neuraminidase  (New England Biolabs)


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    Name:
    alpha 2 3 Neuraminidase S
    Description:
    alpha 2 3 Neuraminidase S 2 000 units
    Catalog Number:
    P0743L
    Price:
    276
    Category:
    Glycosidases
    Size:
    2 000 units
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    Structured Review

    New England Biolabs neuraminidase
    alpha 2 3 Neuraminidase S
    alpha 2 3 Neuraminidase S 2 000 units
    https://www.bioz.com/result/neuraminidase/product/New England Biolabs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    neuraminidase - by Bioz Stars, 2021-06
    94/100 stars

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    Related Articles

    Sequencing:

    Article Title: Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
    Article Snippet: Removal of excess label from the 2-AA fluorescently labeled glycan samples was performed using Speed Amide-2 cartridges (Applied Separations, Allentown, PA). .. Exoglycosidase Sequencing of N-Linked Glycans The 2-AA labeled glycans were sequentially digested using the following exoglycosidases according to the manufacturers’ instructions: α2-3,6,8 neuraminidase from Clostridium perfringens (New England Biolabs, Hertfordshire, UK), α2-3 neuraminidase from Streptococcus pneumoniae (New England BioLabs, Hertfordshire, UK), β1,4-galactosidase from Bacteroides fragilis (New England Biolabs, Hertfordshire, UK), and α-L-fucosidase from bovine kidney (Sigma-Aldrich, Dorset, UK), β-N -acetylglucosaminidase from Xanthomonas manihotis (New England Biolabs, Hertfordshire, UK), and α(1–2,3,6)-mannosidase from Jack bean (Sigma-Aldrich, Dorset, UK). .. Endoglycosidase H (endoH) from Streptomyces picatus (New England BioLabs, Hertfordshire, UK) was used for quantification of oligomannose structures.

    Labeling:

    Article Title: Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
    Article Snippet: Removal of excess label from the 2-AA fluorescently labeled glycan samples was performed using Speed Amide-2 cartridges (Applied Separations, Allentown, PA). .. Exoglycosidase Sequencing of N-Linked Glycans The 2-AA labeled glycans were sequentially digested using the following exoglycosidases according to the manufacturers’ instructions: α2-3,6,8 neuraminidase from Clostridium perfringens (New England Biolabs, Hertfordshire, UK), α2-3 neuraminidase from Streptococcus pneumoniae (New England BioLabs, Hertfordshire, UK), β1,4-galactosidase from Bacteroides fragilis (New England Biolabs, Hertfordshire, UK), and α-L-fucosidase from bovine kidney (Sigma-Aldrich, Dorset, UK), β-N -acetylglucosaminidase from Xanthomonas manihotis (New England Biolabs, Hertfordshire, UK), and α(1–2,3,6)-mannosidase from Jack bean (Sigma-Aldrich, Dorset, UK). .. Endoglycosidase H (endoH) from Streptomyces picatus (New England BioLabs, Hertfordshire, UK) was used for quantification of oligomannose structures.

    Article Title: Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
    Article Snippet: Removal of excess label from the 2-AA fluorescently labeled glycan samples was performed using Speed Amide-2 cartridges (Applied Separations, Allentown, PA). .. The 2-AA labeled glycans were sequentially digested using the following exoglycosidases according to the manufacturers’ instructions: α2-3,6,8 neuraminidase from Clostridium perfringens (New England Biolabs, Hertfordshire, UK), α2-3 neuraminidase from Streptococcus pneumoniae (New England BioLabs, Hertfordshire, UK), β1,4-galactosidase from Bacteroides fragilis (New England Biolabs, Hertfordshire, UK), and α-L-fucosidase from bovine kidney (Sigma-Aldrich, Dorset, UK), β- N -acetylglucosaminidase from Xanthomonas manihotis (New England Biolabs, Hertfordshire, UK), and α(1–2,3,6)-mannosidase from Jack bean (Sigma-Aldrich, Dorset, UK). .. Endoglycosidase H (endoH) from Streptomyces picatus (New England BioLabs, Hertfordshire, UK) was used for quantification of oligomannose structures.

