mgcl2  (Millipore)


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    Magnesium chloride
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    Structured Review

    Millipore mgcl2
    Magnesium chloride

    https://www.bioz.com/result/mgcl2/product/Millipore
    Average 99 stars, based on 1204 article reviews
    Price from $9.99 to $1999.99
    mgcl2 - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins"

    Article Title: PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins

    Journal: eLife

    doi: 10.7554/eLife.50416

    PPM1H dephosphorylates Rab10 in vitro. ( A ) The indicated amounts of recombinant wild-type and mutant PPM1H (with a His-Sumo N-terminal tag, expressed in E. coli ) were incubated in vitro with 2.5 µg pT73 ~60% phosphorylated Rab10[1–181, GDP bound] for 30 min in the presence of 10 mM MgCl2 in 40 mM HEPES pH 7.0 buffer. Reactions were terminated by addition of SDS Sample Buffer and analyzed by phos-tag gel electrophoresis that separates phosphorylated and dephosphorylated Rab10. Gel was stained with Instant Blue Coomassie. Bands corresponding to phosphorylated and non-phosphorylated Rab10 are marked with open (○) and closed (●) circles respectively. ( B ) As in ( A ) except that a time-course assay was performed using 2.5 µg pT73 phosphorylated Rab10[1–181, GDP bound] and 40 ng wild-type or mutant PPM1H for the indicated times. ( C ) As in ( A ) except that PPM1J was assessed. ( D ) As in ( A ) except and PPM1M was assessed.
    Figure Legend Snippet: PPM1H dephosphorylates Rab10 in vitro. ( A ) The indicated amounts of recombinant wild-type and mutant PPM1H (with a His-Sumo N-terminal tag, expressed in E. coli ) were incubated in vitro with 2.5 µg pT73 ~60% phosphorylated Rab10[1–181, GDP bound] for 30 min in the presence of 10 mM MgCl2 in 40 mM HEPES pH 7.0 buffer. Reactions were terminated by addition of SDS Sample Buffer and analyzed by phos-tag gel electrophoresis that separates phosphorylated and dephosphorylated Rab10. Gel was stained with Instant Blue Coomassie. Bands corresponding to phosphorylated and non-phosphorylated Rab10 are marked with open (○) and closed (●) circles respectively. ( B ) As in ( A ) except that a time-course assay was performed using 2.5 µg pT73 phosphorylated Rab10[1–181, GDP bound] and 40 ng wild-type or mutant PPM1H for the indicated times. ( C ) As in ( A ) except that PPM1J was assessed. ( D ) As in ( A ) except and PPM1M was assessed.

    Techniques Used: In Vitro, Recombinant, Mutagenesis, Incubation, Nucleic Acid Electrophoresis, Staining

    2) Product Images from "Colloidal stability as a determinant of nanoparticle behavior in the brain"

    Article Title: Colloidal stability as a determinant of nanoparticle behavior in the brain

    Journal: Colloids and surfaces. B, Biointerfaces

    doi: 10.1016/j.colsurfb.2018.06.050

    Physicochemical characterization of 100 nm PS nanoparticles in calcium solutions. (a) Hydrodynamic diameters of PS-COOH and PS-PEG nanoparticles in varying concentrations of aqueous calcium chloride solutions as measured by DLS (n = 3). (b) Hydrodynamic diameters of PS-COOH and PS-PEG nanoparticles in varying concentrations of magnesium chloride solutions as measured by DLS (n = 3). All values are reported as mean ± SEM. Significance as compared with 0 mM condition are indicated by * p
    Figure Legend Snippet: Physicochemical characterization of 100 nm PS nanoparticles in calcium solutions. (a) Hydrodynamic diameters of PS-COOH and PS-PEG nanoparticles in varying concentrations of aqueous calcium chloride solutions as measured by DLS (n = 3). (b) Hydrodynamic diameters of PS-COOH and PS-PEG nanoparticles in varying concentrations of magnesium chloride solutions as measured by DLS (n = 3). All values are reported as mean ± SEM. Significance as compared with 0 mM condition are indicated by * p

    Techniques Used:

    3) Product Images from "Functional Analysis of an Acid Adaptive DNA Adenine Methyltransferase from Helicobacter pylori 26695"

    Article Title: Functional Analysis of an Acid Adaptive DNA Adenine Methyltransferase from Helicobacter pylori 26695

