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Waters Corporation hilic
Hilic, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 14 article reviews
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Hydrophilic Interaction Liquid Chromatography:

Article Title: Glycosylation of plasma IgG in colorectal cancer prognosis
Article Snippet: .. Hydrophilic Interaction Chromatography (HILIC )-UPLC : Fluorescently labelled N -glycans were separated by HILIC on a Waters Acquity UPLC instrument (Milford, MA, USA) with fluorescence detector set with excitation and emission wavelengths of 330 and 420 nm, respectively. ..

Article Title: Perfluoroalkyl substances, metabolomic profiling, and alterations in glucose homeostasis among overweight and obese Hispanic children: A proof-of-concept analysis
Article Snippet: .. Analyte separation for HILIC was accomplished by a 2.1 mm × 50 mm × 2.5 μm Waters XBridge BEH Amide XP HILIC and an eluent gradient (A = 2% formic acid, B = water, C = acetonitrile) consisting of an initial 1.5 min period of 2.5% A, 22.5% B, 75% C followed by a linear increase to 2.5% A, 77.5% B, 20% C at 4 min and a final hold of 1 min. RPC separation was by 2.1 mm × 50 mm × 3 μm endcapped C18 column (Higgins) using an eluent gradient (A = 2% 5 mM ammonium acetate, B = water, C = acetonitrile) consisting of an initial 2 min period of 5%A, 90%B, 5%C, followed by a linear increase to 5%A, 0%B, 95%C at 6 min and held for the remaining 4 min. For both methods, mobile phase flow rate was held at 0.35 mL/min for the first 1.5 min, increased to 0.5 mL/min and held for the final 4 min. .. The high-resolution mass spectrometer was operated at 120,000 resolution and mass-to-charge ratio (m/z ) range 85–1275.

Flow Cytometry:

Article Title: Perfluoroalkyl substances, metabolomic profiling, and alterations in glucose homeostasis among overweight and obese Hispanic children: A proof-of-concept analysis
Article Snippet: .. Analyte separation for HILIC was accomplished by a 2.1 mm × 50 mm × 2.5 μm Waters XBridge BEH Amide XP HILIC and an eluent gradient (A = 2% formic acid, B = water, C = acetonitrile) consisting of an initial 1.5 min period of 2.5% A, 22.5% B, 75% C followed by a linear increase to 2.5% A, 77.5% B, 20% C at 4 min and a final hold of 1 min. RPC separation was by 2.1 mm × 50 mm × 3 μm endcapped C18 column (Higgins) using an eluent gradient (A = 2% 5 mM ammonium acetate, B = water, C = acetonitrile) consisting of an initial 2 min period of 5%A, 90%B, 5%C, followed by a linear increase to 5%A, 0%B, 95%C at 6 min and held for the remaining 4 min. For both methods, mobile phase flow rate was held at 0.35 mL/min for the first 1.5 min, increased to 0.5 mL/min and held for the final 4 min. .. The high-resolution mass spectrometer was operated at 120,000 resolution and mass-to-charge ratio (m/z ) range 85–1275.

Fluorescence:

Article Title: Glycosylation of plasma IgG in colorectal cancer prognosis
Article Snippet: .. Hydrophilic Interaction Chromatography (HILIC )-UPLC : Fluorescently labelled N -glycans were separated by HILIC on a Waters Acquity UPLC instrument (Milford, MA, USA) with fluorescence detector set with excitation and emission wavelengths of 330 and 420 nm, respectively. ..

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    Waters Corporation hilic uplc
    <t>HILIC-UPLC</t> analysis of 2-AA–labeled N -linked glycans from IgG1-Fc mutants expressed by CHO-K1 cells (see Fig. 1 ). Normal phase HILIC-UPLC analysis of 2-AA–labeled N -linked glycans released from target antibody glycoforms by in-gel protein PNGase F digestion. Glycan profiles for the following variants are shown: hexa-Fc, IgG1-Fc, N563A (upper gel band), and N563A (lower gel band) ( A ); D221N, D221N/N297A, D221N/N563A, and D221N/N297A/N563A ( B ); and C575A, N563A/C575A, and L448STOP ( C ). The y axis displays relative fluorescence, and the x axis the relative elution time. Inserted pie charts represent the means of two analytical replicates; the pie charts summarize the quantification of oligomannose-type ( green ), galactosylated ( yellow ), and sialylated glycans ( pink ) on individual sites. Quantifications are based on the peak lists in supplemental Fig. S1 and supplemental Table S1 . Percentages corresponding to this figure can be found in Table 1 .
    Hilic Uplc, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 89/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hilic uplc/product/Waters Corporation
    Average 89 stars, based on 29 article reviews
    Price from $9.99 to $1999.99
    hilic uplc - by Bioz Stars, 2020-07
    89/100 stars
      Buy from Supplier

