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  • 96
    Thermo Fisher dnapac pa 100 strong anion exchange column
    Dnapac Pa 100 Strong Anion Exchange Column, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Beckman Coulter strong anion exchange hplc
    Phosphorylation of CPV and <t>GCV</t> by pUL97. The time-dependent formation of CPV-MP was determined by UV absorption of the <t>HPLC</t> effluent; that of GCV-MP was measured by liquid scintillation spectrometry. The boxed inset illustrates the time-dependent increase of GCV-MP only. The values represent the means ± standard deviations from at least two experiments.
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    METTLER TOLEDO strong anion exchange hplc
    Phosphorylation of CPV and <t>GCV</t> by pUL97. The time-dependent formation of CPV-MP was determined by UV absorption of the <t>HPLC</t> effluent; that of GCV-MP was measured by liquid scintillation spectrometry. The boxed inset illustrates the time-dependent increase of GCV-MP only. The values represent the means ± standard deviations from at least two experiments.
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    METTLER TOLEDO strong anion exchange hplc column
    Phosphorylation of CPV and <t>GCV</t> by pUL97. The time-dependent formation of CPV-MP was determined by UV absorption of the <t>HPLC</t> effluent; that of GCV-MP was measured by liquid scintillation spectrometry. The boxed inset illustrates the time-dependent increase of GCV-MP only. The values represent the means ± standard deviations from at least two experiments.
    Strong Anion Exchange Hplc Column, supplied by METTLER TOLEDO, used in various techniques. Bioz Stars score: 80/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher strong anion exchange chromatography hplc
    Phosphorylation of CPV and <t>GCV</t> by pUL97. The time-dependent formation of CPV-MP was determined by UV absorption of the <t>HPLC</t> effluent; that of GCV-MP was measured by liquid scintillation spectrometry. The boxed inset illustrates the time-dependent increase of GCV-MP only. The values represent the means ± standard deviations from at least two experiments.
    Strong Anion Exchange Chromatography Hplc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare strong anion exchange hplc
    Anion-exchange <t>HPLC</t> of 3 H-labeled disaccharides. Disaccharides generated by deamination/radiolabeling according to Protocol A ( A ) or Protocol B ( B ) were analyzed by anion-exchange HPLC on a <t>Partisil</t> 10 SAX column. C , end-labeled, N -sulfated oligosaccharides
    Strong Anion Exchange Hplc, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 91/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies strong anion exchange hplc
    Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 <t>-methyl-AMP</t> (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via <t>HPLC.</t> The values represent the mean ± standard deviation from at least three experiments.
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    Waters Corporation semi preparative strong anion exchange sax hplc
    Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 <t>-methyl-AMP</t> (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via <t>HPLC.</t> The values represent the mean ± standard deviation from at least three experiments.
    Semi Preparative Strong Anion Exchange Sax Hplc, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Waters Corporation strong anion exchange hplc
    Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 <t>-methyl-AMP</t> (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via <t>HPLC.</t> The values represent the mean ± standard deviation from at least three experiments.
    Strong Anion Exchange Hplc, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 88/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare strong anion exchange hplc column
    Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 <t>-methyl-AMP</t> (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via <t>HPLC.</t> The values represent the mean ± standard deviation from at least three experiments.
    Strong Anion Exchange Hplc Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 80/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher strong anion exchange sax hplc
    Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 <t>-methyl-AMP</t> (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via <t>HPLC.</t> The values represent the mean ± standard deviation from at least three experiments.
    Strong Anion Exchange Sax Hplc, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    KNAUER Wissenschaftliche strong anion exchange hplc separation
    Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 <t>-methyl-AMP</t> (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via <t>HPLC.</t> The values represent the mean ± standard deviation from at least three experiments.
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    Hichrom Limited strong anion exchange chromatography hplc
    Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 <t>-methyl-AMP</t> (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via <t>HPLC.</t> The values represent the mean ± standard deviation from at least three experiments.
    Strong Anion Exchange Chromatography Hplc, supplied by Hichrom Limited, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare strong anion exchange chromatography hplc
    VIH1 and VIH2 Are Functional Vip1-Type PPIP5 Kinases. (A) and (B) Structural model of the VIH2 ATP-grasp kinase domain (left) and the hPPIP5K2 ATP-grasp kinase domain (PDB ID: 3T9D, right) depicting the 5-InsP 7 binding sites and key catalytic residues. Residues coordinating substrate via polar contacts are shown as sticks, polar interactions are highlighted by dashed lines, α-helices are rendered in blue, β-sheets in orange, substrate (5-InsP 7 ) is rendered in magenta, and Mg 2+ ions are presented as green spheres. Three carbon atoms on the inositol ring are numbered. The ATP analog AMP-PNP (in [B] ) is depicted with gray carbon and orange and red phosphate groups. (C) and (D) Complementation of vip1 Δ-associated growth defects in yeast by ectopic expression of inositol pyrophosphate synthetases. The vip1 Δ yeast strain transformed with episomal pDR195( URA3 ) plasmids carrying either VIP1 , VIH1 , or VIH2 , sequences encoding their respective ATP-grasp kinase domains ( KD ) or designated kinase domain mutants, or carrying KCS1 were spotted in 8-fold serial dilutions onto uracil-free minimal medium in presence or absence of 6-azauracil, as indicated. Rescue on medium supplemented with 6-azauracil (right) reports Vip1 activity. (E) and (F) Normalized <t>HPLC</t> profiles of inositol phosphates of extracts from designated [ 3 H] inositol-labeled yeast transformants. Extracts were resolved by <t>Partisphere</t> SAX HPLC and fractions collected each minute for subsequent determination of radioactivity as indicated. Changes in elution times in independent experiments were observed and can be explained by subtle changes in column properties or column change. Experiments were repeated three times with similar results. (G) Complementation assays of kcs1 Δ-associated growth defects on high salt by ectopic expression inositol pyrophosphate synthetases. Wild-type (wt) or kcs1 Δ yeast transformants (both DDY1810 background) carrying designated plasmids were spotted in 8-fold serial dilutions onto solid minimal media (MM, uracil deficient CSM media with YNB and appropriate supplements) in presence or absence of NaCl and onto solid YPDA media incubated at 37°C.
    Strong Anion Exchange Chromatography Hplc, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare partisphere sax strong anion exchange hplc column
    VIH1 and VIH2 Are Functional Vip1-Type PPIP5 Kinases. (A) and (B) Structural model of the VIH2 ATP-grasp kinase domain (left) and the hPPIP5K2 ATP-grasp kinase domain (PDB ID: 3T9D, right) depicting the 5-InsP 7 binding sites and key catalytic residues. Residues coordinating substrate via polar contacts are shown as sticks, polar interactions are highlighted by dashed lines, α-helices are rendered in blue, β-sheets in orange, substrate (5-InsP 7 ) is rendered in magenta, and Mg 2+ ions are presented as green spheres. Three carbon atoms on the inositol ring are numbered. The ATP analog AMP-PNP (in [B] ) is depicted with gray carbon and orange and red phosphate groups. (C) and (D) Complementation of vip1 Δ-associated growth defects in yeast by ectopic expression of inositol pyrophosphate synthetases. The vip1 Δ yeast strain transformed with episomal pDR195( URA3 ) plasmids carrying either VIP1 , VIH1 , or VIH2 , sequences encoding their respective ATP-grasp kinase domains ( KD ) or