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0016810

    Effect of divalent metal ions on methylation activity of HP0593 MTase. A . Histogram showing methylation activity of 250 nM HP0593 MTase in the absence of any metal ions (-Me 2+ ) and in the presence of cobalt chloride (Co 2+ ), magnesium chloride (Mg 2+ ), manganese chloride (Mn 2+ ), calcium chloride (Ca 2+ ), zinc chloride (Zn 2+ ), and nickel chloride (Ni 2+ ). 1 = 0.4 mM, 2 = 0.5 mM, 3 = 1.0 mM, and 4 = 5.0 mM. Kinetics of DNA binding. HP0593 MTase was injected for 120 sec over streptavidin chip containing immobilized duplex 18 DNA at a flow rate of 20 µl/min followed by dissociation phase of 120 sec. The global fit of the data was used to calculate the binding constants.  B.  SPR sensorgram displaying the response of increasing HP0593 MTase concentrations (25–100 nM) in presence of 1.0 mM MnCl 2 . ( Inset ) kinetic constants.  C.  SPR sensorgram displaying the response of increasing HP0593 MTase concentrations (100–200 nM) in absence of metal. ( Inset ) kinetic constants.
    Figure Legend Snippet: Effect of divalent metal ions on methylation activity of HP0593 MTase. A . Histogram showing methylation activity of 250 nM HP0593 MTase in the absence of any metal ions (-Me 2+ ) and in the presence of cobalt chloride (Co 2+ ), magnesium chloride (Mg 2+ ), manganese chloride (Mn 2+ ), calcium chloride (Ca 2+ ), zinc chloride (Zn 2+ ), and nickel chloride (Ni 2+ ). 1 = 0.4 mM, 2 = 0.5 mM, 3 = 1.0 mM, and 4 = 5.0 mM. Kinetics of DNA binding. HP0593 MTase was injected for 120 sec over streptavidin chip containing immobilized duplex 18 DNA at a flow rate of 20 µl/min followed by dissociation phase of 120 sec. The global fit of the data was used to calculate the binding constants. B. SPR sensorgram displaying the response of increasing HP0593 MTase concentrations (25–100 nM) in presence of 1.0 mM MnCl 2 . ( Inset ) kinetic constants. C. SPR sensorgram displaying the response of increasing HP0593 MTase concentrations (100–200 nM) in absence of metal. ( Inset ) kinetic constants.

    Techniques Used: Methylation, Activity Assay, Binding Assay, Injection, Size-exclusion Chromatography, Chromatin Immunoprecipitation, Flow Cytometry, SPR Assay

    4) Product Images from "RNA Mimicry by the Fap7 Adenylate Kinase in Ribosome Biogenesis"