    Concentration Assay:

    Article Title: Characterizing Protein Glycosylation through On-Chip Glycan Modification and Probing
    Article Snippet: For experiments involving the analysis of human plasma, we diluted each sample 2-fold into a buffer (1X PBS with 0.1% Tween-20, 0.1% Brij-35, species-specific blocking antibodies, and protease inhibitor) and incubated the sample on an antibody array overnight at 4 °C. .. We prepared α2-3 Neuraminidase (P0728L, New England Biolabs, Ipswich) or α2-3, 6, 8 Neuraminidase (P0720S, New England Biolabs, Ipswich) at a concentration of 250 U/mL in the supplied reaction buffer and incubated each separately on arrays containing the captured or spotted glycoproteins overnight at 37°C. .. The arrays not treated with enzymes were incubated with the enzyme reaction buffer in the same conditions.

    Incubation:

    Article Title: Characterizing Protein Glycosylation through On-Chip Glycan Modification and Probing
    Article Snippet: For experiments involving the analysis of human plasma, we diluted each sample 2-fold into a buffer (1X PBS with 0.1% Tween-20, 0.1% Brij-35, species-specific blocking antibodies, and protease inhibitor) and incubated the sample on an antibody array overnight at 4 °C. .. We prepared α2-3 Neuraminidase (P0728L, New England Biolabs, Ipswich) or α2-3, 6, 8 Neuraminidase (P0720S, New England Biolabs, Ipswich) at a concentration of 250 U/mL in the supplied reaction buffer and incubated each separately on arrays containing the captured or spotted glycoproteins overnight at 37°C. .. The arrays not treated with enzymes were incubated with the enzyme reaction buffer in the same conditions.

    Article Title: Sialic acids as cellular markers of immunomodulatory action of dexamethasone on glioma cells of different immunogenicity
    Article Snippet: Sialic acid-dependent binding of Siglec-F was confirmed using α-neuraminidase. .. Briefly, the growing cells were incubated with α-neuraminidase (100 U/ml, from Clostridium perfringens , New England Biolabs) for 24 h at 37 °C. .. α-Neuraminidase activity assay The total Neu activity was assayed using Amplex Red Neuraminidase Assay Kit (Invitrogen) following manufacturer’s instruction.

    other:

    Article Title: The human milk oligosaccharide disialyllacto-N-tetraose prevents necrotising enterocolitis in neonatal rats
    Article Snippet: Linkage promiscuous neuraminidase (α2–3 > 6,8,9; Arthrobacter ureafaciens ) was purchased from Sigma Aldrich (St Louis, Missouri, USA); α2–3-specific neuraminidase ( Salmonella typhimurium ), β1–3 galactosidase ( Xanthomonas manihotis ), β1–4 galactosidase ( Bacteroides fragilis ) and β-N-acetyl-glucosaminidase (GlcNAcase, X manihotis ) were obtained from New England Biolabs (Ipswich, Massachusetts, USA).

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  • 94
    New England Biolabs α2 3 neuraminidase
    Impact of Fc Glycosylation (A) Impact of Fc glycosylation on neutralizing activity. Comparison of the neutralizing activities of wild-type IgG1, wild-type IgA1, and IgA1 in which the glycosylation consensus sequences at position 263 or 459 have been removed. (B) Comparison of the complex glycoforms of IgG1 and IgA1 and the oligomannose-type glycoform of IgA1 expressed in 293S cells (IgA S). (C) Impact of neuraminidase treatment on the neutralization of rg-A/Chicken/Vietnam/C58/2004 (H5N3). The neutralizing activity of the indicated antibodies incubated either with <t>α2–3</t> neuraminidase from Salmonella typhimurium LT2 (NA S) or α2–3,6,8,9 neuraminidase A from Arthrobacter ureafaciens (NA A) was compared to that of the mock-treated IgA1 and IgG1 molecules. (D) Impact of Fc glycosylation on hemagglutination inhibition. A constant amount of the indicated virus was incubated with titrated amounts of the indicated antibodies and added to chicken erythrocytes that were then allowed to sediment at room temperature. (E) Impact of prolonged incubation with virus. Virus and titrated amounts of the indicated isotype of mAb 3.1 were incubated for either 1 hr or overnight before residual infectivity was determined.
    α2 3 Neuraminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α2 3 neuraminidase/product/New England Biolabs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α2 3 neuraminidase - by Bioz Stars, 2021-06
    94/100 stars
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    Impact of Fc Glycosylation (A) Impact of Fc glycosylation on neutralizing activity. Comparison of the neutralizing activities of wild-type IgG1, wild-type IgA1, and IgA1 in which the glycosylation consensus sequences at position 263 or 459 have been removed. (B) Comparison of the complex glycoforms of IgG1 and IgA1 and the oligomannose-type glycoform of IgA1 expressed in 293S cells (IgA S). (C) Impact of neuraminidase treatment on the neutralization of rg-A/Chicken/Vietnam/C58/2004 (H5N3). The neutralizing activity of the indicated antibodies incubated either with α2–3 neuraminidase from Salmonella typhimurium LT2 (NA S) or α2–3,6,8,9 neuraminidase A from Arthrobacter ureafaciens (NA A) was compared to that of the mock-treated IgA1 and IgG1 molecules. (D) Impact of Fc glycosylation on hemagglutination inhibition. A constant amount of the indicated virus was incubated with titrated amounts of the indicated antibodies and added to chicken erythrocytes that were then allowed to sediment at room temperature. (E) Impact of prolonged incubation with virus. Virus and titrated amounts of the indicated isotype of mAb 3.1 were incubated for either 1 hr or overnight before residual infectivity was determined.

