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  • 99
    Thermo Fisher nacl
    pH response of purified pHlash protein in vitro (A) <t>SDS-PAGE</t> gel of purified His-tagged pHlash protein stained with Coomassie Blue dye. Leftmost lane is molecular weight standards with KDa indicated, while the other lanes are the purified pHlash protein loaded at 0.2, 1, and 2 μg per lane. (B ) Construct of the pHlash fusion protein. Rluc8 was linked to cpVenus by the sequence Ala-Glu-Leu. (C ) Raw data (not normalized) of luminescence emission spectra of purified pHlash protein with 10 μM native coelenterazine at different pH values (pH 5.4-9.0) in 50 mM BIS-Tris-propane, 100 mM KCl, and 100 mM <t>NaCl.</t> (D) Normalized luminescence emission spectra of pHlash measured as in panel C. Luminescence intensity was normalized to the peak at 475 nm. (E) The BRET ratio (luminescence at 525nm:475 nm) as a function of pH is shown for pHlash in vitro . Error bars are +/- S.D., but in most cases the error bars are so small that they are obscured by the symbols (n = 3).
    Nacl, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 14348 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore m nacl
    pH response of purified pHlash protein in vitro (A) <t>SDS-PAGE</t> gel of purified His-tagged pHlash protein stained with Coomassie Blue dye. Leftmost lane is molecular weight standards with KDa indicated, while the other lanes are the purified pHlash protein loaded at 0.2, 1, and 2 μg per lane. (B ) Construct of the pHlash fusion protein. Rluc8 was linked to cpVenus by the sequence Ala-Glu-Leu. (C ) Raw data (not normalized) of luminescence emission spectra of purified pHlash protein with 10 μM native coelenterazine at different pH values (pH 5.4-9.0) in 50 mM BIS-Tris-propane, 100 mM KCl, and 100 mM <t>NaCl.</t> (D) Normalized luminescence emission spectra of pHlash measured as in panel C. Luminescence intensity was normalized to the peak at 475 nm. (E) The BRET ratio (luminescence at 525nm:475 nm) as a function of pH is shown for pHlash in vitro . Error bars are +/- S.D., but in most cases the error bars are so small that they are obscured by the symbols (n = 3).
    M Nacl, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 10213 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    FUJIFILM m nacl
    pH response of purified pHlash protein in vitro (A) <t>SDS-PAGE</t> gel of purified His-tagged pHlash protein stained with Coomassie Blue dye. Leftmost lane is molecular weight standards with KDa indicated, while the other lanes are the purified pHlash protein loaded at 0.2, 1, and 2 μg per lane. (B ) Construct of the pHlash fusion protein. Rluc8 was linked to cpVenus by the sequence Ala-Glu-Leu. (C ) Raw data (not normalized) of luminescence emission spectra of purified pHlash protein with 10 μM native coelenterazine at different pH values (pH 5.4-9.0) in 50 mM BIS-Tris-propane, 100 mM KCl, and 100 mM <t>NaCl.</t> (D) Normalized luminescence emission spectra of pHlash measured as in panel C. Luminescence intensity was normalized to the peak at 475 nm. (E) The BRET ratio (luminescence at 525nm:475 nm) as a function of pH is shown for pHlash in vitro . Error bars are +/- S.D., but in most cases the error bars are so small that they are obscured by the symbols (n = 3).
    M Nacl, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 92/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Fisher Scientific m nacl
    pH response of purified pHlash protein in vitro (A) <t>SDS-PAGE</t> gel of purified His-tagged pHlash protein stained with Coomassie Blue dye. Leftmost lane is molecular weight standards with KDa indicated, while the other lanes are the purified pHlash protein loaded at 0.2, 1, and 2 μg per lane. (B ) Construct of the pHlash fusion protein. Rluc8 was linked to cpVenus by the sequence Ala-Glu-Leu. (C ) Raw data (not normalized) of luminescence emission spectra of purified pHlash protein with 10 μM native coelenterazine at different pH values (pH 5.4-9.0) in 50 mM BIS-Tris-propane, 100 mM KCl, and 100 mM <t>NaCl.</t> (D) Normalized luminescence emission spectra of pHlash measured as in panel C. Luminescence intensity was normalized to the peak at 475 nm. (E) The BRET ratio (luminescence at 525nm:475 nm) as a function of pH is shown for pHlash in vitro . Error bars are +/- S.D., but in most cases the error bars are so small that they are obscured by the symbols (n = 3).
    M Nacl, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 92/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck KGaA m nacl