    Article Title: RNA Mimicry by the Fap7 Adenylate Kinase in Ribosome Biogenesis

    Journal: PLoS Biology

    doi: 10.1371/journal.pbio.1001860

    Fap7 ATPase activity regulates its association with Rsp14. Interaction between yFap7 and GST-Rps14 was tested by pulldown experiments. (A) Interaction of yFap7 with GST-Rps14 was tested by addition of 800 pmoles of yFap7 on GST-yRps14 beads resuspended in 1 ml of IP buffer. Effect of addition of ATP, ADP, or AMP-PNP at 1 mM final concentration in the presence of MgCl2 (5 mM) was tested. Protein associated with the beads was analyzed by Coomassie staining. For input controls, 10% of Fap7 (80 pmoles) and the same quantity of Rps14 beads used for the IP were loaded. (B) Effects of magnesium and nucleotide concentration were tested by using the same strategy in the presence of RNA (cf., D). Two quantities of nucleotides were used: 1 µmole (1 mM) or 10 nmole (10 µM). Experiments were done in the presence or in the absence of 5 mM MgCl 2 . (C) Association of GST-yRps14 to RNA was assessed by a competition experiment using a different ratio between RNA and yFap7: 800 pmole Fap7 with 800 pmole RNA (1∶1), 400 pmole Fap7 with 800 pmole RNA (1∶2), and 200 pmole Fap7 with 800 pmole RNA (1∶4). Nucleotides were added at 1 mM final. Protein associated with the beads was analyzed by Coomassie staining. For input controls, 10% of Fap7 (80 pmoles) and the same quantity of Rps14 beads used for the IP were loaded. (D) Same as in C, but this time the RNA counterpart was followed on Urea-acrylamide gel after SYBR Safe staining. For input control, 80 pmole of RNA was loaded. (E) ATPase activity of yFap7 (black points) was followed by a coupled enzyme assay. Effect of addition after 10 min of MBP-yRps14 (black line), buffer (dotted dark line), or Prp43 (dotted dark grey line) was also monitored. In parallel, ATPase activity of MBP-yRps14 (light grey line) alone and the preformed complex yFap7–yRps14 (dark grey line) was also tested.
    Figure Legend Snippet: Fap7 ATPase activity regulates its association with Rsp14. Interaction between yFap7 and GST-Rps14 was tested by pulldown experiments. (A) Interaction of yFap7 with GST-Rps14 was tested by addition of 800 pmoles of yFap7 on GST-yRps14 beads resuspended in 1 ml of IP buffer. Effect of addition of ATP, ADP, or AMP-PNP at 1 mM final concentration in the presence of MgCl2 (5 mM) was tested. Protein associated with the beads was analyzed by Coomassie staining. For input controls, 10% of Fap7 (80 pmoles) and the same quantity of Rps14 beads used for the IP were loaded. (B) Effects of magnesium and nucleotide concentration were tested by using the same strategy in the presence of RNA (cf., D). Two quantities of nucleotides were used: 1 µmole (1 mM) or 10 nmole (10 µM). Experiments were done in the presence or in the absence of 5 mM MgCl 2 . (C) Association of GST-yRps14 to RNA was assessed by a competition experiment using a different ratio between RNA and yFap7: 800 pmole Fap7 with 800 pmole RNA (1∶1), 400 pmole Fap7 with 800 pmole RNA (1∶2), and 200 pmole Fap7 with 800 pmole RNA (1∶4). Nucleotides were added at 1 mM final. Protein associated with the beads was analyzed by Coomassie staining. For input controls, 10% of Fap7 (80 pmoles) and the same quantity of Rps14 beads used for the IP were loaded. (D) Same as in C, but this time the RNA counterpart was followed on Urea-acrylamide gel after SYBR Safe staining. For input control, 80 pmole of RNA was loaded. (E) ATPase activity of yFap7 (black points) was followed by a coupled enzyme assay. Effect of addition after 10 min of MBP-yRps14 (black line), buffer (dotted dark line), or Prp43 (dotted dark grey line) was also monitored. In parallel, ATPase activity of MBP-yRps14 (light grey line) alone and the preformed complex yFap7–yRps14 (dark grey line) was also tested.

    Techniques Used: Activity Assay, Concentration Assay, Staining, Acrylamide Gel Assay, Enzymatic Assay

    5) Product Images from "PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins"

    Article Title: PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins

    Journal: eLife

    doi: 10.7554/eLife.50416

    PPM1H dephosphorylates Rab10 in vitro. ( A ) The indicated amounts of recombinant wild-type and mutant PPM1H (with a His-Sumo N-terminal tag, expressed in E. coli ) were incubated in vitro with 2.5 µg pT73 ~60% phosphorylated Rab10[1–181, GDP bound] for 30 min in the presence of 10 mM MgCl2 in 40 mM HEPES pH 7.0 buffer. Reactions were terminated by addition of SDS Sample Buffer and analyzed by phos-tag gel electrophoresis that separates phosphorylated and dephosphorylated Rab10. Gel was stained with Instant Blue Coomassie. Bands corresponding to phosphorylated and non-phosphorylated Rab10 are marked with open (○) and closed (●) circles respectively. ( B ) As in ( A ) except that a time-course assay was performed using 2.5 µg pT73 phosphorylated Rab10[1–181, GDP bound] and 40 ng wild-type or mutant PPM1H for the indicated times. ( C ) As in ( A ) except that PPM1J was assessed. ( D ) As in ( A ) except and PPM1M was assessed.
    Figure Legend Snippet: PPM1H dephosphorylates Rab10 in vitro. ( A ) The indicated amounts of recombinant wild-type and mutant PPM1H (with a His-Sumo N-terminal tag, expressed in E. coli ) were incubated in vitro with 2.5 µg pT73 ~60% phosphorylated Rab10[1–181, GDP bound] for 30 min in the presence of 10 mM MgCl2 in 40 mM HEPES pH 7.0 buffer. Reactions were terminated by addition of SDS Sample Buffer and analyzed by phos-tag gel electrophoresis that separates phosphorylated and dephosphorylated Rab10. Gel was stained with Instant Blue Coomassie. Bands corresponding to phosphorylated and non-phosphorylated Rab10 are marked with open (○) and closed (●) circles respectively. ( B ) As in ( A ) except that a time-course assay was performed using 2.5 µg pT73 phosphorylated Rab10[1–181, GDP bound] and 40 ng wild-type or mutant PPM1H for the indicated times. ( C ) As in ( A ) except that PPM1J was assessed. ( D ) As in ( A ) except and PPM1M was assessed.