    Journal: Cell Reports

    Article Title: Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses

    doi: 10.1016/j.celrep.2018.03.027

    Figure Lengend Snippet: Impact of Fc Glycosylation (A) Impact of Fc glycosylation on neutralizing activity. Comparison of the neutralizing activities of wild-type IgG1, wild-type IgA1, and IgA1 in which the glycosylation consensus sequences at position 263 or 459 have been removed. (B) Comparison of the complex glycoforms of IgG1 and IgA1 and the oligomannose-type glycoform of IgA1 expressed in 293S cells (IgA S). (C) Impact of neuraminidase treatment on the neutralization of rg-A/Chicken/Vietnam/C58/2004 (H5N3). The neutralizing activity of the indicated antibodies incubated either with α2–3 neuraminidase from Salmonella typhimurium LT2 (NA S) or α2–3,6,8,9 neuraminidase A from Arthrobacter ureafaciens (NA A) was compared to that of the mock-treated IgA1 and IgG1 molecules. (D) Impact of Fc glycosylation on hemagglutination inhibition. A constant amount of the indicated virus was incubated with titrated amounts of the indicated antibodies and added to chicken erythrocytes that were then allowed to sediment at room temperature. (E) Impact of prolonged incubation with virus. Virus and titrated amounts of the indicated isotype of mAb 3.1 were incubated for either 1 hr or overnight before residual infectivity was determined.

    Article Snippet: Exoglycosidase Sequencing of N-Linked Glycans The 2-AA labeled glycans were sequentially digested using the following exoglycosidases according to the manufacturers’ instructions: α2-3,6,8 neuraminidase from Clostridium perfringens (New England Biolabs, Hertfordshire, UK), α2-3 neuraminidase from Streptococcus pneumoniae (New England BioLabs, Hertfordshire, UK), β1,4-galactosidase from Bacteroides fragilis (New England Biolabs, Hertfordshire, UK), and α-L-fucosidase from bovine kidney (Sigma-Aldrich, Dorset, UK), β-N -acetylglucosaminidase from Xanthomonas manihotis (New England Biolabs, Hertfordshire, UK), and α(1–2,3,6)-mannosidase from Jack bean (Sigma-Aldrich, Dorset, UK).

    Techniques: Activity Assay, Neutralization, Incubation, HI Assay, Infection

    SPR analysis of bindings of lectin and SKM9-2 to glycosidase-treated SKMepmin3. Purified SKMepmin3 was incubated with α2-3 Neuraminidase S, Neuraminidase A, or Neuraminidase A + O -Glycosidase; and then was immobilized as a ligand on Ni 2+ -binding sensor chip NTA. The analytes were used at a concentration of 5 µg/mL. ( a ) ABA, ( b ) Jacalin, ( c ) rACG, ( d ) SKM9-2. Glycosidase-digested sample was not tested in the experiment with rACG.