    91
    Waters Corporation hydrophilic interaction chromatography ultraperformance liquid chromatography hilic uplc
    Design and glycosylation patterns of BG505 gp120, WT.SEKS, and SOSIP.664. (A) Schematic representation of the BG505 gp120, WT.SEKS, and SOSIP.664 constructs. Changes to the wild-type BG505 sequence are highlighted in blue. (B) <t>HILIC-UPLC</t> profiles of the
    Hydrophilic Interaction Chromatography Ultraperformance Liquid Chromatography Hilic Uplc, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hydrophilic interaction chromatography ultraperformance liquid chromatography hilic uplc/product/Waters Corporation
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hydrophilic interaction chromatography ultraperformance liquid chromatography hilic uplc - by Bioz Stars, 2020-07
    91/100 stars
      Buy from Supplier

    88
    Waters Corporation hilic uplc analysis
    Role of glycan clusters in maintaining the oligomannose population ( a ) Model of a fully glycosylated BaL trimer based on the reported gp140 trimer crystal structure 21 (PDB accession code: 4NCO). Modelled glycans are shown as sticks. The surface of the glycans and underlying protein are depicted in shades of gray. Man 5 GlcNAc 2 glycans were modelled at sites of predicted complex-type glycans and Man 8 GlcNAc 2 glycans were added at predicted oligomannose sites. ( b ) A close-up view of the gp120 monomer. Glycans are colored according to the effect of their elimination on total Man 9 GlcNAc 2 levels or complex-type glycosylation according to Fig 1d . A change of over 5% is greater than the intrinsic variation of glycosylation ( Supplementary Fig. 1 ; Supplementary Table 1 ). ( c ) Examples of changes in glycan composition upon deletion of individual glycan sites of the mannose patch. Residual plots were calculated by the subtraction of <t>HILIC-UPLC</t> spectra of PNGS-deletion mutants from that of the wild-type. Peaks corresponding to oligomannose-type glycans are highlighted. Man 5-9 GlcNAc 2 (M5–9) are schematically labelled according to the combined nomenclature 69 of Harvey et al 70 and the Center of Functional Glycomics.
    Hilic Uplc Analysis, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hilic uplc analysis/product/Waters Corporation
    Average 88 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    hilic uplc analysis - by Bioz Stars, 2020-07
    88/100 stars
      Buy from Supplier

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    HILIC-UPLC analysis of 2-AA–labeled N -linked glycans from IgG1-Fc mutants expressed by CHO-K1 cells (see Fig. 1 ). Normal phase HILIC-UPLC analysis of 2-AA–labeled N -linked glycans released from target antibody glycoforms by in-gel protein PNGase F digestion. Glycan profiles for the following variants are shown: hexa-Fc, IgG1-Fc, N563A (upper gel band), and N563A (lower gel band) ( A ); D221N, D221N/N297A, D221N/N563A, and D221N/N297A/N563A ( B ); and C575A, N563A/C575A, and L448STOP ( C ). The y axis displays relative fluorescence, and the x axis the relative elution time. Inserted pie charts represent the means of two analytical replicates; the pie charts summarize the quantification of oligomannose-type ( green ), galactosylated ( yellow ), and sialylated glycans ( pink ) on individual sites. Quantifications are based on the peak lists in supplemental Fig. S1 and supplemental Table S1 . Percentages corresponding to this figure can be found in Table 1 .

    Journal: The Journal of Biological Chemistry

    Article Title: Engineering the fragment crystallizable (Fc) region of human IgG1 multimers and monomers to fine-tune interactions with sialic acid-dependent receptors

    doi: 10.1074/jbc.M117.795047

    Figure Lengend Snippet: HILIC-UPLC analysis of 2-AA–labeled N -linked glycans from IgG1-Fc mutants expressed by CHO-K1 cells (see Fig. 1 ). Normal phase HILIC-UPLC analysis of 2-AA–labeled N -linked glycans released from target antibody glycoforms by in-gel protein PNGase F digestion. Glycan profiles for the following variants are shown: hexa-Fc, IgG1-Fc, N563A (upper gel band), and N563A (lower gel band) ( A ); D221N, D221N/N297A, D221N/N563A, and D221N/N297A/N563A ( B ); and C575A, N563A/C575A, and L448STOP ( C ). The y axis displays relative fluorescence, and the x axis the relative elution time. Inserted pie charts represent the means of two analytical replicates; the pie charts summarize the quantification of oligomannose-type ( green ), galactosylated ( yellow ), and sialylated glycans ( pink ) on individual sites. Quantifications are based on the peak lists in supplemental Fig. S1 and supplemental Table S1 . Percentages corresponding to this figure can be found in Table 1 .