    Techniques Used: In Vitro, Recombinant, Mutagenesis, Incubation, Nucleic Acid Electrophoresis, Staining

    6) Product Images from "The plant cuticle regulates apoplastic transport of salicylic acid during systemic acquired resistance"

    Article Title: The plant cuticle regulates apoplastic transport of salicylic acid during systemic acquired resistance

    Journal: Science Advances

    doi: 10.1126/sciadv.aaz0478

    NahG plants are competent in SA transport. ( A ) SA levels in PEX collected from mock (PEX MgCl2 )– or pathogen ( avrRpt2 or TMV)–infected Arabidopsis (Di-3) or tobacco (Samsung N background) wild-type and nahG plants. Results are representative of three independent experiments. Asterisks denote significant differences from respective mock-inoculated samples ( t test, P
    Figure Legend Snippet: NahG plants are competent in SA transport. ( A ) SA levels in PEX collected from mock (PEX MgCl2 )– or pathogen ( avrRpt2 or TMV)–infected Arabidopsis (Di-3) or tobacco (Samsung N background) wild-type and nahG plants. Results are representative of three independent experiments. Asterisks denote significant differences from respective mock-inoculated samples ( t test, P

    Techniques Used: Infection

    Distal transport of SA is associated with water potential. ( A ) SA levels in PEX collected from mock (PEX MgCl2 )– and avrRpt2 (PEX avrRpt2 )–inoculated Nö and acp4 plants. A week before inoculations, one set of plants was covered with a transparent dome to increase humidity and reduce transpiration. Results are representative of three independent experiments. Asterisks denote a significant difference with respective mock-inoculated samples ( t test, P
    Figure Legend Snippet: Distal transport of SA is associated with water potential. ( A ) SA levels in PEX collected from mock (PEX MgCl2 )– and avrRpt2 (PEX avrRpt2 )–inoculated Nö and acp4 plants. A week before inoculations, one set of plants was covered with a transparent dome to increase humidity and reduce transpiration. Results are representative of three independent experiments. Asterisks denote a significant difference with respective mock-inoculated samples ( t test, P

    Techniques Used:

    7) Product Images from "Lassomycin, a ribosomally synthesized cyclic peptide, kills Mycobacterium tuberculosis by targeting the ATP-dependent protease ClpC1P1P2"

    Article Title: Lassomycin, a ribosomally synthesized cyclic peptide, kills Mycobacterium tuberculosis by targeting the ATP-dependent protease ClpC1P1P2

