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Merck KGaA sequant zic hilic column
ESI-MS spectra of selected compounds in the Genista tinctoria extract. Column: <t>ZIC-HILIC</t> (100 × 2.1 mm, 3.5 µ m). Elution gradient: 0–4 min 98% ACN, 6-7 min 90%, 8–8.4 min 80%, 8.4–12 min 50%, and 13–20 min 98%.
Sequant Zic Hilic Column, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 89/100, based on 80 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/sequant zic hilic column/product/Merck KGaA
Average 89 stars, based on 80 article reviews
Price from $9.99 to $1999.99
sequant zic hilic column - by Bioz Stars, 2020-07
89/100 stars

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1) Product Images from "Application of Hydrophilic Interaction Liquid Chromatography for the Quantification of Flavonoids in Genista tinctoria Extract"

Article Title: Application of Hydrophilic Interaction Liquid Chromatography for the Quantification of Flavonoids in Genista tinctoria Extract

Journal: Journal of Analytical Methods in Chemistry

doi: 10.1155/2016/3789348

ESI-MS spectra of selected compounds in the Genista tinctoria extract. Column: ZIC-HILIC (100 × 2.1 mm, 3.5 µ m). Elution gradient: 0–4 min 98% ACN, 6-7 min 90%, 8–8.4 min 80%, 8.4–12 min 50%, and 13–20 min 98%.
Figure Legend Snippet: ESI-MS spectra of selected compounds in the Genista tinctoria extract. Column: ZIC-HILIC (100 × 2.1 mm, 3.5 µ m). Elution gradient: 0–4 min 98% ACN, 6-7 min 90%, 8–8.4 min 80%, 8.4–12 min 50%, and 13–20 min 98%.

Techniques Used: Mass Spectrometry, Hydrophilic Interaction Liquid Chromatography

2) Product Images from "Engineering a surface endogalactanase into Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation"

Article Title: Engineering a surface endogalactanase into Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation

Journal: Nature microbiology

doi: 10.1038/s41564-018-0258-8

HPAEC analysis of the activity of GH43_24 β1,3-D-galactanases The AGPs were at 5 mg/ml for all reactions except BT0264 against LA-AGP and BT3683 against GA-AGP, when substrate concentration was increased to 25 mg/ml, the β-1,3-galactan backbone was at 1.5 mg/ml. Enzyme concentration was 1 µM. Reactions were incubated for 16 h in 20 mM sodium phosphate buffer pH 7.0 containing 150 mM NaCl buffer. The data shown are representative of three independent replicates. a, reveals how the GH127 β-L-arabinofuranosidase BT3674 acts in synergy with the exo-β1,3-galactosidases BT0265 and BT3683 on LA-AGP. The synergy between the endo-β1,3-galactanase with BT0265 and BT3683 acting on LA-AGP and GA-AGP was shown in b and c , respectively. d , shows a time course of BT0264 acting on β-1,3-galactan. Peaks containing a defined galactooligosaccharide are identified by a yellow circle with the degree of polymerization shown in subscript. In b and c the peaks corresponding to β1,6-galactobiose and β1,6-galactotriose were identified by LC-MS (see Supplementary Fig. 1d ), and the β1,6 linkage was revealed by sensitivity to the β1,6-galactosidase BT0290.
Figure Legend Snippet: HPAEC analysis of the activity of GH43_24 β1,3-D-galactanases The AGPs were at 5 mg/ml for all reactions except BT0264 against LA-AGP and BT3683 against GA-AGP, when substrate concentration was increased to 25 mg/ml, the β-1,3-galactan backbone was at 1.5 mg/ml. Enzyme concentration was 1 µM. Reactions were incubated for 16 h in 20 mM sodium phosphate buffer pH 7.0 containing 150 mM NaCl buffer. The data shown are representative of three independent replicates. a, reveals how the GH127 β-L-arabinofuranosidase BT3674 acts in synergy with the exo-β1,3-galactosidases BT0265 and BT3683 on LA-AGP. The synergy between the endo-β1,3-galactanase with BT0265 and BT3683 acting on LA-AGP and GA-AGP was shown in b and c , respectively. d , shows a time course of BT0264 acting on β-1,3-galactan. Peaks containing a defined galactooligosaccharide are identified by a yellow circle with the degree of polymerization shown in subscript. In b and c the peaks corresponding to β1,6-galactobiose and β1,6-galactotriose were identified by LC-MS (see Supplementary Fig. 1d ), and the β1,6 linkage was revealed by sensitivity to the β1,6-galactosidase BT0290.

