Structured Review

GE Healthcare ethylenediaminetetraacetic acid
Ethylenediaminetetraacetic Acid, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ethylenediaminetetraacetic acid/product/GE Healthcare
Average 92 stars, based on 14 article reviews
Price from $9.99 to $1999.99
ethylenediaminetetraacetic acid - by Bioz Stars, 2020-07
92/100 stars

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Related Articles

Chromatography:

Article Title: Surfactant proteins A and D inhibit the growth of Gram-negative bacteria by increasing membrane permeability
Article Snippet: .. After elution with 2 mM EDTA, gel exclusion chromatography with Superose 6 (Amersham Biosciences, Piscataway, New Jersey, USA) was used to remove contaminating SP-D. ..

Purification:

Article Title: Identification of Channel-lining Amino Acid Residues in the Hydrophobic Segment of Colicin Ia
Article Snippet: .. Dialyzed streptomycin-sulfate supernatants in 50 mM sodium borate, pH 9.0, 2 mM dithiothreitol (DTT), and 2 mM EDTA were purified on 1- or 5-ml pre-packed HiTrap CM FF columns (GE Healthcare). ..

Article Title: Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities
Article Snippet: .. For further purification, the buffer of partially purified enzymes was changed to 50 mM Tris-HCl, 200 mM NaCl and 1 mM EDTA (pH 8.0) by using PD-10 columns (GE Healthcare, Chalfont St. Giles, Buckinghamshire, UK). .. Final purification was obtained by the use of size exclusion chromatography on Superdex 200 column (GE Healthcare) equilibrated in 50 mM Tris-HCl, 200 mM NaCl and 1 mM EDTA (pH 8.0).

Article Title: The Arabidopsis Chloroplastic NifU-Like Protein CnfU, Which Can Act as an Iron-Sulfur Cluster Scaffold Protein, Is Required for Biogenesis of Ferredoxin and Photosystem I W⃞
Article Snippet: .. Purified AtCnfU-V (25 μg) dissolved in a buffer containing 50 mM Tris-HCl, pH 7.5, 150 mM KCl, and 5 mM DTT were further treated either with 10 mM EDTA or 1 mM DTT on ice for 1 h. After treatment, samples were loaded onto Superdex 75 columns (Amersham Biosciences) and eluted with the same buffer. ..

Fast Protein Liquid Chromatography:

Article Title: Stability and Function of the Sec61 Translocation Complex Depends on the Sss1p Tail-Anchor Sequence
Article Snippet: .. A total of 300µl of the cleared sample was loaded directly onto a Superdex 200 HR 10/30 column (or Superose 6 HR 10/30 column for WT, CTSa and TMSa samples) (Amersham Pharmacia Biotech, GE Healthcare Life Sciences, Canada) pre-equilibrated in 50mM HEPES-KOH, pH 7.5, 500mM potassium acetate, 0.1% digitonin, 1mM EDTA, 5mM β-mercaptoethanol, and 1XCPIC and run at 0.2ml/min on an ÄKTA FPLC System (Amersham Pharmacia Biotech, GE Healthcare Life Sciences, Canada) at 4°C. .. Fifty 0.5ml fractions were collected, and the proteins were precipitated with trichloroacetic acid, separated by SDS-PAGE, and transferred to nitrocellulose.

Article Title: Oxygen-Linked S-Nitrosation in Fish Myoglobins: A Cysteine-Specific Tertiary Allosteric Effect
Article Snippet: .. Samples were centrifuged for 25 min at 12,000 g, passed on a PD-10 column (GE Healthcare) equilibrated with 50 mM Tris-HCl, 0.5 mM EDTA, 3 mM dithiothreitol (DTT), pH 8.3 and loaded on a gel-filtration Tricorn Superdex 75 10/300 GL FPLC-column (GE-Healthcare) equilibrated with 50 mM Tris-HCl, 0.5 mM EDTA, 3 mM DTT, 0.15 M NaCl, pH 8.3. .. Finally, the sample was dialysed against 20 mM Tris-HCl pH 9.2, passed through an ion exchange Hitrap Q-FF FPLC-column, and eluted with a 30-min gradient of 0–0.5 M NaCl in 20 mM Tris-HCl pH 9.2 at a flow rate of 1 mL/min.