designated kinase domain mutants, or carrying KCS1 were spotted in 8-fold serial dilutions onto uracil-free minimal medium in presence or absence of 6-azauracil, as indicated. Rescue on medium supplemented with 6-azauracil (right) reports Vip1 activity. (E) and (F) Normalized <t>HPLC</t> profiles of inositol phosphates of extracts from designated [ 3 H] inositol-labeled yeast transformants. Extracts were resolved by <t>Partisphere</t> SAX HPLC and fractions collected each minute for subsequent determination of radioactivity as indicated. Changes in elution times in independent experiments were observed and can be explained by subtle changes in column properties or column change. Experiments were repeated three times with similar results. (G) Complementation assays of kcs1 Δ-associated growth defects on high salt by ectopic expression inositol pyrophosphate synthetases. Wild-type (wt) or kcs1 Δ yeast transformants (both DDY1810 background) carrying designated plasmids were spotted in 8-fold serial dilutions onto solid minimal media (MM, uracil deficient CSM media with YNB and appropriate supplements) in presence or absence of NaCl and onto solid YPDA media incubated at 37°C.
    Partisphere Sax Strong Anion Exchange Hplc Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Agilent technologies strong anion exchange bio monolith qa hplc column
    VIH1 and VIH2 Are Functional Vip1-Type PPIP5 Kinases. (A) and (B) Structural model of the VIH2 ATP-grasp kinase domain (left) and the hPPIP5K2 ATP-grasp kinase domain (PDB ID: 3T9D, right) depicting the 5-InsP 7 binding sites and key catalytic residues. Residues coordinating substrate via polar contacts are shown as sticks, polar interactions are highlighted by dashed lines, α-helices are rendered in blue, β-sheets in orange, substrate (5-InsP 7 ) is rendered in magenta, and Mg 2+ ions are presented as green spheres. Three carbon atoms on the inositol ring are numbered. The ATP analog AMP-PNP (in [B] ) is depicted with gray carbon and orange and red phosphate groups. (C) and (D) Complementation of vip1 Δ-associated growth defects in yeast by ectopic expression of inositol pyrophosphate synthetases. The vip1 Δ yeast strain transformed with episomal pDR195( URA3 ) plasmids carrying either VIP1 , VIH1 , or VIH2 , sequences encoding their respective ATP-grasp kinase domains ( KD ) or designated kinase domain mutants, or carrying KCS1 were spotted in 8-fold serial dilutions onto uracil-free minimal medium in presence or absence of 6-azauracil, as indicated. Rescue on medium supplemented with 6-azauracil (right) reports Vip1 activity. (E) and (F) Normalized <t>HPLC</t> profiles of inositol phosphates of extracts from designated [ 3 H] inositol-labeled yeast transformants. Extracts were resolved by <t>Partisphere</t> SAX HPLC and fractions collected each minute for subsequent determination of radioactivity as indicated. Changes in elution times in independent experiments were observed and can be explained by subtle changes in column properties or column change. Experiments were repeated three times with similar results. (G) Complementation assays of kcs1 Δ-associated growth defects on high salt by ectopic expression inositol pyrophosphate synthetases. Wild-type (wt) or kcs1 Δ yeast transformants (both DDY1810 background) carrying designated plasmids were spotted in 8-fold serial dilutions onto solid minimal media (MM, uracil deficient CSM media with YNB and appropriate supplements) in presence or absence of NaCl and onto solid YPDA media incubated at 37°C.
    Strong Anion Exchange Bio Monolith Qa Hplc Column, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare strong anion exchange partisil 10 sax
    VIH1 and VIH2 Are Functional Vip1-Type PPIP5 Kinases. (A) and (B) Structural model of the VIH2 ATP-grasp kinase domain (left) and the hPPIP5K2 ATP-grasp kinase domain (PDB ID: 3T9D, right) depicting the 5-InsP 7 binding sites and key catalytic residues. Residues coordinating substrate via polar contacts are shown as sticks, polar interactions are highlighted by dashed lines, α-helices are rendered in blue, β-sheets in orange, substrate (5-InsP 7 ) is rendered in magenta, and Mg 2+ ions are presented as green spheres. Three carbon atoms on the inositol ring are numbered. The ATP analog AMP-PNP (in [B] ) is depicted with gray carbon and orange and red phosphate groups. (C) and (D) Complementation