Techniques Used: Activity Assay, Concentration Assay, Incubation, Liquid Chromatography with Mass Spectroscopy

The crystal structure of GH43_24 β1,3-D-galactosidases in complex with ligands. a, schematic of BT0265 (left) and BT3683 (right) in which the catalytic domains are colour ramped from blue at the N-terminus to red at the C-terminus. The C-terminal β-sandwich domain in BT0265 is coloured cyan. b, shows the solvent exposed surface of BT0265 in complex with the heptasaccharide shown in Supplementary Fig. 3 (terminal α-Gal and α-Rha are not visible). Electron density for the terminal α-Gal was too weak to model the sugar. The red dashes show the polar interactions between the ligand and both side chains and backbone N and O. Residues that make polar contacts with the side chain of the ligand are also shown. c , an overlay of the residues in BT0265 ( cyan ), BT3683 ( green ) and the GH43_24 β1,3-galactosidase Cthe_1271 ( grey ; PDB code 3VSZ) that interact with galactose ( yellow ) in complex with BT3683. d, BT3683 in complex with galactose (Gal), deoxygalactonojirimycin (DGJ) and galactose-imidazole (Gal-Im). Direct polar interactions between enzyme and ligand are indicated by black dashes and the indirect water-mediated hydrogen bonds in magenta dashes. The red dashed line represents the polar interaction between the catalytic acid (Glu520) and Ser487. The two conformations of Glu520 in the Gal-Im complex is denoted by a and b.
Figure Legend Snippet: The crystal structure of GH43_24 β1,3-D-galactosidases in complex with ligands. a, schematic of BT0265 (left) and BT3683 (right) in which the catalytic domains are colour ramped from blue at the N-terminus to red at the C-terminus. The C-terminal β-sandwich domain in BT0265 is coloured cyan. b, shows the solvent exposed surface of BT0265 in complex with the heptasaccharide shown in Supplementary Fig. 3 (terminal α-Gal and α-Rha are not visible). Electron density for the terminal α-Gal was too weak to model the sugar. The red dashes show the polar interactions between the ligand and both side chains and backbone N and O. Residues that make polar contacts with the side chain of the ligand are also shown. c , an overlay of the residues in BT0265 ( cyan ), BT3683 ( green ) and the GH43_24 β1,3-galactosidase Cthe_1271 ( grey ; PDB code 3VSZ) that interact with galactose ( yellow ) in complex with BT3683. d, BT3683 in complex with galactose (Gal), deoxygalactonojirimycin (DGJ) and galactose-imidazole (Gal-Im). Direct polar interactions between enzyme and ligand are indicated by black dashes and the indirect water-mediated hydrogen bonds in magenta dashes. The red dashed line represents the polar interaction between the catalytic acid (Glu520) and Ser487. The two conformations of Glu520 in the Gal-Im complex is denoted by a and b.