    pH response of purified pHlash protein in vitro (A) <t>SDS-PAGE</t> gel of purified His-tagged pHlash protein stained with Coomassie Blue dye. Leftmost lane is molecular weight standards with KDa indicated, while the other lanes are the purified pHlash protein loaded at 0.2, 1, and 2 μg per lane. (B ) Construct of the pHlash fusion protein. Rluc8 was linked to cpVenus by the sequence Ala-Glu-Leu. (C ) Raw data (not normalized) of luminescence emission spectra of purified pHlash protein with 10 μM native coelenterazine at different pH values (pH 5.4-9.0) in 50 mM BIS-Tris-propane, 100 mM KCl, and 100 mM <t>NaCl.</t> (D) Normalized luminescence emission spectra of pHlash measured as in panel C. Luminescence intensity was normalized to the peak at 475 nm. (E) The BRET ratio (luminescence at 525nm:475 nm) as a function of pH is shown for pHlash in vitro . Error bars are +/- S.D., but in most cases the error bars are so small that they are obscured by the symbols (n = 3).
    M Nacl, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 92/100, based on 132 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher igg elution buffer 4 m nacl
    pH response of purified pHlash protein in vitro (A) <t>SDS-PAGE</t> gel of purified His-tagged pHlash protein stained with Coomassie Blue dye. Leftmost lane is molecular weight standards with KDa indicated, while the other lanes are the purified pHlash protein loaded at 0.2, 1, and 2 μg per lane. (B ) Construct of the pHlash fusion protein. Rluc8 was linked to cpVenus by the sequence Ala-Glu-Leu. (C ) Raw data (not normalized) of luminescence emission spectra of purified pHlash protein with 10 μM native coelenterazine at different pH values (pH 5.4-9.0) in 50 mM BIS-Tris-propane, 100 mM KCl, and 100 mM <t>NaCl.</t> (D) Normalized luminescence emission spectra of pHlash measured as in panel C. Luminescence intensity was normalized to the peak at 475 nm. (E) The BRET ratio (luminescence at 525nm:475 nm) as a function of pH is shown for pHlash in vitro . Error bars are +/- S.D., but in most cases the error bars are so small that they are obscured by the symbols (n = 3).
    Igg Elution Buffer 4 M Nacl, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bio-Rad m nacl
    pH response of purified pHlash protein in vitro (A) <t>SDS-PAGE</t> gel of purified His-tagged pHlash protein stained with Coomassie Blue dye. Leftmost lane is molecular weight standards with KDa indicated, while the other lanes are the purified pHlash protein loaded at 0.2, 1, and 2 μg per lane. (B ) Construct of the pHlash fusion protein. Rluc8 was linked to cpVenus by the sequence Ala-Glu-Leu. (C ) Raw data (not normalized) of luminescence emission spectra of purified pHlash protein with 10 μM native coelenterazine at different pH values (pH 5.4-9.0) in 50 mM BIS-Tris-propane, 100 mM KCl, and 100 mM <t>NaCl.</t> (D) Normalized luminescence emission spectra of pHlash measured as in panel C. Luminescence intensity was normalized to the peak at 475 nm. (E) The BRET ratio (luminescence at 525nm:475 nm) as a function of pH is shown for pHlash in vitro . Error bars are +/- S.D., but in most cases the error bars are so small that they are obscured by the symbols (n = 3).
    M Nacl, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 585 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Carl Roth GmbH m nacl
    pH response of purified pHlash protein in vitro (A) <t>SDS-PAGE</t> gel of purified His-tagged pHlash protein stained with Coomassie Blue dye. Leftmost lane is molecular weight standards with KDa indicated, while the other lanes are the purified pHlash protein loaded at 0.2, 1, and 2 μg per lane. (B ) Construct of the pHlash fusion protein. Rluc8 was linked to cpVenus by the sequence Ala-Glu-Leu. (C ) Raw data (not normalized) of luminescence emission spectra of purified pHlash protein with 10 μM native coelenterazine at different pH values (pH 5.4-9.0) in 50 mM BIS-Tris-propane, 100 mM KCl, and 100 mM <t>NaCl.</t> (D) Normalized luminescence emission spectra of pHlash measured as in panel C. Luminescence intensity was normalized to the peak at 475 nm. (E) The BRET ratio (luminescence at 525nm:475 nm) as a function of pH is shown for pHlash in vitro . Error bars are +/- S.D., but in most cases the error bars are so small that they are obscured by the symbols (n = 3).
    M Nacl, supplied by Carl Roth GmbH, used in various techniques. Bioz Stars score: 92/100, based on 79 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare m nacl
    Binding of M. jannaschii FlaH to immobilized ATP. 10 μg of FlaH were incubated with 20 μL of ATP‐agarose in 20 m M <t>HEPES,</t> pH 8.0, 100 m M <t>NaCl,</t> 5 m M MgCl 2 for 2 h at 30°C. Samples were analyzed by SDS‐PAGE. 1, loaded protein; 2, supernatant after incubation; 3, ATP elution; 4, elution with SDS‐PAAG loading buffer. Agarose was used as a blank control.