of vip1 Δ-associated growth defects in yeast by ectopic expression of inositol pyrophosphate synthetases. The vip1 Δ yeast strain transformed with episomal pDR195( URA3 ) plasmids carrying either VIP1 , VIH1 , or VIH2 , sequences encoding their respective ATP-grasp kinase domains ( KD ) or designated kinase domain mutants, or carrying KCS1 were spotted in 8-fold serial dilutions onto uracil-free minimal medium in presence or absence of 6-azauracil, as indicated. Rescue on medium supplemented with 6-azauracil (right) reports Vip1 activity. (E) and (F) Normalized <t>HPLC</t> profiles of inositol phosphates of extracts from designated [ 3 H] inositol-labeled yeast transformants. Extracts were resolved by <t>Partisphere</t> SAX HPLC and fractions collected each minute for subsequent determination of radioactivity as indicated. Changes in elution times in independent experiments were observed and can be explained by subtle changes in column properties or column change. Experiments were repeated three times with similar results. (G) Complementation assays of kcs1 Δ-associated growth defects on high salt by ectopic expression inositol pyrophosphate synthetases. Wild-type (wt) or kcs1 Δ yeast transformants (both DDY1810 background) carrying designated plasmids were spotted in 8-fold serial dilutions onto solid minimal media (MM, uracil deficient CSM media with YNB and appropriate supplements) in presence or absence of NaCl and onto solid YPDA media incubated at 37°C.
    Strong Anion Exchange Partisil 10 Sax, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Waters Corporation 2695 hplc system
    VIH1 and VIH2 Are Functional Vip1-Type PPIP5 Kinases. (A) and (B) Structural model of the VIH2 ATP-grasp kinase domain (left) and the hPPIP5K2 ATP-grasp kinase domain (PDB ID: 3T9D, right) depicting the 5-InsP 7 binding sites and key catalytic residues. Residues coordinating substrate via polar contacts are shown as sticks, polar interactions are highlighted by dashed lines, α-helices are rendered in blue, β-sheets in orange, substrate (5-InsP 7 ) is rendered in magenta, and Mg 2+ ions are presented as green spheres. Three carbon atoms on the inositol ring are numbered. The ATP analog AMP-PNP (in [B] ) is depicted with gray carbon and orange and red phosphate groups. (C) and (D) Complementation of vip1 Δ-associated growth defects in yeast by ectopic expression of inositol pyrophosphate synthetases. The vip1 Δ yeast strain transformed with episomal pDR195( URA3 ) plasmids carrying either VIP1 , VIH1 , or VIH2 , sequences encoding their respective ATP-grasp kinase domains ( KD ) or designated kinase domain mutants, or carrying KCS1 were spotted in 8-fold serial dilutions onto uracil-free minimal medium in presence or absence of 6-azauracil, as indicated. Rescue on medium supplemented with 6-azauracil (right) reports Vip1 activity. (E) and (F) Normalized <t>HPLC</t> profiles of inositol phosphates of extracts from designated [ 3 H] inositol-labeled yeast transformants. Extracts were resolved by <t>Partisphere</t> SAX HPLC and fractions collected each minute for subsequent determination of radioactivity as indicated. Changes in elution times in independent experiments were observed and can be explained by subtle changes in column properties or column change. Experiments were repeated three times with similar results. (G) Complementation assays of kcs1 Δ-associated growth defects on high salt by ectopic expression inositol pyrophosphate synthetases. Wild-type (wt) or kcs1 Δ yeast transformants (both DDY1810 background) carrying designated plasmids were spotted in 8-fold serial dilutions onto solid minimal media (MM, uracil deficient CSM media with YNB and appropriate supplements) in presence or absence of NaCl and onto solid YPDA media incubated at 37°C.
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    GE Healthcare partisphere sax