Techniques Used:

Degradation of GA-AGP side chains. The pentasaccharide substrate shown in a grey box was released from GA-AGP by the exo-β1,3-galactosidase BT0265 and then purified by size exclusion chromatography. Individual B. thetaiotaomicron enzymes (1 μM) were incubated with the glycan (5 mM) for 16 h at 37 °C in 20 mM sodium phosphate buffer, pH 7.0. Monosaccharides and oligosaccharides generated were identified by HPAEC-PAD. The data in a and b show that the pentasaccharide could be degraded by the enzymes that comprise the LU and RG pathways, respectively. Note that the enzymes in the two pathways Verification of the degradative pathway was achieved by reconstituting the pathway using the only functioned in the order shown in the figure. The example is representative of independent replicates ( n = 3).
Figure Legend Snippet: Degradation of GA-AGP side chains. The pentasaccharide substrate shown in a grey box was released from GA-AGP by the exo-β1,3-galactosidase BT0265 and then purified by size exclusion chromatography. Individual B. thetaiotaomicron enzymes (1 μM) were incubated with the glycan (5 mM) for 16 h at 37 °C in 20 mM sodium phosphate buffer, pH 7.0. Monosaccharides and oligosaccharides generated were identified by HPAEC-PAD. The data in a and b show that the pentasaccharide could be degraded by the enzymes that comprise the LU and RG pathways, respectively. Note that the enzymes in the two pathways Verification of the degradative pathway was achieved by reconstituting the pathway using the only functioned in the order shown in the figure. The example is representative of independent replicates ( n = 3).

Techniques Used: Purification, Size-exclusion Chromatography, Incubation, Generated

3) Product Images from "Extracellular vesicles are independent metabolic units with asparaginase activity"

Article Title: Extracellular vesicles are independent metabolic units with asparaginase activity

Journal: Nature chemical biology

doi: 10.1038/nchembio.2422

NSC EVs are metabolically active in vitro . (a) Scatter plot of metabolomics experiment showing log 2 fold changes of extracellular metabolites in medium + EVs vs . Vehicle as in a . Positive/negative values indicate production/consumption of metabolites, respectively. Data from two independent experiments are shown. (b) Barplot of the consumption of 15 N 2 -Asn and production of 15 N-Asp mediated by EVs, conditioned medium (i.e. CM, medium with EVs) and supernatant (i.e. SN, medium deprived of EVs), with or without heat inactivation (100°C for 10’). Data are mean ± SEM and have been obtained from n= 2 independent experiments. Statistical analysis was performed using one-way ANOVA, followed by Bonferroni’s test correction. * p
Figure Legend Snippet: NSC EVs are metabolically active in vitro . (a) Scatter plot of metabolomics experiment showing log 2 fold changes of extracellular metabolites in medium + EVs vs . Vehicle as in a . Positive/negative values indicate production/consumption of metabolites, respectively. Data from two independent experiments are shown. (b) Barplot of the consumption of 15 N 2 -Asn and production of 15 N-Asp mediated by EVs, conditioned medium (i.e. CM, medium with EVs) and supernatant (i.e. SN, medium deprived of EVs), with or without heat inactivation (100°C for 10’). Data are mean ± SEM and have been obtained from n= 2 independent experiments. Statistical analysis was performed using one-way ANOVA, followed by Bonferroni’s test correction. * p

Techniques Used: Metabolic Labelling, In Vitro

4) Product Images from "Organic and Peptidyl Constituents of Snake Venoms: The Picture Is Vastly More Complex Than We Imagined"

Article Title: Organic and Peptidyl Constituents of Snake Venoms: The Picture Is Vastly More Complex Than We Imagined

