. (A) . SFVmac PR-RT variants used in this study harboring one to four of the relevant resistance substitutions are highlighted by red rectangles. (B) Polymerization initiation . Initiation of polymerization was checked with 20 nM 5′ 32 P-P 30 /T 50 substrate, 250 μM dNTPs and 10 nM enzyme at 37°C for 10 min. The PR-RTs used are indicated on top of the gel. WT, wild type; Control, sample without enzyme. (C) AZTMP removal in the presence of ATP. 5 nM of an AZTMP-terminated and 5′ 32 P-labeled substrate P 30-AZTMP /T 50, 0.02 U of pyrophosphatase and 5 mM ATP were preincubated for 5 min. Reactions were started by the addition of 320 nM enzyme as indicated on top and stopped after 20 min. Reaction products were separated on 10% sequencing gels and visualized by phosphoimaging. P 30-AZT, AZTMP terminated primer; P 30, unblocked primer.
    Figure Legend Snippet: Polymerization activity and AZT resistance of SFVmac PR-RT variants. (A) . SFVmac PR-RT variants used in this study harboring one to four of the relevant resistance substitutions are highlighted by red rectangles. (B) Polymerization initiation . Initiation of polymerization was checked with 20 nM 5′ 32 P-P 30 /T 50 substrate, 250 μM dNTPs and 10 nM enzyme at 37°C for 10 min. The PR-RTs used are indicated on top of the gel. WT, wild type; Control, sample without enzyme. (C) AZTMP removal in the presence of ATP. 5 nM of an AZTMP-terminated and 5′ 32 P-labeled substrate P 30-AZTMP /T 50, 0.02 U of pyrophosphatase and 5 mM ATP were preincubated for 5 min. Reactions were started by the addition of 320 nM enzyme as indicated on top and stopped after 20 min. Reaction products were separated on 10% sequencing gels and visualized by phosphoimaging. P 30-AZT, AZTMP terminated primer; P 30, unblocked primer.

    Techniques Used: Activity Assay, Labeling, Sequencing

    Related Articles

    In Vitro:

    Article Title: A small molecular inhibitor of LRRK1 identified by homology modeling and virtual screening suppresses osteoclast function, but not osteoclast differentiation, in vitro
    Article Snippet: .. In vitro inhibition of ATP binding assay IN04 inhibition of ATP binding to hLRRK1 KD was assessed by a pulldown assay with ATP-agarose according to the manufacturer's instructions (ATP Affpur kit III, Jena Bioscience, Jena, Germany). .. Briefly, 50 ng recombinant hLRRK1 KD was first incubated with various concentrations of IN04 inhibitor (3.2 nM, 16, nM, 80 nM, 0.4 μM, and 5.0 μM) or the same volume of DMSO in 500 μl of 1x binding buffer on ice for 15 minutes.

    Labeling:

    Article Title: AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase
    Article Snippet: .. ATP binding experiments 2D [1 H-15 N] HSQC experiments were recorded in the absence and presence of ATP (21 mM) (Jena Bioscience, Jena, Germany) with RTshort-WT, RTshort-mt4 and RTshort-mt4 -T345S in binding buffer [50 mM Tris/HCl pH 6.725°C , 150 mM NaCl, 6 mM MgCl2 , 0.5 mM DTT] with 10% (v/v) D2 O at 298 K. To determine the KD -value for ATP of RTshort-mt4, transverse relaxation-optimized spectroscopy (TROSY) 1 H/15 N-HSQC experiments [ , ] were done with 205 μM of deuterated and 15 N labeled 2 H/15 N RTshort-mt4 in binding buffer. .. 1 H back-exchange of amide protons was achieved by overnight dialysis of the protein against binding buffer at 4°C.

    Inhibition:

    Article Title: A small molecular inhibitor of LRRK1 identified by homology modeling and virtual screening suppresses osteoclast function, but not osteoclast differentiation, in vitro
    Article Snippet: .. In vitro inhibition of ATP binding assay IN04 inhibition of ATP binding to hLRRK1 KD was assessed by a pulldown assay with ATP-agarose according to the manufacturer's instructions (ATP Affpur kit III, Jena Bioscience, Jena, Germany). .. Briefly, 50 ng recombinant hLRRK1 KD was first incubated with various concentrations of IN04 inhibitor (3.2 nM, 16, nM, 80 nM, 0.4 μM, and 5.0 μM) or the same volume of DMSO in 500 μl of 1x binding buffer on ice for 15 minutes.

    Imaging:

    Article Title: Direct visualization of human myosin II force generation using DNA origami-based thick filaments
    Article Snippet: .. In the fluorescent ATP experiments, Cy3-labeled 2′/3′-O-(2-aminoethyl-carbamoyl)-adenosine-5′-triphosphate (Jena Bioscience) was added to the imaging buffer instead of ATP. .. Objective-type evanescent field darkfield microscopy GNP imaging was performed with a MicroMirror TIRF system (Mad City Labs) , .