    VIH1 and VIH2 Are Functional Vip1-Type PPIP5 Kinases. (A) and (B) Structural model of the VIH2 ATP-grasp kinase domain (left) and the hPPIP5K2 ATP-grasp kinase domain (PDB ID: 3T9D, right) depicting the 5-InsP 7 binding sites and key catalytic residues. Residues coordinating substrate via polar contacts are shown as sticks, polar interactions are highlighted by dashed lines, α-helices are rendered in blue, β-sheets in orange, substrate (5-InsP 7 ) is rendered in magenta, and Mg 2+ ions are presented as green spheres. Three carbon atoms on the inositol ring are numbered. The ATP analog AMP-PNP (in [B] ) is depicted with gray carbon and orange and red phosphate groups. (C) and (D) Complementation of vip1 Δ-associated growth defects in yeast by ectopic expression of inositol pyrophosphate synthetases. The vip1 Δ yeast strain transformed with episomal pDR195( URA3 ) plasmids carrying either VIP1 , VIH1 , or VIH2 , sequences encoding their respective ATP-grasp kinase domains ( KD ) or designated kinase domain mutants, or carrying KCS1 were spotted in 8-fold serial dilutions onto uracil-free minimal medium in presence or absence of 6-azauracil, as indicated. Rescue on medium supplemented with 6-azauracil (right) reports Vip1 activity. (E) and (F) Normalized <t>HPLC</t> profiles of inositol phosphates of extracts from designated [ 3 H] inositol-labeled yeast transformants. Extracts were resolved by <t>Partisphere</t> SAX HPLC and fractions collected each minute for subsequent determination of radioactivity as indicated. Changes in elution times in independent experiments were observed and can be explained by subtle changes in column properties or column change. Experiments were repeated three times with similar results. (G) Complementation assays of kcs1 Δ-associated growth defects on high salt by ectopic expression inositol pyrophosphate synthetases. Wild-type (wt) or kcs1 Δ yeast transformants (both DDY1810 background) carrying designated plasmids were spotted in 8-fold serial dilutions onto solid minimal media (MM, uracil deficient CSM media with YNB and appropriate supplements) in presence or absence of NaCl and onto solid YPDA media incubated at 37°C.
    Partisphere Sax, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Waters Corporation spherisorb s5 sax
    VIH1 and VIH2 Are Functional Vip1-Type PPIP5 Kinases. (A) and (B) Structural model of the VIH2 ATP-grasp kinase domain (left) and the hPPIP5K2 ATP-grasp kinase domain (PDB ID: 3T9D, right) depicting the 5-InsP 7 binding sites and key catalytic residues. Residues coordinating substrate via polar contacts are shown as sticks, polar interactions are highlighted by dashed lines, α-helices are rendered in blue, β-sheets in orange, substrate (5-InsP 7 ) is rendered in magenta, and Mg 2+ ions are presented as green spheres. Three carbon atoms on the inositol ring are numbered. The ATP analog AMP-PNP (in [B] ) is depicted with gray carbon and orange and red phosphate groups. (C) and (D) Complementation of vip1 Δ-associated growth defects in yeast by ectopic expression of inositol pyrophosphate synthetases. The vip1 Δ yeast strain transformed with episomal pDR195( URA3 ) plasmids carrying either VIP1 , VIH1 , or VIH2 , sequences encoding their respective ATP-grasp kinase domains ( KD ) or designated kinase domain mutants, or carrying KCS1 were spotted in 8-fold serial dilutions onto uracil-free minimal medium in presence or absence of 6-azauracil, as indicated. Rescue on medium supplemented with 6-azauracil (right) reports Vip1 activity. (E) and (F) Normalized <t>HPLC</t> profiles of inositol phosphates of extracts from designated [ 3 H] inositol-labeled yeast transformants. Extracts were resolved by <t>Partisphere</t> SAX HPLC and fractions collected each minute for subsequent determination of radioactivity as indicated. Changes in elution times in independent experiments were observed and can be explained by subtle changes in column properties or column change. Experiments were repeated three times with similar results. (G) Complementation assays of kcs1 Δ-associated growth defects on high salt by ectopic expression inositol pyrophosphate synthetases. Wild-type (wt) or kcs1 Δ yeast transformants (both DDY1810 background) carrying designated plasmids were spotted in 8-fold serial dilutions onto solid minimal media (MM, uracil deficient CSM media with YNB and appropriate supplements) in presence or absence of NaCl and onto solid YPDA media incubated at 37°C.
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    Phosphorylation of CPV and GCV by pUL97. The time-dependent formation of CPV-MP was determined by UV absorption of the HPLC effluent; that of GCV-MP was measured by liquid scintillation spectrometry. The boxed inset illustrates the time-dependent increase of GCV-MP only. The values represent the means ± standard deviations from at least two experiments.