    Journal: Chemistry & biology

    doi: 10.1016/j.chembiol.2014.01.014

    Lassomycin effect on ClpC1 ATPase activity and protein degradation by ClpC1P1P2 complex A) Lassomycin stimulates ATPase activity of ClpC1 . 32 nM of pure ClpC1 were mixed with 100 μl of the assay buffer (50 mM TrisHCl pH 7.8; 100 mM KCl; 10% glycerol; 1 mM phosphoenolpyruvate; 1 mM NADH; 2 units of pyruvate kinase/lactic dehydrogenase (Sigma); 4 mM MgCl2 and 1 mM ATP) and the ATPase activity of ClpC1 was followed by measuring the coupled oxidation of NADH to NAD + ). The rate of ATPase activity in the absence of lassomycin was taken as 100%. The apparent K d and Hill coefficient for lassomycin activation of ClpC1 ATPase were determined using curve fitting with classic Hill-kinetic through a Scaled Levenberg-Marquardt algorithm; tolerance 0.0001. B) ClpC1 does not activate degradation of casein by ClpP1P2 in the presence of lassomycin . ClpP1P2 (100 nM) and ClpC1 (100 nM) were mixed in 80µlofreaction buffer containing 50 mM potassium phosphate (pH 7.6), 100 mM KCl, 8 mM MgCl 2 , 5% glycerol, 2 mM ATP, 5 mM Z-Leu-Leu. Enzymatic activity was measured fluorometrically using FITC-casein as a substrate in the presence or absence of 10 µM of lassomycin. The rate of degradation of ClpP1P2 was taken as 100%. C) Lassomycin does not interfere with casein binding to ClpC1 . ATPase activity of ClpC1 (32nM) was measured as in Fig. 5A in the presence or absence of casein (10 µM) and lassomycin (1 µM). The activity of ClpC1 alone (control) was taken as 100%. D) Stimulation of ClpC1 ATPase activity by lassomycin is highly specific . The activities of purified ATPases from bacteria ( M. tuberculosis ClpX; E.coli ClpA, ClpB and GroEL), archaea (PAN) and mouse (26S proteasome) were measured in the presence and absence of lassomycin (10 μM). ATPase activity of each ATPase in the absence of lassomycin was taken as 100%.
    Figure Legend Snippet: Lassomycin effect on ClpC1 ATPase activity and protein degradation by ClpC1P1P2 complex A) Lassomycin stimulates ATPase activity of ClpC1 . 32 nM of pure ClpC1 were mixed with 100 μl of the assay buffer (50 mM TrisHCl pH 7.8; 100 mM KCl; 10% glycerol; 1 mM phosphoenolpyruvate; 1 mM NADH; 2 units of pyruvate kinase/lactic dehydrogenase (Sigma); 4 mM MgCl2 and 1 mM ATP) and the ATPase activity of ClpC1 was followed by measuring the coupled oxidation of NADH to NAD + ). The rate of ATPase activity in the absence of lassomycin was taken as 100%. The apparent K d and Hill coefficient for lassomycin activation of ClpC1 ATPase were determined using curve fitting with classic Hill-kinetic through a Scaled Levenberg-Marquardt algorithm; tolerance 0.0001. B) ClpC1 does not activate degradation of casein by ClpP1P2 in the presence of lassomycin . ClpP1P2 (100 nM) and ClpC1 (100 nM) were mixed in 80µlofreaction buffer containing 50 mM potassium phosphate (pH 7.6), 100 mM KCl, 8 mM MgCl 2 , 5% glycerol, 2 mM ATP, 5 mM Z-Leu-Leu. Enzymatic activity was measured fluorometrically using FITC-casein as a substrate in the presence or absence of 10 µM of lassomycin. The rate of degradation of ClpP1P2 was taken as 100%. C) Lassomycin does not interfere with casein binding to ClpC1 . ATPase activity of ClpC1 (32nM) was measured as in Fig. 5A in the presence or absence of casein (10 µM) and lassomycin (1 µM). The activity of ClpC1 alone (control) was taken as 100%. D) Stimulation of ClpC1 ATPase activity by lassomycin is highly specific . The activities of purified ATPases from bacteria ( M. tuberculosis ClpX; E.coli ClpA, ClpB and GroEL), archaea (PAN) and mouse (26S proteasome) were measured in the presence and absence of lassomycin (10 μM). ATPase activity of each ATPase in the absence of lassomycin was taken as 100%.

    Techniques Used: Activity Assay, Activation Assay, Binding Assay, Purification

    Related Articles

    Protease Inhibitor:

    Article Title: The plant cuticle regulates apoplastic transport of salicylic acid during systemic acquired resistance
    Article Snippet: .. Protein extraction and immunoblot analysis Proteins were extracted in buffer containing 50 mM tris-HCl (pH7.5), 10% glycerol, 150 mM NaCl, 10 mM MgCl2 , 5 mM EDTA, 5 mM dithiothreitol, and 1× protease inhibitor cocktail (Sigma-Aldrich, St. Louis, MO). .. Protein concentration was measured by the Bio-Rad protein assay (Bio-Rad, CA).

    Protein Extraction:

    Article Title: The plant cuticle regulates apoplastic transport of salicylic acid during systemic acquired resistance
    Article Snippet: .. Protein extraction and immunoblot analysis Proteins were extracted in buffer containing 50 mM tris-HCl (pH7.5), 10% glycerol, 150 mM NaCl, 10 mM MgCl2 , 5 mM EDTA, 5 mM dithiothreitol, and 1× protease inhibitor cocktail (Sigma-Aldrich, St. Louis, MO). .. Protein concentration was measured by the Bio-Rad protein assay (Bio-Rad, CA).

    other:

    Article Title: In vitro evaluation of the toxic effects of MgO nanostructure in Hela cell line
    Article Snippet: Chemicals and Synthesis of MgO Nanotubes Magnesium chloride (MgCl2 ), sodium hydroxide (NaOH), polyvinyl alcohol (PVA), and ethanol were purchased from Sigma Aldrich and used as chemical reagents.

    Article Title: Colloidal stability as a determinant of nanoparticle behavior in the brain
    Article Snippet: ACSF was prepared with the addition of the following concentrations of reagents to deionized (DI) water: 119 mM NaCl (MilliporeSigma), 26.2 mM NaHCO3 (MilliporeSigma), 2.5 mM KCl (MilliporeSigma), 1 mM NaH2 PO4 (MilliporeSigma), 1.3 mM MgCl2 (MilliporeSigma), and 10 mM glucose (MilliporeSigma).