    Article Snippet: HILIC-UPLC Fluorescently labeled glycans were separated by HILIC-UPLC using a 2.1 × 10-mm (1.7-μm particle size) ACQUITY® ethylene bridged hybrid glycan column (Waters) on a Waters ACQUITY® UPLC instrument.

    Techniques: Hydrophilic Interaction Liquid Chromatography, Labeling, Fluorescence

    HILIC-FLD-UPLC profiles of Gpc1 N -glycans subjected to exoglycosidase digestions to assign their structures. UND represents the undigested pool of glycans; this pool was digested with sialidase ( ABS and NAN1 ), α-fucosidase ( BKF ), β-galactosidase

    Journal: The Journal of Biological Chemistry

    Article Title: Structural Aspects of N-Glycosylations and the C-terminal Region in Human Glypican-1 *

    doi: 10.1074/jbc.M115.660878

    Figure Lengend Snippet: HILIC-FLD-UPLC profiles of Gpc1 N -glycans subjected to exoglycosidase digestions to assign their structures. UND represents the undigested pool of glycans; this pool was digested with sialidase ( ABS and NAN1 ), α-fucosidase ( BKF ), β-galactosidase

    Article Snippet: The samples were dissolved in acetonitrile/H2 O (70:30) and analyzed by HILIC-FLD-UPLC using a 1.7-μm BEH glycan column (2.1 × 15 mm, Waters) and Waters ACQUITY UPLC I-class with fluorescence detection.

    Techniques: Hydrophilic Interaction Liquid Chromatography

    Design and glycosylation patterns of BG505 gp120, WT.SEKS, and SOSIP.664. (A) Schematic representation of the BG505 gp120, WT.SEKS, and SOSIP.664 constructs. Changes to the wild-type BG505 sequence are highlighted in blue. (B) HILIC-UPLC profiles of the

    Journal: Journal of Virology

    Article Title: Molecular Architecture of the Cleavage-Dependent Mannose Patch on a Soluble HIV-1 Envelope Glycoprotein Trimer

    doi: 10.1128/JVI.01894-16

    Figure Lengend Snippet: Design and glycosylation patterns of BG505 gp120, WT.SEKS, and SOSIP.664. (A) Schematic representation of the BG505 gp120, WT.SEKS, and SOSIP.664 constructs. Changes to the wild-type BG505 sequence are highlighted in blue. (B) HILIC-UPLC profiles of the

    Article Snippet: The 2-AA-labeled glycans were subsequently analyzed by hydrophilic interaction chromatography-ultraperformance liquid chromatography (HILIC-UPLC) in a Waters Acquity UPLC instrument ( ).

    Techniques: Construct, Sequencing, Hydrophilic Interaction Liquid Chromatography

    Role of glycan clusters in maintaining the oligomannose population ( a ) Model of a fully glycosylated BaL trimer based on the reported gp140 trimer crystal structure 21 (PDB accession code: 4NCO). Modelled glycans are shown as sticks. The surface of the glycans and underlying protein are depicted in shades of gray. Man 5 GlcNAc 2 glycans were modelled at sites of predicted complex-type glycans and Man 8 GlcNAc 2 glycans were added at predicted oligomannose sites. ( b ) A close-up view of the gp120 monomer. Glycans are colored according to the effect of their elimination on total Man 9 GlcNAc 2 levels or complex-type glycosylation according to Fig 1d . A change of over 5% is greater than the intrinsic variation of glycosylation ( Supplementary Fig. 1 ; Supplementary Table 1 ). ( c ) Examples of changes in glycan composition upon deletion of individual glycan sites of the mannose patch. Residual plots were calculated by the subtraction of HILIC-UPLC spectra of PNGS-deletion mutants from that of the wild-type. Peaks corresponding to oligomannose-type glycans are highlighted. Man 5-9 GlcNAc 2 (M5–9) are schematically labelled according to the combined nomenclature 69 of Harvey et al 70 and the Center of Functional Glycomics.