    M Nacl, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 5281 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck & Co m nacl
    Binding of M. jannaschii FlaH to immobilized ATP. 10 μg of FlaH were incubated with 20 μL of ATP‐agarose in 20 m M <t>HEPES,</t> pH 8.0, 100 m M <t>NaCl,</t> 5 m M MgCl 2 for 2 h at 30°C. Samples were analyzed by SDS‐PAGE. 1, loaded protein; 2, supernatant after incubation; 3, ATP elution; 4, elution with SDS‐PAAG loading buffer. Agarose was used as a blank control.
    M Nacl, supplied by Merck & Co, used in various techniques. Bioz Stars score: 92/100, based on 89 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Bioanalytical Systems ag agcl 3 m nacl reference electrode
    Binding of M. jannaschii FlaH to immobilized ATP. 10 μg of FlaH were incubated with 20 μL of ATP‐agarose in 20 m M <t>HEPES,</t> pH 8.0, 100 m M <t>NaCl,</t> 5 m M MgCl 2 for 2 h at 30°C. Samples were analyzed by SDS‐PAGE. 1, loaded protein; 2, supernatant after incubation; 3, ATP elution; 4, elution with SDS‐PAAG loading buffer. Agarose was used as a blank control.
    Ag Agcl 3 M Nacl Reference Electrode, supplied by Bioanalytical Systems, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore protease inhibitor cocktail
    Binding of M. jannaschii FlaH to immobilized ATP. 10 μg of FlaH were incubated with 20 μL of ATP‐agarose in 20 m M <t>HEPES,</t> pH 8.0, 100 m M <t>NaCl,</t> 5 m M MgCl 2 for 2 h at 30°C. Samples were analyzed by SDS‐PAGE. 1, loaded protein; 2, supernatant after incubation; 3, ATP elution; 4, elution with SDS‐PAAG loading buffer. Agarose was used as a blank control.
    Protease Inhibitor Cocktail, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 134786 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher m nacl dynabeads protein g
    Binding of M. jannaschii FlaH to immobilized ATP. 10 μg of FlaH were incubated with 20 μL of ATP‐agarose in 20 m M <t>HEPES,</t> pH 8.0, 100 m M <t>NaCl,</t> 5 m M MgCl 2 for 2 h at 30°C. Samples were analyzed by SDS‐PAGE. 1, loaded protein; 2, supernatant after incubation; 3, ATP elution; 4, elution with SDS‐PAAG loading buffer. Agarose was used as a blank control.
    M Nacl Dynabeads Protein G, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Applichem m nacl
    Binding of M. jannaschii FlaH to immobilized ATP. 10 μg of FlaH were incubated with 20 μL of ATP‐agarose in 20 m M <t>HEPES,</t> pH 8.0, 100 m M <t>NaCl,</t> 5 m M MgCl 2 for 2 h at 30°C. Samples were analyzed by SDS‐PAGE. 1, loaded protein; 2, supernatant after incubation; 3, ATP elution; 4, elution with SDS‐PAAG loading buffer. Agarose was used as a blank control.
    M Nacl, supplied by Applichem, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Avantor m nacl
    Binding of M. jannaschii FlaH to immobilized ATP. 10 μg of FlaH were incubated with 20 μL of ATP‐agarose in 20 m M <t>HEPES,</t> pH 8.0, 100 m M <t>NaCl,</t> 5 m M MgCl 2 for 2 h at 30°C. Samples were analyzed by SDS‐PAGE. 1, loaded protein; 2, supernatant after incubation; 3, ATP elution; 4, elution with SDS‐PAAG loading buffer. Agarose was used as a blank control.
    M Nacl, supplied by Avantor, used in various techniques. Bioz Stars score: 92/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cellgro m nacl
    Binding of M. jannaschii FlaH to immobilized ATP. 10 μg of FlaH were incubated with 20 μL of ATP‐agarose in 20 m M <t>HEPES,</t> pH 8.0, 100 m M <t>NaCl,</t> 5 m M MgCl 2 for 2 h at 30°C. Samples were analyzed by SDS‐PAGE. 1, loaded protein; 2, supernatant after incubation; 3, ATP elution; 4, elution with SDS‐PAAG loading buffer. Agarose was used as a blank control.
    M Nacl, supplied by Cellgro, used in various techniques. Bioz Stars score: 92/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    pH response of purified pHlash protein in vitro (A) SDS-PAGE gel of purified His-tagged pHlash protein stained with Coomassie Blue dye. Leftmost lane is molecular weight standards with KDa indicated, while the other lanes are the purified pHlash protein loaded at 0.2, 1, and 2 μg per lane. (B ) Construct of the pHlash fusion protein. Rluc8 was linked to cpVenus by the sequence Ala-Glu-Leu. (C ) Raw data (not normalized) of luminescence emission spectra of purified pHlash protein with 10 μM native coelenterazine at different pH values (pH 5.4-9.0) in 50 mM BIS-Tris-propane, 100 mM KCl, and 100 mM NaCl. (D) Normalized luminescence emission spectra of pHlash measured as in panel C. Luminescence intensity was normalized to the peak at 475 nm. (E) The BRET ratio (luminescence at 525nm:475 nm) as a function of pH is shown for pHlash in vitro . Error bars are +/- S.D., but in most cases the error bars are so small that they are obscured by the symbols (n = 3).