Western Blot:

Article Title: A novel mechanism of “metal gel-shift” by histidine-rich Ni2+-binding Hpn protein from Helicobacter pylori strain SS1
Article Snippet: .. Western blotting analysis The Hpn protein (25 μM) treated with indicated mol equivalent of EDTA or Ni2+ resolved on SDS-PAGE (20%) and then electrophoretically blotted onto polyvinylidene fluoride (PVDF) membrane (Amersham Hybond-P, GE Healthcare, code: RPN303F) in transfer buffer containing no methanol. ..

Recombinant:

Article Title: DSSylation, a novel protein modification targets proteins induced by oxidative stress, and facilitates their degradation in cells
Article Snippet: .. The DSS1-V5-His recombinant protein was eluted with 1× TBS [20 mmol/L Tris-HCl (pH = 7.4) and 0.9% NaCl] containing 50 mmol/L EDTA followed by loading it onto the 1 mL HiTrap Capto DEAE ion exchange column (GE Healthcare). ..

SDS Page:

Article Title: A novel mechanism of “metal gel-shift” by histidine-rich Ni2+-binding Hpn protein from Helicobacter pylori strain SS1
Article Snippet: .. Western blotting analysis The Hpn protein (25 μM) treated with indicated mol equivalent of EDTA or Ni2+ resolved on SDS-PAGE (20%) and then electrophoretically blotted onto polyvinylidene fluoride (PVDF) membrane (Amersham Hybond-P, GE Healthcare, code: RPN303F) in transfer buffer containing no methanol. ..

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  • 92
    GE Healthcare edta plasma supernatant
    Separation of C3dg from the larger C3 fragments. Measurements of C3 molecules encompassing the determinants of the segment C3dg, i.e., C3 and all degradation molecules containing this part of C3. (A) The figure illustrates C3dg measurement on gel permeation chromatography (GPC) fractions of serum before activation (red line) and supernatant of polyethylene glycol <t>(PEG)-precipitated</t> activated serum (blue line). (B) Test for the optimal concentration of PEG for precipitation. Increasing concentrations of PEG were added to <t>EDTA</t> plasma and C3dg was estimated in the supernatants. (C) GPC of supernatant after precipitation of EDTA plasma with 11% (red) and 16% (blue) PEG. C3dg in the fractions was measured. The 11% supernatant shows two major peaks, the first corresponding to C3 and larger C3 components, and the second corresponding to free C3dg. After precipitation with 16% PEG the first was significantly reduced. Panel (D) shows the results of western blotting of supernatants of EDTA-plasma precipitated with 16% (lane 1) or 11% (lane 2) PEG. The samples (corresponding to 0.1 µl plasma) were run non-reduced on the SDS-PAGE. The blot was developed with anti-C3d antibody. It can be seen that the 11% PEG supernatant still contains appreciable amounts of larger C3dg-encompassing molecules. This was repeated three times with similar results.
    Edta Plasma Supernatant, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/edta plasma supernatant/product/GE Healthcare
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    edta plasma supernatant - by Bioz Stars, 2020-07
    92/100 stars
      Buy from Supplier

    93
    GE Healthcare edta
    Steady-state kinetic parameters for mAOX1-4 with aromatic aldehydes as substrates containing a benzyl-group. Apparent steady-state kinetic parameters were recorded in 50 mM <t>Tris-HCl,</t> 200 mM NaCl, and 1 mM <t>EDTA</t> (pH 8.0) in the presence of 100 μM DCPIP as electron acceptor. The substrate concentrations were varied around 0.5 and 10 times the K M . The chemical structure of each substrate is shown in the Fig. The values were corrected to a molybdenum saturation of 100% for each mAOX variant for a better comparability. Kinetic Data are mean values from three independent measurements (±S.D.). n.d. = no activity detectable.
    Edta, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 73 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/edta/product/GE Healthcare
    Average 93 stars, based on 73 article reviews
    Price from $9.99 to $1999.99
    edta - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