    Journal: Nature communications

    Article Title: Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies

    doi: 10.1038/ncomms8479

    Figure Lengend Snippet: Role of glycan clusters in maintaining the oligomannose population ( a ) Model of a fully glycosylated BaL trimer based on the reported gp140 trimer crystal structure 21 (PDB accession code: 4NCO). Modelled glycans are shown as sticks. The surface of the glycans and underlying protein are depicted in shades of gray. Man 5 GlcNAc 2 glycans were modelled at sites of predicted complex-type glycans and Man 8 GlcNAc 2 glycans were added at predicted oligomannose sites. ( b ) A close-up view of the gp120 monomer. Glycans are colored according to the effect of their elimination on total Man 9 GlcNAc 2 levels or complex-type glycosylation according to Fig 1d . A change of over 5% is greater than the intrinsic variation of glycosylation ( Supplementary Fig. 1 ; Supplementary Table 1 ). ( c ) Examples of changes in glycan composition upon deletion of individual glycan sites of the mannose patch. Residual plots were calculated by the subtraction of HILIC-UPLC spectra of PNGS-deletion mutants from that of the wild-type. Peaks corresponding to oligomannose-type glycans are highlighted. Man 5-9 GlcNAc 2 (M5–9) are schematically labelled according to the combined nomenclature 69 of Harvey et al 70 and the Center of Functional Glycomics.

    Article Snippet: HILIC-UPLC analysis of N-linked glycans Fluorescently labelled glycans were separated by HILIC-UPLC using a 2.1 mm × 10 mm Acquity BEH Amide Column (1.7 μm particle size; Waters, Elstree, UK).

    Techniques: Hydrophilic Interaction Liquid Chromatography, Functional Assay

    Contribution of individual glycans to the total glycosylation of gp120 BaL ( a ) HILIC-UPLC profile of N-linked glycans released from gp120 BaL . The Man 5-9 GlcNAc 2 series is labelled M5–M9 and highlighted in blue. Remaining peaks correspond to hybrid and complex-type glycans ( b ) Schematic showing the distribution of the 23 PNGSs of gp120 BaL . Sites were allocated as putative complex-type or putative oligomannose-type based on previous reports 1 , 35 - 37 . ( c ) Percentage conservation of the individual PNGSs across different clades, based on analysis of over 4000 aligned Env sequences from the Los Alamos HIV sequence database ( http://www.hiv.lanl.gov/ ). ( d ) Effect of PNGS-deletion on the total abundance of oligomannose-type glycans, and the individual abundance of Man 9 GlcNAc 2 . Values were obtained by integration of corresponding HILIC-UPLC peaks ( Supplementary Fig. 2 ), before and after Endoglycosidase H treatment, and represent the percentage change in abundance (relative to wild-type). Percentage change = [(% oligomannose in wild-type − % oligomannose in mutant)/(% oligomannose in wild-type)] × 100. Values are reported in Supplementary Table 2 . The dashed line represents the predicted drop in oligomannose levels from the elimination of one site containing only oligomannose-type glycans.

    Journal: Nature communications

    Article Title: Glycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodies

    doi: 10.1038/ncomms8479

    Figure Lengend Snippet: Contribution of individual glycans to the total glycosylation of gp120 BaL ( a ) HILIC-UPLC profile of N-linked glycans released from gp120 BaL . The Man 5-9 GlcNAc 2 series is labelled M5–M9 and highlighted in blue. Remaining peaks correspond to hybrid and complex-type glycans ( b ) Schematic showing the distribution of the 23 PNGSs of gp120 BaL . Sites were allocated as putative complex-type or putative oligomannose-type based on previous reports 1 , 35 - 37 . ( c ) Percentage conservation of the individual PNGSs across different clades, based on analysis of over 4000 aligned Env sequences from the Los Alamos HIV sequence database ( http://www.hiv.lanl.gov/ ). ( d ) Effect of PNGS-deletion on the total abundance of oligomannose-type glycans, and the individual abundance of Man 9 GlcNAc 2 . Values were obtained by integration of corresponding HILIC-UPLC peaks ( Supplementary Fig. 2 ), before and after Endoglycosidase H treatment, and represent the percentage change in abundance (relative to wild-type). Percentage change = [(% oligomannose in wild-type − % oligomannose in mutant)/(% oligomannose in wild-type)] × 100. Values are reported in Supplementary Table 2 . The dashed line represents the predicted drop in oligomannose levels from the elimination of one site containing only oligomannose-type glycans.

    Article Snippet: HILIC-UPLC analysis of N-linked glycans Fluorescently labelled glycans were separated by HILIC-UPLC using a 2.1 mm × 10 mm Acquity BEH Amide Column (1.7 μm particle size; Waters, Elstree, UK).

    Techniques: Hydrophilic Interaction Liquid Chromatography, Sequencing, Mutagenesis