    Journal: Methods in molecular biology (Clifton, N.J.)

    Article Title: Monitoring Intracellular pH change with a Genetically Encoded and Ratiometric Luminescence Sensor in Yeast and Mammalian Cells

    doi: 10.1007/978-1-4939-3813-1_9

    Figure Lengend Snippet: pH response of purified pHlash protein in vitro (A) SDS-PAGE gel of purified His-tagged pHlash protein stained with Coomassie Blue dye. Leftmost lane is molecular weight standards with KDa indicated, while the other lanes are the purified pHlash protein loaded at 0.2, 1, and 2 μg per lane. (B ) Construct of the pHlash fusion protein. Rluc8 was linked to cpVenus by the sequence Ala-Glu-Leu. (C ) Raw data (not normalized) of luminescence emission spectra of purified pHlash protein with 10 μM native coelenterazine at different pH values (pH 5.4-9.0) in 50 mM BIS-Tris-propane, 100 mM KCl, and 100 mM NaCl. (D) Normalized luminescence emission spectra of pHlash measured as in panel C. Luminescence intensity was normalized to the peak at 475 nm. (E) The BRET ratio (luminescence at 525nm:475 nm) as a function of pH is shown for pHlash in vitro . Error bars are +/- S.D., but in most cases the error bars are so small that they are obscured by the symbols (n = 3).