    Article Title: UbFluor: A Fluorescent Thioester to Monitor HECT E3 Ligase Catalysis
    Article Snippet: 500 mM Na2 HPO4 /NaH2 PO4 pH 8.0 pH 8.0 (see recipe) Adenosine triphosphate disodium salt hydrate (ATP, Aldrich) 2-mercaptoethanesulfonic acid sodium salt (MESNa, Aldrich) Magnesium chloride Ubiquitin from bovine erythrocytes (Aldrich) Storage Buffer A: 25 mM NaCl, 12.5 mM HEPES pH 6.7 (see recipe) Cysteamine hydrochloride Trifluoroacetic acid (TFA) Methylene chloride Trityl chloride 1 M NaOH aqueous solution Saturated sodium chloride aqueous solution Magnesium sulfate (anhydrous) Diethyl ether/n-pentane (1:4 ratio) Dimethylformamide (DMF) Fluorescein isothiocyanate (Aldrich, isomer 1) N,N-diisopropylethylamine 50 mM HEPES pH 6.5 (see recipe) Silica gel, standard grade (Sorbent technologies, 60 Å, 40-63 μm particle size or comparable) Ethyl acetate Sand Methanol Trifluoroacetic acid Triethylsilane Acetonitrile/water (3:7) with 0.1 % TFA (see recipe) DMSO/H2O (1:1) (see recipe) Sodium bicarbonate 1 M HEPES pH 7.5 (see recipe) Tris(2-carboxyethyl)phosphine hydrochloride (Aldrich) Guanidine hydrochloride Storage Buffer B: 250 mM NaCl, 12.5 mM HEPES pH 6.0 (see recipe) 1 × PBS with 20 mM BME (see recipe)

    Article Title: Functional Analysis of an Acid Adaptive DNA Adenine Methyltransferase from Helicobacter pylori 26695
    Article Snippet: Chloramphenicol, bovine serum albumin, MgCl2 , MnCl2 , CoCl2 , CaCl2 , NiCl2 , ZnCl2 , ampicillin, imidazole, Coomassie Brilliant Blue R-250, RNase A, glutaraldehyde, and S -adenosyl-L-homocysteine (AdoHcy) were procured from Sigma-Aldrich Co., USA.

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  • 92
    Millipore atp measurement
    <t>AMD</t> RPE are more susceptible to oxidative stress and show lower mitochondrial activity. ( a and b ) Cell viability assays of AMD and control RPE treated with increasing concentrations of H 2 O 2 for 24 h ( a ) and 48 h ( b ). Higher susceptibility of the AMD RPE under oxidative stress conditions is observed in 48 h. ( c ) ROS production under stress is significantly higher in AMD RPE. ( d and e ) AMD RPE have significantly lower mitochondrial activity, as indicated by their <t>ATP</t> levels measured by a luminescence assay in the presence of hexokinase inhibitor. ( d ) ATP levels produced by mitochondria are significantly lower in AMD RPE as measured in the presence of hexokinase inhibitor. ( e ) ATP levels produced by glycolysis are higher in AMD RPE as measured in the absence of hexokinase inhibitor. The difference in ATP levels measured in the presence ( d ) and absence ( e ) of hexokinase inhibitor show glycolysis as the major source of ATP production in AMD RPE. Asterisks (*) indicate statistical significance, determined by the ANOVA analysis followed by Tukey's test ( P -value
    Atp Measurement, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 57 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/atp measurement/product/Millipore
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    AMD RPE are more susceptible to oxidative stress and show lower mitochondrial activity. ( a and b ) Cell viability assays of AMD and control RPE treated with increasing concentrations of H 2 O 2 for 24 h ( a ) and 48 h ( b ). Higher susceptibility of the AMD RPE under oxidative stress conditions is observed in 48 h. ( c ) ROS production under stress is significantly higher in AMD RPE. ( d and e ) AMD RPE have significantly lower mitochondrial activity, as indicated by their ATP levels measured by a luminescence assay in the presence of hexokinase inhibitor. ( d ) ATP levels produced by mitochondria are significantly lower in AMD RPE as measured in the presence of hexokinase inhibitor. ( e ) ATP levels produced by glycolysis are higher in AMD RPE as measured in the absence of hexokinase inhibitor. The difference in ATP levels measured in the presence ( d ) and absence ( e ) of hexokinase inhibitor show glycolysis as the major source of ATP production in AMD RPE. Asterisks (*) indicate statistical significance, determined by the ANOVA analysis followed by Tukey's test ( P -value