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Stereoselective Phosphorylation of Cyclopropavir by pUL97 and Competitive Inhibition by Maribavir ▿

    doi: 10.1128/AAC.00468-10

    Figure Lengend Snippet: Phosphorylation of CPV and GCV by pUL97. The time-dependent formation of CPV-MP was determined by UV absorption of the HPLC effluent; that of GCV-MP was measured by liquid scintillation spectrometry. The boxed inset illustrates the time-dependent increase of GCV-MP only. The values represent the means ± standard deviations from at least two experiments.

    Article Snippet: GCV and GCV-MP were separated by strong-anion-exchange HPLC (Beckman Coulter [Fullerton, CA] System Gold programmable solvent module 125 and System Gold programmable detector module 166 controlled by 32 Karat software [version 7.0]).

    Techniques: High Performance Liquid Chromatography

    Anion-exchange HPLC of 3 H-labeled disaccharides. Disaccharides generated by deamination/radiolabeling according to Protocol A ( A ) or Protocol B ( B ) were analyzed by anion-exchange HPLC on a Partisil 10 SAX column. C , end-labeled, N -sulfated oligosaccharides

    Journal: The Journal of Biological Chemistry

    Article Title: Drosophila Heparan Sulfate, a Novel Design *

    doi: 10.1074/jbc.M112.350389

    Figure Lengend Snippet: Anion-exchange HPLC of 3 H-labeled disaccharides. Disaccharides generated by deamination/radiolabeling according to Protocol A ( A ) or Protocol B ( B ) were analyzed by anion-exchange HPLC on a Partisil 10 SAX column. C , end-labeled, N -sulfated oligosaccharides

    Article Snippet: The compositions of labeled disaccharides obtained by either Protocol A or B were determined by strong anion-exchange HPLC using a Whatman Partisil 10 SAX column ( ) in combination, when required, with high-voltage paper electrophoresis in 0.83 m pyridine and 0.5 m acetic acid (pH 5.3) and paper chromatography as described ( ).

    Techniques: High Performance Liquid Chromatography, Labeling, Generated, Radioactivity

    Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 -methyl-AMP (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via HPLC. The values represent the mean ± standard deviation from at least three experiments.

    Journal: Antimicrobial Agents and Chemotherapy

    Article Title: Activation of 6-Alkoxy-Substituted Methylenecyclopropane Nucleoside Analogs Requires Enzymatic Modification by Adenosine Deaminase-Like Protein 1

    doi: 10.1128/AAC.01301-19

    Figure Lengend Snippet: Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 -methyl-AMP (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via HPLC. The values represent the mean ± standard deviation from at least three experiments.

    Article Snippet: N 6 -Methyl-AMP and IMP were separated and quantified using strong-anion-exchange HPLC (Agilent Technologies 1200 Infinity Series system, controlled by OpenLAB v1.3.4 software).

    Techniques: Purification, High Performance Liquid Chromatography, Standard Deviation

    VIH1 and VIH2 Are Functional Vip1-Type PPIP5 Kinases. (A) and (B) Structural model of the VIH2 ATP-grasp kinase domain (left) and the hPPIP5K2 ATP-grasp kinase domain (PDB ID: 3T9D, right) depicting the 5-InsP 7 binding sites and key catalytic residues. Residues coordinating substrate via polar contacts are shown as sticks, polar interactions are highlighted by dashed lines, α-helices are rendered in blue, β-sheets in orange, substrate (5-InsP 7 ) is rendered in magenta, and Mg 2+ ions are presented as green spheres. Three carbon atoms on the inositol ring are numbered. The ATP analog AMP-PNP (in [B] ) is depicted with gray carbon and orange and red phosphate groups. (C) and (D) Complementation of vip1 Δ-associated growth defects in yeast by ectopic expression of inositol pyrophosphate synthetases. The vip1 Δ yeast strain transformed with episomal pDR195( URA3 ) plasmids carrying either VIP1 , VIH1 , or VIH2 , sequences encoding their respective ATP-grasp kinase domains ( KD ) or designated kinase domain mutants, or carrying KCS1 were spotted in 8-fold serial dilutions onto uracil-free minimal medium in presence or absence of 6-azauracil, as indicated. Rescue on medium supplemented with 6-azauracil (right) reports Vip1 activity. (E) and (F) Normalized HPLC profiles of inositol phosphates of extracts from designated [ 3 H] inositol-labeled yeast transformants. Extracts were resolved by Partisphere SAX HPLC and fractions collected each minute for subsequent determination of radioactivity as indicated. Changes in elution times in independent experiments were observed and can be explained by subtle changes in column properties or column change. Experiments were repeated three times with similar results. (G) Complementation assays of kcs1 Δ-associated growth defects on high salt by ectopic expression inositol pyrophosphate synthetases. Wild-type (wt) or kcs1 Δ yeast transformants (both DDY1810 background) carrying designated plasmids were spotted in 8-fold serial dilutions onto solid minimal media (MM, uracil deficient CSM media with YNB and appropriate supplements) in presence or absence of NaCl and onto solid YPDA media incubated at 37°C.