    Article Snippet: 50-mL flask and 2-L flask LB medium with ampicillin (60 μg/mL) TALON metal affinity resin (Clontech) Equilibration/Wash buffer: 50 mM sodium phosphate, 300 mM NaCl, pH 7.0 Elution buffer: 50 mM sodium phosphate, 300 mM NaCl, 150 mM imidazole, pH 7.0 10% SDS-PAGE gel Dialysis cassette (20K MWCO) (Thermo Scientific) Dialysis buffer: 30 mM MOPS, 5% Glycerol, pH 7.2 BSA standard solution and Protein Assay Dye Reagent Concentrate (Bio-Rad)

    Techniques: Purification, In Vitro, SDS Page, Staining, Molecular Weight, Construct, Sequencing, Bioluminescence Resonance Energy Transfer

    CaM directly interacts with DR5 in DR5 death domain in a Ca 2+ -dependent manner. A , CaM pull-down of purified DR5 cytoplasmic region (DR5 CR) and DR5 death domain (DR5 DD) in a 50 m m Tris, pH 7.6, 120 m m NaCl, 1% Brij buffer with 1 m m Ca 2+ , or 2 m m EGTA.

    Journal: The Journal of Biological Chemistry

    Article Title: Characterization of the Interactions between Calmodulin and Death Receptor 5 in Triple-negative and Estrogen Receptor-positive Breast Cancer Cells

    doi: 10.1074/jbc.M116.727727

    Figure Lengend Snippet: CaM directly interacts with DR5 in DR5 death domain in a Ca 2+ -dependent manner. A , CaM pull-down of purified DR5 cytoplasmic region (DR5 CR) and DR5 death domain (DR5 DD) in a 50 m m Tris, pH 7.6, 120 m m NaCl, 1% Brij buffer with 1 m m Ca 2+ , or 2 m m EGTA.

    Article Snippet: ER-positive or triple-negative breast cancer cells were lysed using a 50 m m Tris-HCL pH 7.5, 150 m m NaCl, 1% Triton X-100, and 1:100 Halt protease inhibitor (Thermo Fisher Scientific, Waltham, MA) buffer at 4 °C for 30 min.

    Techniques: Chick Chorioallantoic Membrane Assay, Purification

    DNA/PEI ratio affects the particle size of PEI–DNA complexes and transfection efficiency in CHO-S cells a DNA and different amounts of PEI were diluted in 300 mM NaCl solution. After incubating for different times (5, 10, 30, 60, and 120 min),

    Journal: Cytotechnology

    Article Title: Salt ions and related parameters affect PEI–DNA particle size and transfection efficiency in Chinese hamster ovary cells

    doi: 10.1007/s10616-013-9658-z

    Figure Lengend Snippet: DNA/PEI ratio affects the particle size of PEI–DNA complexes and transfection efficiency in CHO-S cells a DNA and different amounts of PEI were diluted in 300 mM NaCl solution. After incubating for different times (5, 10, 30, 60, and 120 min),

    Article Snippet: To examine the effects of the culture medium on the stability of PEI–DNA complexes, DNA/PEI (1:4) was diluted in 300 mM NaCl solution, and then basic medium (DMEM, Gibco) was added after incubation.

    Techniques: Transfection

    Stability of PEI–DNA complexes in culture medium. DNA/PEI (1:4) was diluted in 300 mM NaCl solution, and then basic medium was added. The particle size of PEI–DNA complexes was measured at different time intervals (0, 5, 10, 30,

    Journal: Cytotechnology

    Article Title: Salt ions and related parameters affect PEI–DNA particle size and transfection efficiency in Chinese hamster ovary cells

    doi: 10.1007/s10616-013-9658-z

    Figure Lengend Snippet: Stability of PEI–DNA complexes in culture medium. DNA/PEI (1:4) was diluted in 300 mM NaCl solution, and then basic medium was added. The particle size of PEI–DNA complexes was measured at different time intervals (0, 5, 10, 30,

    Article Snippet: To examine the effects of the culture medium on the stability of PEI–DNA complexes, DNA/PEI (1:4) was diluted in 300 mM NaCl solution, and then basic medium (DMEM, Gibco) was added after incubation.