Journal: Toxins

doi: 10.3390/toxins10100392

Total ion chromatograms of negative and positive ions of metabolites and peptides from Agkistrodon piscivorus leucostoma venom. The negative ion peak that dwarfs all others is citric acid. Assuming no metabolite loss during deproteination, the metabolites and peptides separated here represent the small molecule component of ~69 µg of crude venom. Metabolites were separated on a SeQuant ZIC-pHILIC HPLC 2.1 × 150 mm column, flow rate 120 µL/min, using acetonitrile as solvent A, and 10 mM ammonium carbonate, 0.1% ammonium hydroxide in water as solvent B. Separation was done in HILIC mode, with a linear gradient from 20% to 80% solvent B in 30 min, followed by a wash for 20 min with 20% acetonitrile, 0.5 M sodium chloride in water (solvent C) and, finally, column re-equilibration with starting conditions for 15 min.
Figure Legend Snippet: Total ion chromatograms of negative and positive ions of metabolites and peptides from Agkistrodon piscivorus leucostoma venom. The negative ion peak that dwarfs all others is citric acid. Assuming no metabolite loss during deproteination, the metabolites and peptides separated here represent the small molecule component of ~69 µg of crude venom. Metabolites were separated on a SeQuant ZIC-pHILIC HPLC 2.1 × 150 mm column, flow rate 120 µL/min, using acetonitrile as solvent A, and 10 mM ammonium carbonate, 0.1% ammonium hydroxide in water as solvent B. Separation was done in HILIC mode, with a linear gradient from 20% to 80% solvent B in 30 min, followed by a wash for 20 min with 20% acetonitrile, 0.5 M sodium chloride in water (solvent C) and, finally, column re-equilibration with starting conditions for 15 min.

Techniques Used: High Performance Liquid Chromatography, Flow Cytometry, Hydrophilic Interaction Liquid Chromatography

5) Product Images from "Engineering a surface endogalactanase into Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation"

Article Title: Engineering a surface endogalactanase into Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation

Journal: Nature microbiology

doi: 10.1038/s41564-018-0258-8

HPAEC analysis of the activity of GH43_24 β1,3-D-galactanases The AGPs were at 5 mg/ml for all reactions except BT0264 against LA-AGP and BT3683 against GA-AGP, when substrate concentration was increased to 25 mg/ml, the β-1,3-galactan backbone was at 1.5 mg/ml. Enzyme concentration was 1 µM. Reactions were incubated for 16 h in 20 mM sodium phosphate buffer pH 7.0 containing 150 mM NaCl buffer. The data shown are representative of three independent replicates. a, reveals how the GH127 β-L-arabinofuranosidase BT3674 acts in synergy with the exo-β1,3-galactosidases BT0265 and BT3683 on LA-AGP. The synergy between the endo-β1,3-galactanase with BT0265 and BT3683 acting on LA-AGP and GA-AGP was shown in b and c , respectively. d , shows a time course of BT0264 acting on β-1,3-galactan. Peaks containing a defined galactooligosaccharide are identified by a yellow circle with the degree of polymerization shown in subscript. In b and c the peaks corresponding to β1,6-galactobiose and β1,6-galactotriose were identified by LC-MS (see Supplementary Fig. 1d ), and the β1,6 linkage was revealed by sensitivity to the β1,6-galactosidase BT0290.
Figure Legend Snippet: HPAEC analysis of the activity of GH43_24 β1,3-D-galactanases The AGPs were at 5 mg/ml for all reactions except BT0264 against LA-AGP and BT3683 against GA-AGP, when substrate concentration was increased to 25 mg/ml, the β-1,3-galactan backbone was at 1.5 mg/ml. Enzyme concentration was 1 µM. Reactions were incubated for 16 h in 20 mM sodium phosphate buffer pH 7.0 containing 150 mM NaCl buffer. The data shown are representative of three independent replicates. a, reveals how the GH127 β-L-arabinofuranosidase BT3674 acts in synergy with the exo-β1,3-galactosidases BT0265 and BT3683 on LA-AGP. The synergy between the endo-β1,3-galactanase with BT0265 and BT3683 acting on LA-AGP and GA-AGP was shown in b and c , respectively. d , shows a time course of BT0264 acting on β-1,3-galactan. Peaks containing a defined galactooligosaccharide are identified by a yellow circle with the degree of polymerization shown in subscript. In b and c the peaks corresponding to β1,6-galactobiose and β1,6-galactotriose were identified by LC-MS (see Supplementary Fig. 1d ), and the β1,6 linkage was revealed by sensitivity to the β1,6-galactosidase BT0290.