    92
    GE Healthcare immunoprecipitation buffer
    <t>Immunoprecipitation</t> of GS under different experimental conditions. The cells were incubated under the different conditions for 24–48 h beyond the logarithmic stage of growth. After this period, GS was immunoprecipitated and analyzed for protein oxidation detection as described in Materials and Methods. Oxidized GS was identified by using anti-DNP antibodies: (C) control, (-N 24 h) and (-N 48 h) nitrogen starvation at 24 and 48 h, (-Fe) iron starvation, (-P) phosphorus starvation, (DK) darkness, (DC) DCMU, (DB) DBMIB.
    Immunoprecipitation Buffer, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/immunoprecipitation buffer/product/GE Healthcare
    Average 92 stars, based on 21 article reviews
    Price from $9.99 to $1999.99
    immunoprecipitation buffer - by Bioz Stars, 2020-07
    92/100 stars
      Buy from Supplier

    Image Search Results


    Separation of C3dg from the larger C3 fragments. Measurements of C3 molecules encompassing the determinants of the segment C3dg, i.e., C3 and all degradation molecules containing this part of C3. (A) The figure illustrates C3dg measurement on gel permeation chromatography (GPC) fractions of serum before activation (red line) and supernatant of polyethylene glycol (PEG)-precipitated activated serum (blue line). (B) Test for the optimal concentration of PEG for precipitation. Increasing concentrations of PEG were added to EDTA plasma and C3dg was estimated in the supernatants. (C) GPC of supernatant after precipitation of EDTA plasma with 11% (red) and 16% (blue) PEG. C3dg in the fractions was measured. The 11% supernatant shows two major peaks, the first corresponding to C3 and larger C3 components, and the second corresponding to free C3dg. After precipitation with 16% PEG the first was significantly reduced. Panel (D) shows the results of western blotting of supernatants of EDTA-plasma precipitated with 16% (lane 1) or 11% (lane 2) PEG. The samples (corresponding to 0.1 µl plasma) were run non-reduced on the SDS-PAGE. The blot was developed with anti-C3d antibody. It can be seen that the 11% PEG supernatant still contains appreciable amounts of larger C3dg-encompassing molecules. This was repeated three times with similar results.

    Journal: Frontiers in Immunology

    Article Title: The C3dg Fragment of Complement Is Superior to Conventional C3 as a Diagnostic Biomarker in Systemic Lupus Erythematosus

    doi: 10.3389/fimmu.2018.00581

    Figure Lengend Snippet: Separation of C3dg from the larger C3 fragments. Measurements of C3 molecules encompassing the determinants of the segment C3dg, i.e., C3 and all degradation molecules containing this part of C3. (A) The figure illustrates C3dg measurement on gel permeation chromatography (GPC) fractions of serum before activation (red line) and supernatant of polyethylene glycol (PEG)-precipitated activated serum (blue line). (B) Test for the optimal concentration of PEG for precipitation. Increasing concentrations of PEG were added to EDTA plasma and C3dg was estimated in the supernatants. (C) GPC of supernatant after precipitation of EDTA plasma with 11% (red) and 16% (blue) PEG. C3dg in the fractions was measured. The 11% supernatant shows two major peaks, the first corresponding to C3 and larger C3 components, and the second corresponding to free C3dg. After precipitation with 16% PEG the first was significantly reduced. Panel (D) shows the results of western blotting of supernatants of EDTA-plasma precipitated with 16% (lane 1) or 11% (lane 2) PEG. The samples (corresponding to 0.1 µl plasma) were run non-reduced on the SDS-PAGE. The blot was developed with anti-C3d antibody. It can be seen that the 11% PEG supernatant still contains appreciable amounts of larger C3dg-encompassing molecules. This was repeated three times with similar results.