    Spectroscopy:

    Article Title: AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase
    Article Snippet: .. ATP binding experiments 2D [1 H-15 N] HSQC experiments were recorded in the absence and presence of ATP (21 mM) (Jena Bioscience, Jena, Germany) with RTshort-WT, RTshort-mt4 and RTshort-mt4 -T345S in binding buffer [50 mM Tris/HCl pH 6.725°C , 150 mM NaCl, 6 mM MgCl2 , 0.5 mM DTT] with 10% (v/v) D2 O at 298 K. To determine the KD -value for ATP of RTshort-mt4, transverse relaxation-optimized spectroscopy (TROSY) 1 H/15 N-HSQC experiments [ , ] were done with 205 μM of deuterated and 15 N labeled 2 H/15 N RTshort-mt4 in binding buffer. .. 1 H back-exchange of amide protons was achieved by overnight dialysis of the protein against binding buffer at 4°C.

    Binding Assay:

    Article Title: Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator
    Article Snippet: .. Measurement of Kti12 nucleotide binding affinity Parameters of nucleotide binding by CtKti12 were dissected using MANT-labeled (2′/3′-O-(N-Methyl-anthraniloyl), Jena Bioscience) ATP or its non-hydrolysable analog, AMPPNP (adenosine-5′-[(β,γ)-imido] triphosphate). ..

    Article Title: A small molecular inhibitor of LRRK1 identified by homology modeling and virtual screening suppresses osteoclast function, but not osteoclast differentiation, in vitro
    Article Snippet: .. In vitro inhibition of ATP binding assay IN04 inhibition of ATP binding to hLRRK1 KD was assessed by a pulldown assay with ATP-agarose according to the manufacturer's instructions (ATP Affpur kit III, Jena Bioscience, Jena, Germany). .. Briefly, 50 ng recombinant hLRRK1 KD was first incubated with various concentrations of IN04 inhibitor (3.2 nM, 16, nM, 80 nM, 0.4 μM, and 5.0 μM) or the same volume of DMSO in 500 μl of 1x binding buffer on ice for 15 minutes.

    Article Title: AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase
    Article Snippet: .. ATP binding experiments 2D [1 H-15 N] HSQC experiments were recorded in the absence and presence of ATP (21 mM) (Jena Bioscience, Jena, Germany) with RTshort-WT, RTshort-mt4 and RTshort-mt4 -T345S in binding buffer [50 mM Tris/HCl pH 6.725°C , 150 mM NaCl, 6 mM MgCl2 , 0.5 mM DTT] with 10% (v/v) D2 O at 298 K. To determine the KD -value for ATP of RTshort-mt4, transverse relaxation-optimized spectroscopy (TROSY) 1 H/15 N-HSQC experiments [ , ] were done with 205 μM of deuterated and 15 N labeled 2 H/15 N RTshort-mt4 in binding buffer. .. 1 H back-exchange of amide protons was achieved by overnight dialysis of the protein against binding buffer at 4°C.

    Article Title: Disruption of Heat Shock Protein 90 (Hsp90)-Protein Kinase Cδ (PKCδ) Interaction by (−)-Maackiain Suppresses Histamine H1 Receptor Gene Transcription in HeLa Cells *
    Article Snippet: .. For the maackiain competition assay, the extracts were preincubated on ice with 1 m m (−)-maackiain for 30 min. To assess the effect of (−)-maackiain on ATP binding by Hsp90, γ-aminophenyl ATP-immobilized agarose (Jena Bioscience, Jena, Germany) was used. ..

    Competitive Binding Assay:

    Article Title: Disruption of Heat Shock Protein 90 (Hsp90)-Protein Kinase Cδ (PKCδ) Interaction by (−)-Maackiain Suppresses Histamine H1 Receptor Gene Transcription in HeLa Cells *
    Article Snippet: .. For the maackiain competition assay, the extracts were preincubated on ice with 1 m m (−)-maackiain for 30 min. To assess the effect of (−)-maackiain on ATP binding by Hsp90, γ-aminophenyl ATP-immobilized agarose (Jena Bioscience, Jena, Germany) was used. ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94
    Jena Bioscience atp
    <t>ATP</t> dependency of ATP waiting times measured by GNP tracking and fluorescent ATP experiments. a A plot of the ATP binding rate against ATP concentrations. The ATP binding rate was fit to a straight line with a slope of 0.0038 ± 0.0001 s −1 nM −1 and an intercept of 0.17 ± 0.07 s −1 . The ATP binding rates indicated by green were calculated from the GNP tracking experiments. The ATP binding rates indicated by red were calculated from the fluorescent ATP turnover 53 , 54 . See Methods for details. Error bars indicate standard deviations. The points were obtained by the cumulative frequency plots in Supplementary Fig. 6 . Data were obtained from at least three independent experiments for each ATP concentration. b A schematic of the ATP waiting time measurement and a representative time course of the fluorescence intensity. A scattering image of GNP was used to decide the position of the myosin head. At the position, the time course of the fluorescence intensity from <t>Cy3-labeled</t> ATP (Cy3ATP) was monitored. Each spike indicates a binding event of Cy3ATP to a myosin head. The time between spikes corresponds to ATP waiting time.
    Atp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/atp/product/Jena Bioscience
    Average 94 stars, based on 20 article reviews
    Price from $9.99 to $1999.99
    atp - by Bioz Stars, 2020-07
    94/100 stars
      Buy from Supplier