Techniques Used: Activity Assay, Concentration Assay, Incubation, Liquid Chromatography with Mass Spectroscopy

Degradation of GA-AGP side chains. The pentasaccharide substrate shown in a grey box was released from GA-AGP by the exo-β1,3-galactosidase BT0265 and then purified by size exclusion chromatography. Individual B. thetaiotaomicron enzymes (1 μM) were incubated with the glycan (5 mM) for 16 h at 37 °C in 20 mM sodium phosphate buffer, pH 7.0. Monosaccharides and oligosaccharides generated were identified by HPAEC-PAD. The data in a and b show that the pentasaccharide could be degraded by the enzymes that comprise the LU and RG pathways, respectively. Note that the enzymes in the two pathways Verification of the degradative pathway was achieved by reconstituting the pathway using the only functioned in the order shown in the figure. The example is representative of independent replicates ( n = 3).
Figure Legend Snippet: Degradation of GA-AGP side chains. The pentasaccharide substrate shown in a grey box was released from GA-AGP by the exo-β1,3-galactosidase BT0265 and then purified by size exclusion chromatography. Individual B. thetaiotaomicron enzymes (1 μM) were incubated with the glycan (5 mM) for 16 h at 37 °C in 20 mM sodium phosphate buffer, pH 7.0. Monosaccharides and oligosaccharides generated were identified by HPAEC-PAD. The data in a and b show that the pentasaccharide could be degraded by the enzymes that comprise the LU and RG pathways, respectively. Note that the enzymes in the two pathways Verification of the degradative pathway was achieved by reconstituting the pathway using the only functioned in the order shown in the figure. The example is representative of independent replicates ( n = 3).

Techniques Used: Purification, Size-exclusion Chromatography, Incubation, Generated

Related Articles

Hydrophilic Interaction Liquid Chromatography:

Article Title: Survey of moniliformin in wheat- and corn-based products using a straightforward analytical method
Article Snippet: .. The following chromatographic columns were assessed: Synchronis™ HILIC 100 × 2.1 mm 1.7 μm (Thermo Fisher Scientific, Waltham, MA, USA), Gemini® C6-Phenyl 100 × 2.0 mm 3 μm (Phenomenex, Utrecht, the Netherlands) and SeQuant® ZIC®-HILIC 100 × 2.1 mm 5 μm (Merck Millipore, Darmstadt, Germany). .. Water with 1% formic acid and water buffered at pH 6.4 with ammonium formate were tested as mobile phase A, while acetonitrile (with and without formic acid 1%) and methanol with 1% formic acid were used as mobile phase B. Optimization was carried out in an Acquity UPLC coupled with a Xevo TQ-S mass spectrometer (Waters, Milford, MA, USA).

High Performance Liquid Chromatography:

Article Title: Identification and Functional Characterization of Small Alarmone Synthetases in Corynebacterium glutamicum
Article Snippet: .. HPLC analysis of all assay reactions was performed using a LaChrome ULTRA system (HITACHI) and a SeQuant ZIC-pHILIC column (Merck Millipore). .. A MicrOTOFQ (Bruker Daltonics) was used for the mass spectroscopic identification of the different nucleotide species.

Article Title: Organic and Peptidyl Constituents of Snake Venoms: The Picture Is Vastly More Complex Than We Imagined
Article Snippet: .. Hydrophobic Interaction Chromatography A SeQuant ZIC-pHILIC HPLC 2.1 × 150 mm column (Merck Millipore, Burlington, MA, USA) was used for separation, flow rate 250 µL/min, using acetonitrile as solvent A and 10 mM ammonium carbonate, 0.2% ammonium hydroxide (pH 9.4) as solvent B. .. Separation was done in HILIC mode, with a linear gradient from 20% to 80% solvent B in 15 min, followed by a wash for 20 min with 20% acetonitrile, 0.5 M ammonium carbonate in water (solvent C) and, finally, column re-equilibration under starting conditions for 15 min [ ].