    Article Snippet: Samples of serum, supernatant of PEG precipitated activated serum and EDTA-plasma supernatant after precipitation with either 11 or 16% PEG (w/v), were subjected to GPC on a Superose 6 10/300 GL column (GE Healthcare).

    Techniques: GPC Assay, Gel Permeation Chromatography, Activation Assay, Concentration Assay, Western Blot, SDS Page

    Steady-state kinetic parameters for mAOX1-4 with aromatic aldehydes as substrates containing a benzyl-group. Apparent steady-state kinetic parameters were recorded in 50 mM Tris-HCl, 200 mM NaCl, and 1 mM EDTA (pH 8.0) in the presence of 100 μM DCPIP as electron acceptor. The substrate concentrations were varied around 0.5 and 10 times the K M . The chemical structure of each substrate is shown in the Fig. The values were corrected to a molybdenum saturation of 100% for each mAOX variant for a better comparability. Kinetic Data are mean values from three independent measurements (±S.D.). n.d. = no activity detectable.

    Journal: PLoS ONE

    Article Title: Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities

    doi: 10.1371/journal.pone.0191819

    Figure Lengend Snippet: Steady-state kinetic parameters for mAOX1-4 with aromatic aldehydes as substrates containing a benzyl-group. Apparent steady-state kinetic parameters were recorded in 50 mM Tris-HCl, 200 mM NaCl, and 1 mM EDTA (pH 8.0) in the presence of 100 μM DCPIP as electron acceptor. The substrate concentrations were varied around 0.5 and 10 times the K M . The chemical structure of each substrate is shown in the Fig. The values were corrected to a molybdenum saturation of 100% for each mAOX variant for a better comparability. Kinetic Data are mean values from three independent measurements (±S.D.). n.d. = no activity detectable.

    Article Snippet: For further purification, the buffer of partially purified enzymes was changed to 50 mM Tris-HCl, 200 mM NaCl and 1 mM EDTA (pH 8.0) by using PD-10 columns (GE Healthcare, Chalfont St. Giles, Buckinghamshire, UK).

    Techniques: Variant Assay, Activity Assay

    Steady-state kinetic parameters for mAOX1-4 with N-heterocyclic compounds as substrates. Apparent steady-state kinetic parameters were recorded in 50 mM Tris-HCl, 200 mM NaCl, and 1 mM EDTA (pH 8.0) in the presence of 100 μM DCPIP as electron acceptor. The substrate concentrations were varied around 0.5 and 10 times the K M . The chemical structure of each substrate is shown in the Fig. The values were corrected to a molybdenum saturation of 100% for each mAOX variant for a better comparability. Kinetic Data are mean values from three independent measurements (±S.D.). n.d. = no activity detectable.

    Journal: PLoS ONE

    Article Title: Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities

    doi: 10.1371/journal.pone.0191819

    Figure Lengend Snippet: Steady-state kinetic parameters for mAOX1-4 with N-heterocyclic compounds as substrates. Apparent steady-state kinetic parameters were recorded in 50 mM Tris-HCl, 200 mM NaCl, and 1 mM EDTA (pH 8.0) in the presence of 100 μM DCPIP as electron acceptor. The substrate concentrations were varied around 0.5 and 10 times the K M . The chemical structure of each substrate is shown in the Fig. The values were corrected to a molybdenum saturation of 100% for each mAOX variant for a better comparability. Kinetic Data are mean values from three independent measurements (±S.D.). n.d. = no activity detectable.

    Article Snippet: For further purification, the buffer of partially purified enzymes was changed to 50 mM Tris-HCl, 200 mM NaCl and 1 mM EDTA (pH 8.0) by using PD-10 columns (GE Healthcare, Chalfont St. Giles, Buckinghamshire, UK).