    Image Search Results


    ATP dependency of ATP waiting times measured by GNP tracking and fluorescent ATP experiments. a A plot of the ATP binding rate against ATP concentrations. The ATP binding rate was fit to a straight line with a slope of 0.0038 ± 0.0001 s −1 nM −1 and an intercept of 0.17 ± 0.07 s −1 . The ATP binding rates indicated by green were calculated from the GNP tracking experiments. The ATP binding rates indicated by red were calculated from the fluorescent ATP turnover 53 , 54 . See Methods for details. Error bars indicate standard deviations. The points were obtained by the cumulative frequency plots in Supplementary Fig. 6 . Data were obtained from at least three independent experiments for each ATP concentration. b A schematic of the ATP waiting time measurement and a representative time course of the fluorescence intensity. A scattering image of GNP was used to decide the position of the myosin head. At the position, the time course of the fluorescence intensity from Cy3-labeled ATP (Cy3ATP) was monitored. Each spike indicates a binding event of Cy3ATP to a myosin head. The time between spikes corresponds to ATP waiting time.

    Journal: Communications Biology

    Article Title: Direct visualization of human myosin II force generation using DNA origami-based thick filaments

    doi: 10.1038/s42003-019-0683-0

    Figure Lengend Snippet: ATP dependency of ATP waiting times measured by GNP tracking and fluorescent ATP experiments. a A plot of the ATP binding rate against ATP concentrations. The ATP binding rate was fit to a straight line with a slope of 0.0038 ± 0.0001 s −1 nM −1 and an intercept of 0.17 ± 0.07 s −1 . The ATP binding rates indicated by green were calculated from the GNP tracking experiments. The ATP binding rates indicated by red were calculated from the fluorescent ATP turnover 53 , 54 . See Methods for details. Error bars indicate standard deviations. The points were obtained by the cumulative frequency plots in Supplementary Fig. 6 . Data were obtained from at least three independent experiments for each ATP concentration. b A schematic of the ATP waiting time measurement and a representative time course of the fluorescence intensity. A scattering image of GNP was used to decide the position of the myosin head. At the position, the time course of the fluorescence intensity from Cy3-labeled ATP (Cy3ATP) was monitored. Each spike indicates a binding event of Cy3ATP to a myosin head. The time between spikes corresponds to ATP waiting time.

    Article Snippet: In the fluorescent ATP experiments, Cy3-labeled 2′/3′-O-(2-aminoethyl-carbamoyl)-adenosine-5′-triphosphate (Jena Bioscience) was added to the imaging buffer instead of ATP.

    Techniques: Binding Assay, Concentration Assay, Fluorescence, Labeling

    (−)-Maackiain binds to Hsp90 and disrupts Hsp90-PKCδ interaction. A and B , pull-down assay. Whole cell extracts were incubated with (−)-maackiain-immobilized beads ( A ) or ATP-immobilized agarose ( B ), and Hsp90 was detected by immunoblot

    Journal: The Journal of Biological Chemistry

    Article Title: Disruption of Heat Shock Protein 90 (Hsp90)-Protein Kinase Cδ (PKCδ) Interaction by (−)-Maackiain Suppresses Histamine H1 Receptor Gene Transcription in HeLa Cells *

    doi: 10.1074/jbc.M115.657023

    Figure Lengend Snippet: (−)-Maackiain binds to Hsp90 and disrupts Hsp90-PKCδ interaction. A and B , pull-down assay. Whole cell extracts were incubated with (−)-maackiain-immobilized beads ( A ) or ATP-immobilized agarose ( B ), and Hsp90 was detected by immunoblot

    Article Snippet: For the maackiain competition assay, the extracts were preincubated on ice with 1 m m (−)-maackiain for 30 min. To assess the effect of (−)-maackiain on ATP binding by Hsp90, γ-aminophenyl ATP-immobilized agarose (Jena Bioscience, Jena, Germany) was used.