Flow Cytometry:

Article Title: Organic and Peptidyl Constituents of Snake Venoms: The Picture Is Vastly More Complex Than We Imagined
Article Snippet: .. Hydrophobic Interaction Chromatography A SeQuant ZIC-pHILIC HPLC 2.1 × 150 mm column (Merck Millipore, Burlington, MA, USA) was used for separation, flow rate 250 µL/min, using acetonitrile as solvent A and 10 mM ammonium carbonate, 0.2% ammonium hydroxide (pH 9.4) as solvent B. .. Separation was done in HILIC mode, with a linear gradient from 20% to 80% solvent B in 15 min, followed by a wash for 20 min with 20% acetonitrile, 0.5 M ammonium carbonate in water (solvent C) and, finally, column re-equilibration under starting conditions for 15 min [ ].

Chromatography:

Article Title: Engineering a surface endogalactanase into Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation
Article Snippet: .. Liquid chromatography-mass spectrometry The sample containing the oligosaccharides generated by treatment of LA-AGP with BT0265 was diluted 1:10 (v/v) with Buffer B (85% acetonitrile/15% 50 mM ammonium formate in water, pH 4.7) and 0.5 µL was analysed by LC-MS analysis via elution from a ZIC-HILIC (SeQuant®, 3.5 µm, 200Å, 150 X 0.3 mm, Merck, UK) capillary column. .. The column was connected to a NanoAcquity HPLC system (Waters, UK) and heated to 35°C with an elution gradient as follows; 100% Buffer B for 5 min, followed by a gradient to 25% Buffer B/75% Buffer A (50 mM ammonium formate in water, pH 4.7) over 40 min.

Hydrophobic Interaction Chromatography:

Article Title: Organic and Peptidyl Constituents of Snake Venoms: The Picture Is Vastly More Complex Than We Imagined
Article Snippet: .. Hydrophobic Interaction Chromatography A SeQuant ZIC-pHILIC HPLC 2.1 × 150 mm column (Merck Millipore, Burlington, MA, USA) was used for separation, flow rate 250 µL/min, using acetonitrile as solvent A and 10 mM ammonium carbonate, 0.2% ammonium hydroxide (pH 9.4) as solvent B. .. Separation was done in HILIC mode, with a linear gradient from 20% to 80% solvent B in 15 min, followed by a wash for 20 min with 20% acetonitrile, 0.5 M ammonium carbonate in water (solvent C) and, finally, column re-equilibration under starting conditions for 15 min [ ].

Generated:

Article Title: Engineering a surface endogalactanase into Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation
Article Snippet: .. Liquid chromatography-mass spectrometry The sample containing the oligosaccharides generated by treatment of LA-AGP with BT0265 was diluted 1:10 (v/v) with Buffer B (85% acetonitrile/15% 50 mM ammonium formate in water, pH 4.7) and 0.5 µL was analysed by LC-MS analysis via elution from a ZIC-HILIC (SeQuant®, 3.5 µm, 200Å, 150 X 0.3 mm, Merck, UK) capillary column. .. The column was connected to a NanoAcquity HPLC system (Waters, UK) and heated to 35°C with an elution gradient as follows; 100% Buffer B for 5 min, followed by a gradient to 25% Buffer B/75% Buffer A (50 mM ammonium formate in water, pH 4.7) over 40 min.

Liquid Chromatography with Mass Spectroscopy:

Article Title: Extracellular vesicles are independent metabolic units with asparaginase activity
Article Snippet: .. LC-MS metabolomic analysis For the LC separation, column used was the Sequant ZIC-HILIC (150mm × 4.6 mm, particle size 5 μm) with a guard column (20 mm × 2.1 mm, 5 µm) from Merck Millipore (HiChrom, Reading, UK). ..