    Techniques:

    Longer incubation time increases particle size and decreases transfection efficiency a The DNA-PEI complexes (DNA/PEI = 1:4) was incubated in 300 mM NaCl for different times. The particle sizes of PEI–DNA complexes increased

    Journal: Cytotechnology

    Article Title: Salt ions and related parameters affect PEI–DNA particle size and transfection efficiency in Chinese hamster ovary cells

    doi: 10.1007/s10616-013-9658-z

    Figure Lengend Snippet: Longer incubation time increases particle size and decreases transfection efficiency a The DNA-PEI complexes (DNA/PEI = 1:4) was incubated in 300 mM NaCl for different times. The particle sizes of PEI–DNA complexes increased

    Article Snippet: To examine the effects of the culture medium on the stability of PEI–DNA complexes, DNA/PEI (1:4) was diluted in 300 mM NaCl solution, and then basic medium (DMEM, Gibco) was added after incubation.

    Techniques: Incubation, Transfection

    NaCl increases the particle size of PEI–DNA complexes and transfection efficiency a DNA and PEI were diluted with different concentrations of NaCl solution (0, 150, 300, and 600 mM NaCl). The particle size of PEI–DNA complexes

    Journal: Cytotechnology

    Article Title: Salt ions and related parameters affect PEI–DNA particle size and transfection efficiency in Chinese hamster ovary cells

    doi: 10.1007/s10616-013-9658-z

    Figure Lengend Snippet: NaCl increases the particle size of PEI–DNA complexes and transfection efficiency a DNA and PEI were diluted with different concentrations of NaCl solution (0, 150, 300, and 600 mM NaCl). The particle size of PEI–DNA complexes

    Article Snippet: To examine the effects of the culture medium on the stability of PEI–DNA complexes, DNA/PEI (1:4) was diluted in 300 mM NaCl solution, and then basic medium (DMEM, Gibco) was added after incubation.

    Techniques: Transfection

    P 12 /T 26 as a substrate for nucleotide incorporation catalyzed by NS5pol. A , the primer/template double-stranded RNA, P 12 /T 26 is shown. B , shown is a single nucleotide primer extension assay without enzyme-RNA preincubation. The reaction was initiated at 37 °C by the addition of NS5pol (0.6 μ m ) to a mixture containing P 12 /T 26 (0.5 μ m ) and GTP (0.5 m m ) in the reaction buffer (40 m m Tris-Cl, pH 7.4, 23.8 m m NaCl, 3 m m DTT, 15% glycerol, and 2 m m MgCl 2 ); aliquots of the reaction were quenched by a formamide-EDTA solution at the indicated times. The samples were resolved on a 16% denaturing polyacrylamide gel. C , shown is the time course of 13-mer product formation from the experiment described in B . The data were fit to a single exponential, yielding a rate of 0.00110 ± 0.00003 s −1 and an amplitude of 0.460 ± 0.005 μ m .

    Journal: The Journal of Biological Chemistry

    Article Title: Characterization of the Elongation Complex of Dengue Virus RNA Polymerase

    doi: 10.1074/jbc.M110.162685

    Figure Lengend Snippet: P 12 /T 26 as a substrate for nucleotide incorporation catalyzed by NS5pol. A , the primer/template double-stranded RNA, P 12 /T 26 is shown. B , shown is a single nucleotide primer extension assay without enzyme-RNA preincubation. The reaction was initiated at 37 °C by the addition of NS5pol (0.6 μ m ) to a mixture containing P 12 /T 26 (0.5 μ m ) and GTP (0.5 m m ) in the reaction buffer (40 m m Tris-Cl, pH 7.4, 23.8 m m NaCl, 3 m m DTT, 15% glycerol, and 2 m m MgCl 2 ); aliquots of the reaction were quenched by a formamide-EDTA solution at the indicated times. The samples were resolved on a 16% denaturing polyacrylamide gel. C , shown is the time course of 13-mer product formation from the experiment described in B . The data were fit to a single exponential, yielding a rate of 0.00110 ± 0.00003 s −1 and an amplitude of 0.460 ± 0.005 μ m .

    Article Snippet: MgCl2 , EDTA, NaCl solutions, and Tris-Cl buffers were purchased from Ambion (Austin, TX).