    Techniques: Pull Down Assay, Incubation

    HSQC spectra of RTshort-WT, RTshort- mt4 and RTshort- mt4 -T345S . Overlays of 1 H/ 15 N-HSQC spectra of RTshort proteins in the absence of ATP (black) and in the presence of 21 mM ATP (red) in binding buffer with 10% D 2 O at a sample temperature of 298 K. (A) black: 460 μM RTshort-WT without ATP; red: 363 μM RTshort-WT with a 58 fold ATP excess. (B) black: 550 μM RTshort- mt4 without ATP; red: 434 μM RTshort with a 48 fold ATP excess. (C) black: RTshort- mt4 -T345S without ATP; red: 355 μM RTshort- mt4 -T345S with a 59 fold ATP excess

    Journal: Retrovirology

    Article Title: AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase

    doi: 10.1186/s12977-015-0147-7

    Figure Lengend Snippet: HSQC spectra of RTshort-WT, RTshort- mt4 and RTshort- mt4 -T345S . Overlays of 1 H/ 15 N-HSQC spectra of RTshort proteins in the absence of ATP (black) and in the presence of 21 mM ATP (red) in binding buffer with 10% D 2 O at a sample temperature of 298 K. (A) black: 460 μM RTshort-WT without ATP; red: 363 μM RTshort-WT with a 58 fold ATP excess. (B) black: 550 μM RTshort- mt4 without ATP; red: 434 μM RTshort with a 48 fold ATP excess. (C) black: RTshort- mt4 -T345S without ATP; red: 355 μM RTshort- mt4 -T345S with a 59 fold ATP excess

    Article Snippet: ATP binding experiments 2D [1 H-15 N] HSQC experiments were recorded in the absence and presence of ATP (21 mM) (Jena Bioscience, Jena, Germany) with RTshort-WT, RTshort-mt4 and RTshort-mt4 -T345S in binding buffer [50 mM Tris/HCl pH 6.725°C , 150 mM NaCl, 6 mM MgCl2 , 0.5 mM DTT] with 10% (v/v) D2 O at 298 K. To determine the KD -value for ATP of RTshort-mt4, transverse relaxation-optimized spectroscopy (TROSY) 1 H/15 N-HSQC experiments [ , ] were done with 205 μM of deuterated and 15 N labeled 2 H/15 N RTshort-mt4 in binding buffer.

    Techniques: Binding Assay

    Titration of RTshort- mt4 with ATP . (A) Overlay of TROSY- 1 H/ 15 N-HSQC spectra of 205 μM RTshort- mt4 recorded at a sample temperature of 288 K during the titration with different ATP/protein ratios. Key: black: 0; red: 15; green: 48; cyan: 92; blue: 142; pink: 195. Blow-ups of the framed areas (a) and (b ) are shown underneath the spectra and represent examples of significant chemical shift changes with RTshort- mt4 and ATP. (B) Determination of the mean K D -value for ATP with RTshort- mt4 . Seven fits for normalized chemical shift changes of seven shifting residues encircled in (A) were used to calculate the mean K D -value with standard deviation. Exemplified, fitted curves for three signal changes depicted in boxes (a) and (b) are shown as a function of the [ATP]/[RTshort- mt4 ] ratio.

    Journal: Retrovirology

    Article Title: AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase

    doi: 10.1186/s12977-015-0147-7

    Figure Lengend Snippet: Titration of RTshort- mt4 with ATP . (A) Overlay of TROSY- 1 H/ 15 N-HSQC spectra of 205 μM RTshort- mt4 recorded at a sample temperature of 288 K during the titration with different ATP/protein ratios. Key: black: 0; red: 15; green: 48; cyan: 92; blue: 142; pink: 195. Blow-ups of the framed areas (a) and (b ) are shown underneath the spectra and represent examples of significant chemical shift changes with RTshort- mt4 and ATP. (B) Determination of the mean K D -value for ATP with RTshort- mt4 . Seven fits for normalized chemical shift changes of seven shifting residues encircled in (A) were used to calculate the mean K D -value with standard deviation. Exemplified, fitted curves for three signal changes depicted in boxes (a) and (b) are shown as a function of the [ATP]/[RTshort- mt4 ] ratio.

    Article Snippet: ATP binding experiments 2D [1 H-15 N] HSQC experiments were recorded in the absence and presence of ATP (21 mM) (Jena Bioscience, Jena, Germany) with RTshort-WT, RTshort-mt4 and RTshort-mt4 -T345S in binding buffer [50 mM Tris/HCl pH 6.725°C , 150 mM NaCl, 6 mM MgCl2 , 0.5 mM DTT] with 10% (v/v) D2 O at 298 K. To determine the KD -value for ATP of RTshort-mt4, transverse relaxation-optimized spectroscopy (TROSY) 1 H/15 N-HSQC experiments [ , ] were done with 205 μM of deuterated and 15 N labeled 2 H/15 N RTshort-mt4 in binding buffer.

    Techniques: Titration, Standard Deviation