    Journal: The Plant Cell

    Article Title: VIH2 Regulates the Synthesis of Inositol Pyrophosphate InsP8 and Jasmonate-Dependent Defenses in Arabidopsis [OPEN]

    doi: 10.1105/tpc.114.135160

    Figure Lengend Snippet: VIH1 and VIH2 Are Functional Vip1-Type PPIP5 Kinases. (A) and (B) Structural model of the VIH2 ATP-grasp kinase domain (left) and the hPPIP5K2 ATP-grasp kinase domain (PDB ID: 3T9D, right) depicting the 5-InsP 7 binding sites and key catalytic residues. Residues coordinating substrate via polar contacts are shown as sticks, polar interactions are highlighted by dashed lines, α-helices are rendered in blue, β-sheets in orange, substrate (5-InsP 7 ) is rendered in magenta, and Mg 2+ ions are presented as green spheres. Three carbon atoms on the inositol ring are numbered. The ATP analog AMP-PNP (in [B] ) is depicted with gray carbon and orange and red phosphate groups. (C) and (D) Complementation of vip1 Δ-associated growth defects in yeast by ectopic expression of inositol pyrophosphate synthetases. The vip1 Δ yeast strain transformed with episomal pDR195( URA3 ) plasmids carrying either VIP1 , VIH1 , or VIH2 , sequences encoding their respective ATP-grasp kinase domains ( KD ) or designated kinase domain mutants, or carrying KCS1 were spotted in 8-fold serial dilutions onto uracil-free minimal medium in presence or absence of 6-azauracil, as indicated. Rescue on medium supplemented with 6-azauracil (right) reports Vip1 activity. (E) and (F) Normalized HPLC profiles of inositol phosphates of extracts from designated [ 3 H] inositol-labeled yeast transformants. Extracts were resolved by Partisphere SAX HPLC and fractions collected each minute for subsequent determination of radioactivity as indicated. Changes in elution times in independent experiments were observed and can be explained by subtle changes in column properties or column change. Experiments were repeated three times with similar results. (G) Complementation assays of kcs1 Δ-associated growth defects on high salt by ectopic expression inositol pyrophosphate synthetases. Wild-type (wt) or kcs1 Δ yeast transformants (both DDY1810 background) carrying designated plasmids were spotted in 8-fold serial dilutions onto solid minimal media (MM, uracil deficient CSM media with YNB and appropriate supplements) in presence or absence of NaCl and onto solid YPDA media incubated at 37°C.

    Article Snippet: Inositol polyphosphates were extracted as described previously ( ) and resolved by strong anion exchange chromatography HPLC (using the partisphere SAX 4.6 × 125 mm column; Whatman) at a flow rate of 0.5 mL min−1 with the gradient of buffers A (1 mM EDTA) and B [1 mM EDTA and 1.3 M (NH4 )2 HPO4 , pH 3.8, with H3 PO4 ] following the standard protocol mentioned above.

    Techniques: Functional Assay, Binding Assay, Expressing, Transformation Assay, Activity Assay, High Performance Liquid Chromatography, Labeling, Radioactivity, Incubation