    Techniques: Variant Assay, Activity Assay

    Steady-state kinetic parameters for mAOX1-4 with aliphatic aldehydes as substrates. Apparent steady-state kinetic parameters were recorded in 50 mM Tris-HCl, 200 mM NaCl, and 1 mM EDTA (pH 8.0) in the presence of 100 μM DCPIP as electron acceptor. The substrate concentrations were varied around 0.5 and 10 times the K M . The chemical structure of each substrate is shown in the Fig. The values were corrected to a molybdenum saturation of 100% for each mAOX variant for a better comparability. Kinetic Data are mean values from three independent measurements (±S.D.). n.d. = no activity detectable.

    Journal: PLoS ONE

    Article Title: Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities

    doi: 10.1371/journal.pone.0191819

    Figure Lengend Snippet: Steady-state kinetic parameters for mAOX1-4 with aliphatic aldehydes as substrates. Apparent steady-state kinetic parameters were recorded in 50 mM Tris-HCl, 200 mM NaCl, and 1 mM EDTA (pH 8.0) in the presence of 100 μM DCPIP as electron acceptor. The substrate concentrations were varied around 0.5 and 10 times the K M . The chemical structure of each substrate is shown in the Fig. The values were corrected to a molybdenum saturation of 100% for each mAOX variant for a better comparability. Kinetic Data are mean values from three independent measurements (±S.D.). n.d. = no activity detectable.

    Article Snippet: For further purification, the buffer of partially purified enzymes was changed to 50 mM Tris-HCl, 200 mM NaCl and 1 mM EDTA (pH 8.0) by using PD-10 columns (GE Healthcare, Chalfont St. Giles, Buckinghamshire, UK).

    Techniques: Variant Assay, Activity Assay

    Steady-state kinetic parameters for mAOX1-4 with cinnamaldehyde-related compounds as substrates aromatic aldehydes as substrates. Apparent steady-state kinetic parameters were recorded in 50 mM Tris-HCl, 200 mM NaCl, and 1 mM EDTA (pH 8.0) in the presence of 100 μM DCPIP as electron acceptor. The substrate concentrations were varied around 0.5 and 10 times the K M . The chemical structure of each substrate is shown in the Fig. The values were corrected to a molybdenum saturation of 100% for each mAOX variant for a better comparability. Kinetic Data are mean values from three independent measurements (±S.D.). n.d. = no activity detectable.

    Journal: PLoS ONE

    Article Title: Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities

    doi: 10.1371/journal.pone.0191819

    Figure Lengend Snippet: Steady-state kinetic parameters for mAOX1-4 with cinnamaldehyde-related compounds as substrates aromatic aldehydes as substrates. Apparent steady-state kinetic parameters were recorded in 50 mM Tris-HCl, 200 mM NaCl, and 1 mM EDTA (pH 8.0) in the presence of 100 μM DCPIP as electron acceptor. The substrate concentrations were varied around 0.5 and 10 times the K M . The chemical structure of each substrate is shown in the Fig. The values were corrected to a molybdenum saturation of 100% for each mAOX variant for a better comparability. Kinetic Data are mean values from three independent measurements (±S.D.). n.d. = no activity detectable.

    Article Snippet: For further purification, the buffer of partially purified enzymes was changed to 50 mM Tris-HCl, 200 mM NaCl and 1 mM EDTA (pH 8.0) by using PD-10 columns (GE Healthcare, Chalfont St. Giles, Buckinghamshire, UK).

    Techniques: Variant Assay, Activity Assay

    Effect of trans MTSET on the macroscopic current through colicin Ia mutant N578C channels. The top trace shows the membrane current and the bottom trace shows the voltage, each as a function of time. Before the start of the record, DTT was added to the trans compartment to a final concentration of 5 μM and 1.0 μg N578C (along with 4.5 μg octylglucoside and DTT to 5 μM) was added to the cis compartment. We quickly opened on the order of 1,000 channels by stepping the membrane potential to +70 mV, and then switched it to +50 mV to establish a slower channel-opening rate. At the arrow, 200 μg MTSET was added to the trans compartment. This caused a decrease in current of ∼25%, demonstrating that residue N578C was accessible for reaction. Finally, we confirmed that the channels closed normally when the membrane potential was switched to −50 mV. The solution on both sides of the membrane was 100 mM KCl, 5 mM CaCl 2 , 1 mM EDTA, 20 mM HEPES, pH 7.2. (The membrane broke after colicin addition and was reformed before the start of the record; similar results were obtained with membranes that had not broken.)