    Journal: Cell Death & Disease

    Article Title: Dysfunctional autophagy in RPE, a contributing factor in age-related macular degeneration

    doi: 10.1038/cddis.2016.453

    Figure Lengend Snippet: AMD RPE are more susceptible to oxidative stress and show lower mitochondrial activity. ( a and b ) Cell viability assays of AMD and control RPE treated with increasing concentrations of H 2 O 2 for 24 h ( a ) and 48 h ( b ). Higher susceptibility of the AMD RPE under oxidative stress conditions is observed in 48 h. ( c ) ROS production under stress is significantly higher in AMD RPE. ( d and e ) AMD RPE have significantly lower mitochondrial activity, as indicated by their ATP levels measured by a luminescence assay in the presence of hexokinase inhibitor. ( d ) ATP levels produced by mitochondria are significantly lower in AMD RPE as measured in the presence of hexokinase inhibitor. ( e ) ATP levels produced by glycolysis are higher in AMD RPE as measured in the absence of hexokinase inhibitor. The difference in ATP levels measured in the presence ( d ) and absence ( e ) of hexokinase inhibitor show glycolysis as the major source of ATP production in AMD RPE. Asterisks (*) indicate statistical significance, determined by the ANOVA analysis followed by Tukey's test ( P -value

    Article Snippet: To assay the mitochondrial activity in AMD and normal RPE, the ATP measurement was performed following 2-h incubation with or without 10 μ M of the bromopyruvate analog (3-BrPA), an inhibitor of the glycolytic enzyme hexokinase II (EMD Millipore, Billerica, MA, USA).

    Techniques: Activity Assay, Luminescence Assay, Produced

    Fluorescence anisotropy measurements (Δ r ) of equilibrium binding of ISWI to DNA and nucleosomes in the presence of nucleotides. (A) Equilibrium binding to a 20 bp FITC-labeled DNA substrate (25 nM) in the presence of ATP-γ-S. These data were analyzed using Scheme 1 as described in Experimental Procedures . The solid lines in the figure represent the fits of the data to this scheme, which returned the following values: 1/β A = 140 ± 30 μM, 1/β A,1 = 390 ± 70 μM, and 1/β 1,A = 42 ± 8 nM. (B) Equilibrium binding to a 20 bp FITC-labeled DNA substrate (25 nM) in the presence of ADP. The solid line in this figure represents the fit of equilibrium DNA binding data collected in the absence of nucleotide (Figure 1 A). (C) Equilibrium binding to an Alexa488-labeled 10N5 nucleosome substrate in the presence of ATP-γ-S. (D) Equilibrium binding to an Alexa488-labeled 10N5 nucleosome substrate in the presence of ADP. The solid lines in panels C and D are the fits of the equilibrium nucleosome binding data collected in the absence of nucleotides (Figure 1 C).

    Journal: Biochemistry

    Article Title: Quantitative Determination of Binding of ISWI to Nucleosomes and DNA Shows Allosteric Regulation of DNA Binding by Nucleotides

    doi: 10.1021/bi500224t

    Figure Lengend Snippet: Fluorescence anisotropy measurements (Δ r ) of equilibrium binding of ISWI to DNA and nucleosomes in the presence of nucleotides. (A) Equilibrium binding to a 20 bp FITC-labeled DNA substrate (25 nM) in the presence of ATP-γ-S. These data were analyzed using Scheme 1 as described in Experimental Procedures . The solid lines in the figure represent the fits of the data to this scheme, which returned the following values: 1/β A = 140 ± 30 μM, 1/β A,1 = 390 ± 70 μM, and 1/β 1,A = 42 ± 8 nM. (B) Equilibrium binding to a 20 bp FITC-labeled DNA substrate (25 nM) in the presence of ADP. The solid line in this figure represents the fit of equilibrium DNA binding data collected in the absence of nucleotide (Figure 1 A). (C) Equilibrium binding to an Alexa488-labeled 10N5 nucleosome substrate in the presence of ATP-γ-S. (D) Equilibrium binding to an Alexa488-labeled 10N5 nucleosome substrate in the presence of ADP. The solid lines in panels C and D are the fits of the equilibrium nucleosome binding data collected in the absence of nucleotides (Figure 1 C).

    Article Snippet: To separate ADP from ATP species, reaction mixtures were analyzed using thin liquid chromatography PEI-cellulose plates (EMD chemicals) in 0.6 M potassium phosphate (pH 3.4) buffer, quantified using a Typhoon Phosphor imager.