    Techniques: Primer Extension Assay

    miRNA expression analysis using Affymetrix chip. RNA samples were isolated from Thellungiella roots and leaves at 0 h, 3 h, 9 h, and 24 h treated with 200 mM NaCl. Bars represent the standard deviations of three replicates. (A) miR156a. (B) miR156k. (C) miR160a. (D) miR162a. (E) miR64a. (F) miR168a. (G) miR171c. (H) miR395a. (I) miR395b. (J) miR824. Duration of NaCl treatment (h) .

    Journal: BMC Plant Biology

    Article Title: Genome-wide identification of Thellungiella salsuginea microRNAs with putative roles in the salt stress response

    doi: 10.1186/1471-2229-13-180

    Figure Lengend Snippet: miRNA expression analysis using Affymetrix chip. RNA samples were isolated from Thellungiella roots and leaves at 0 h, 3 h, 9 h, and 24 h treated with 200 mM NaCl. Bars represent the standard deviations of three replicates. (A) miR156a. (B) miR156k. (C) miR160a. (D) miR162a. (E) miR64a. (F) miR168a. (G) miR171c. (H) miR395a. (I) miR395b. (J) miR824. Duration of NaCl treatment (h) .

    Article Snippet: Expression analysis of miRNAs by microarray and qRT-PCR analysis The expression of some conserved miRNAs in leaves and roots was examined in the presence or absence of NaCl treatment using an Affymetrix miRNA chip.

    Techniques: Expressing, Chromatin Immunoprecipitation, Isolation

    Relative expression of miRNAs as determined by stem-loop qRT-PCR. Total RNA isolated from control seedlings and those treated with 200 mM NaCl. The reverse transcription reaction was carried out using stem-loop primers (Additional file 9 : Table S9) of these miRNAs. The level of expression was normalized to that of U6. The normalized miRNA levels in the control were arbitrarily set to 1. Error bars indicate ± SE obtained from three biological repeats. Student’s T -test was performed to analyze the changes in the gene expression after treated with NaCl. **denotes the p value

    Journal: BMC Plant Biology

    Article Title: Genome-wide identification of Thellungiella salsuginea microRNAs with putative roles in the salt stress response

    doi: 10.1186/1471-2229-13-180

    Figure Lengend Snippet: Relative expression of miRNAs as determined by stem-loop qRT-PCR. Total RNA isolated from control seedlings and those treated with 200 mM NaCl. The reverse transcription reaction was carried out using stem-loop primers (Additional file 9 : Table S9) of these miRNAs. The level of expression was normalized to that of U6. The normalized miRNA levels in the control were arbitrarily set to 1. Error bars indicate ± SE obtained from three biological repeats. Student’s T -test was performed to analyze the changes in the gene expression after treated with NaCl. **denotes the p value

    Article Snippet: Expression analysis of miRNAs by microarray and qRT-PCR analysis The expression of some conserved miRNAs in leaves and roots was examined in the presence or absence of NaCl treatment using an Affymetrix miRNA chip.

    Techniques: Expressing, Quantitative RT-PCR, Isolation

    Binding of M. jannaschii FlaH to immobilized ATP. 10 μg of FlaH were incubated with 20 μL of ATP‐agarose in 20 m M HEPES, pH 8.0, 100 m M NaCl, 5 m M MgCl 2 for 2 h at 30°C. Samples were analyzed by SDS‐PAGE. 1, loaded protein; 2, supernatant after incubation; 3, ATP elution; 4, elution with SDS‐PAAG loading buffer. Agarose was used as a blank control.

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly

    doi: 10.1002/pro.2932

    Figure Lengend Snippet: Binding of M. jannaschii FlaH to immobilized ATP. 10 μg of FlaH were incubated with 20 μL of ATP‐agarose in 20 m M HEPES, pH 8.0, 100 m M NaCl, 5 m M MgCl 2 for 2 h at 30°C. Samples were analyzed by SDS‐PAGE. 1, loaded protein; 2, supernatant after incubation; 3, ATP elution; 4, elution with SDS‐PAAG loading buffer. Agarose was used as a blank control.

    Article Snippet: Eluted protein was dialyzed against 40 m M HEPES, pH 8.0, 50 m M NaCl, and applied to a Mono Q column (GE Healthcare) equilibrated with the same buffer.

    Techniques: Binding Assay, Incubation, SDS Page