    Journal: The Journal of General Physiology

    Article Title: Identification of Channel-lining Amino Acid Residues in the Hydrophobic Segment of Colicin Ia

    doi: 10.1085/jgp.200810042

    Figure Lengend Snippet: Effect of trans MTSET on the macroscopic current through colicin Ia mutant N578C channels. The top trace shows the membrane current and the bottom trace shows the voltage, each as a function of time. Before the start of the record, DTT was added to the trans compartment to a final concentration of 5 μM and 1.0 μg N578C (along with 4.5 μg octylglucoside and DTT to 5 μM) was added to the cis compartment. We quickly opened on the order of 1,000 channels by stepping the membrane potential to +70 mV, and then switched it to +50 mV to establish a slower channel-opening rate. At the arrow, 200 μg MTSET was added to the trans compartment. This caused a decrease in current of ∼25%, demonstrating that residue N578C was accessible for reaction. Finally, we confirmed that the channels closed normally when the membrane potential was switched to −50 mV. The solution on both sides of the membrane was 100 mM KCl, 5 mM CaCl 2 , 1 mM EDTA, 20 mM HEPES, pH 7.2. (The membrane broke after colicin addition and was reformed before the start of the record; similar results were obtained with membranes that had not broken.)

    Article Snippet: Dialyzed streptomycin-sulfate supernatants in 50 mM sodium borate, pH 9.0, 2 mM dithiothreitol (DTT), and 2 mM EDTA were purified on 1- or 5-ml pre-packed HiTrap CM FF columns (GE Healthcare).

    Techniques: IA, Mutagenesis, Concentration Assay

    Immunoprecipitation of GS under different experimental conditions. The cells were incubated under the different conditions for 24–48 h beyond the logarithmic stage of growth. After this period, GS was immunoprecipitated and analyzed for protein oxidation detection as described in Materials and Methods. Oxidized GS was identified by using anti-DNP antibodies: (C) control, (-N 24 h) and (-N 48 h) nitrogen starvation at 24 and 48 h, (-Fe) iron starvation, (-P) phosphorus starvation, (DK) darkness, (DC) DCMU, (DB) DBMIB.

    Journal: PLoS ONE

    Article Title: Glutamine Synthetase Sensitivity to Oxidative Modification during Nutrient Starvation in Prochlorococcus marinus PCC 9511

    doi: 10.1371/journal.pone.0135322

    Figure Lengend Snippet: Immunoprecipitation of GS under different experimental conditions. The cells were incubated under the different conditions for 24–48 h beyond the logarithmic stage of growth. After this period, GS was immunoprecipitated and analyzed for protein oxidation detection as described in Materials and Methods. Oxidized GS was identified by using anti-DNP antibodies: (C) control, (-N 24 h) and (-N 48 h) nitrogen starvation at 24 and 48 h, (-Fe) iron starvation, (-P) phosphorus starvation, (DK) darkness, (DC) DCMU, (DB) DBMIB.

    Article Snippet: A volume of extract containing 750 μg of protein was mixed with 40 μL of immunoprecipitation buffer (20 mM Tris-HCl, pH 7.5, 1% Triton X-100, 150 mM NaCl, 10% glycerol, 1 mM Na3 VO4 , 50 mM NaF, 2 mM EDTA, 1 mM PMSF) with protein G Sepharose (GE Healthcare) and 6 μg of the Synechocystis anti-GS antibodies, incubated at 4°C overnight with rotation.

    Techniques: Immunoprecipitation, Incubation