Article Title: Engineering a surface endogalactanase into Bacteroides thetaiotaomicron confers keystone status for arabinogalactan degradation
Article Snippet: .. Liquid chromatography-mass spectrometry The sample containing the oligosaccharides generated by treatment of LA-AGP with BT0265 was diluted 1:10 (v/v) with Buffer B (85% acetonitrile/15% 50 mM ammonium formate in water, pH 4.7) and 0.5 µL was analysed by LC-MS analysis via elution from a ZIC-HILIC (SeQuant®, 3.5 µm, 200Å, 150 X 0.3 mm, Merck, UK) capillary column. .. The column was connected to a NanoAcquity HPLC system (Waters, UK) and heated to 35°C with an elution gradient as follows; 100% Buffer B for 5 min, followed by a gradient to 25% Buffer B/75% Buffer A (50 mM ammonium formate in water, pH 4.7) over 40 min.

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    Merck KGaA sequant zic hilic column
    ESI-MS spectra of selected compounds in the Genista tinctoria extract. Column: <t>ZIC-HILIC</t> (100 × 2.1 mm, 3.5 µ m). Elution gradient: 0–4 min 98% ACN, 6-7 min 90%, 8–8.4 min 80%, 8.4–12 min 50%, and 13–20 min 98%.
    Sequant Zic Hilic Column, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 89/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sequant zic hilic column/product/Merck KGaA
    Average 89 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    sequant zic hilic column - by Bioz Stars, 2020-07
    89/100 stars
      Buy from Supplier

    86
    Merck KGaA 100a sequant zic hilic column
    ESI-MS spectra of selected compounds in the Genista tinctoria extract. Column: <t>ZIC-HILIC</t> (100 × 2.1 mm, 3.5 µ m). Elution gradient: 0–4 min 98% ACN, 6-7 min 90%, 8–8.4 min 80%, 8.4–12 min 50%, and 13–20 min 98%.
    100a Sequant Zic Hilic Column, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/100a sequant zic hilic column/product/Merck KGaA
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    100a sequant zic hilic column - by Bioz Stars, 2020-07
    86/100 stars
      Buy from Supplier

    90
    Merck KGaA sequant zic hilic
    ESI-MS spectra of selected compounds in the Genista tinctoria extract. Column: <t>ZIC-HILIC</t> (100 × 2.1 mm, 3.5 µ m). Elution gradient: 0–4 min 98% ACN, 6-7 min 90%, 8–8.4 min 80%, 8.4–12 min 50%, and 13–20 min 98%.
    Sequant Zic Hilic, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sequant zic hilic/product/Merck KGaA
    Average 90 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    sequant zic hilic - by Bioz Stars, 2020-07
    90/100 stars
      Buy from Supplier

    Image Search Results


    ESI-MS spectra of selected compounds in the Genista tinctoria extract. Column: ZIC-HILIC (100 × 2.1 mm, 3.5 µ m). Elution gradient: 0–4 min 98% ACN, 6-7 min 90%, 8–8.4 min 80%, 8.4–12 min 50%, and 13–20 min 98%.

    Journal: Journal of Analytical Methods in Chemistry

    Article Title: Application of Hydrophilic Interaction Liquid Chromatography for the Quantification of Flavonoids in Genista tinctoria Extract

    doi: 10.1155/2016/3789348

    Figure Lengend Snippet: ESI-MS spectra of selected compounds in the Genista tinctoria extract. Column: ZIC-HILIC (100 × 2.1 mm, 3.5 µ m). Elution gradient: 0–4 min 98% ACN, 6-7 min 90%, 8–8.4 min 80%, 8.4–12 min 50%, and 13–20 min 98%.

    Article Snippet: Compounds were separated on two chromatographic columns: Atlantis-HILIC column (100 × 2.1 mm, 3.0 μ m) from Waters (Milford, MA, USA), and SeQuant™ ZIC-HILIC column (100 × 2.1 mm, 3.5 µ m) from Merck (Darmstadt, Germany).

    Techniques: Mass Spectrometry, Hydrophilic Interaction Liquid Chromatography