    Techniques: Fluorescence, Binding Assay, Labeling

    Identification of CK2 phosphorylation sites in mouse SIRT1. (A) Diagram of recombinant mouse SIRT1 fragments produced in E.coli. The a.a. number of the first and last a. a. for each fragment is as indicated. (B) SIRT1 fragments from (A) were incubated with CK2 α and 32 P[γ-ATP], subjected to SDS-PAGE, Coomassie staining and autoradiography. GST-PC, which contains the optimized CK2 phosphorylation site, was used as a positive control. (C) Evolutionarily conserved CK2 consensus sites located in the fragments phosphorylated by CK2 are marked (*). (D–H) Indicated Ser (S) residues in SIRT1 fragments (see Fig. 2A ) were mutated to Ala (A) individually or in combination. Fragments containing the mutation were incubated with CK2 α and 32 P[γ-ATP] and then subjected to SDS-PAGE, Coomassie staining and autoradiography. (I) CK2-dependent phosphorylation of full-length (FL) and S154/649/651/683A (4A) mutant SIRT1 in vitro . CK2 phosphorylation was performed and visualized as in (B).

    Journal: PLoS ONE

    Article Title: CK2 Is the Regulator of SIRT1 Substrate-Binding Affinity, Deacetylase Activity and Cellular Response to DNA-Damage

    doi: 10.1371/journal.pone.0006611

    Figure Lengend Snippet: Identification of CK2 phosphorylation sites in mouse SIRT1. (A) Diagram of recombinant mouse SIRT1 fragments produced in E.coli. The a.a. number of the first and last a. a. for each fragment is as indicated. (B) SIRT1 fragments from (A) were incubated with CK2 α and 32 P[γ-ATP], subjected to SDS-PAGE, Coomassie staining and autoradiography. GST-PC, which contains the optimized CK2 phosphorylation site, was used as a positive control. (C) Evolutionarily conserved CK2 consensus sites located in the fragments phosphorylated by CK2 are marked (*). (D–H) Indicated Ser (S) residues in SIRT1 fragments (see Fig. 2A ) were mutated to Ala (A) individually or in combination. Fragments containing the mutation were incubated with CK2 α and 32 P[γ-ATP] and then subjected to SDS-PAGE, Coomassie staining and autoradiography. (I) CK2-dependent phosphorylation of full-length (FL) and S154/649/651/683A (4A) mutant SIRT1 in vitro . CK2 phosphorylation was performed and visualized as in (B).

    Article Snippet: In vitro kinase assay To identify CK2 phosphorylation sites, recombinant full-length or truncated His-tagged or GST-tagged SIRT1 proteins were incubated in kinase buffer (20 mM HEPES at pH 7.0, 10 mM MgCl2 , 1 mM DTT) containing 100 µM cold ATP, 1 µCi (3000 mCi/mmole) 32 P[γ-ATP] and 20 ng CK2α enzyme (Millipore) for 20 min at 30°C.

    Techniques: Recombinant, Produced, Incubation, SDS Page, Staining, Autoradiography, Positive Control, Mutagenesis, In Vitro

    Serine 324 is required for UV-induced MSK2 activation and for autophosphorylation at MSK2-Ser 196 . A , purified recombinant GST or GST-MSK2 was subjected to CK2 in vitro kinase reactions with γ-[ 32 P]ATP. [ 32 P]ATP incorporation was assessed by autoradiography.

    Journal:

    Article Title: Differential Regulation of Mitogen- and Stress-activated Protein Kinase-1 and -2 (MSK1 and MSK2) by CK2 following UV Radiation *

    doi: 10.1074/jbc.M109.083808

    Figure Lengend Snippet: Serine 324 is required for UV-induced MSK2 activation and for autophosphorylation at MSK2-Ser 196 . A , purified recombinant GST or GST-MSK2 was subjected to CK2 in vitro kinase reactions with γ-[ 32 P]ATP. [ 32 P]ATP incorporation was assessed by autoradiography.

    Article Snippet: Immunoprecipitation kinase assays were performed with 10 m m MOPS, pH 7.2, 12.5 m m β-glycerol phosphate, 2.5 m m EGTA, 0.5 m m sodium orthovanadate, 0.5 m m dithiothreitol, 6.25 m m magnesium acetate, 62.5 μ m cold ATP, 10 μCi of γ-[32 P]ATP, and 20 μ m crosstide (GRPRTSSFAEG- KK ) (Millipore) harboring two lysine residues (underlined) at the C terminus to facilitate binding to P81 paper.

    Techniques: Activation Assay, Purification, Recombinant, In Vitro, Autoradiography