    Journal: Scientific Reports

    Article Title: Identification of mesothelioma-specific sialylated epitope recognized with monoclonal antibody SKM9-2 in a mucin-like membrane protein HEG1

    doi: 10.1038/s41598-018-32534-8

    Figure Lengend Snippet: SPR analysis of bindings of lectin and SKM9-2 to glycosidase-treated SKMepmin3. Purified SKMepmin3 was incubated with α2-3 Neuraminidase S, Neuraminidase A, or Neuraminidase A + O -Glycosidase; and then was immobilized as a ligand on Ni 2+ -binding sensor chip NTA. The analytes were used at a concentration of 5 µg/mL. ( a ) ABA, ( b ) Jacalin, ( c ) rACG, ( d ) SKM9-2. Glycosidase-digested sample was not tested in the experiment with rACG.

    Article Snippet: Deglycosylation analysis Cell lysate or SKMepmin3 was treated with α2-3 Neuraminidase S, α2-3, 6, 8, 9 Neuraminidase A, and O -Glycosidase (New England Biolabs Japan, Tokyo, Japan) in 50 mM sodium phosphate (pH 7.5) containing 1% Nonidet P-40, according to the manufacturer’s instructions.

    Techniques: SPR Assay, Purification, Incubation, Binding Assay, Chromatin Immunoprecipitation, Concentration Assay

    SKM9-2 epitope produced from mesothelioma cells. ( a ) Chromatogram of SKMepmin3 separation using anion exchange column. SKMepmin3 produced from HEK293T (blue line) or ACC-MESO4 (pink line) was affinity-purified using SKM9-2-immobilized resins and separated by Mini Q 4.6/50 PE. A major peak of SKMepmin3 purified from HEK293T contained two disialyl T antigens (Fig. 6 ). ( b ) Western blotting for epitope-fused GPI-anchor protein (7.6231) treated with neuraminidases. Cell lysate of 7.6231-transfected ACC-MESO1 (top panel), ACC-MESO4 (middle panel), or HEK293T (lower panel) was treated with α2-3 Neuraminidase S or Neuraminidase A, resolved by 4–15% SDS-PAGE, and analyzed by western blotting using SKM9-2. ( c ) Western blotting for full-length HEG1 treated with neuraminidases. Cell lysates of ACC-MESO4 (upper panel) and HEG1-transfected HEK293T (lower panel) were treated with α2-3 Neuraminidase S or Neuraminidase A and analyzed by 6% SDS-PAGE and western blotting using SKM9-2. ( d ) Schematic of SKM9-2 epitope. Full-length blots are presented in Supplementary Fig. S10 .

    Journal: Scientific Reports

    Article Title: Identification of mesothelioma-specific sialylated epitope recognized with monoclonal antibody SKM9-2 in a mucin-like membrane protein HEG1

    doi: 10.1038/s41598-018-32534-8

    Figure Lengend Snippet: SKM9-2 epitope produced from mesothelioma cells. ( a ) Chromatogram of SKMepmin3 separation using anion exchange column. SKMepmin3 produced from HEK293T (blue line) or ACC-MESO4 (pink line) was affinity-purified using SKM9-2-immobilized resins and separated by Mini Q 4.6/50 PE. A major peak of SKMepmin3 purified from HEK293T contained two disialyl T antigens (Fig. 6 ). ( b ) Western blotting for epitope-fused GPI-anchor protein (7.6231) treated with neuraminidases. Cell lysate of 7.6231-transfected ACC-MESO1 (top panel), ACC-MESO4 (middle panel), or HEK293T (lower panel) was treated with α2-3 Neuraminidase S or Neuraminidase A, resolved by 4–15% SDS-PAGE, and analyzed by western blotting using SKM9-2. ( c ) Western blotting for full-length HEG1 treated with neuraminidases. Cell lysates of ACC-MESO4 (upper panel) and HEG1-transfected HEK293T (lower panel) were treated with α2-3 Neuraminidase S or Neuraminidase A and analyzed by 6% SDS-PAGE and western blotting using SKM9-2. ( d ) Schematic of SKM9-2 epitope. Full-length blots are presented in Supplementary Fig. S10 .

    Article Snippet: Deglycosylation analysis Cell lysate or SKMepmin3 was treated with α2-3 Neuraminidase S, α2-3, 6, 8, 9 Neuraminidase A, and O -Glycosidase (New England Biolabs Japan, Tokyo, Japan) in 50 mM sodium phosphate (pH 7.5) containing 1% Nonidet P-40, according to the manufacturer’s instructions.

    Techniques: Produced, Affinity Purification, Purification, Western Blot, Transfection, SDS Page

    The binding of Siglec-F/Fc Chimera to GL261 ( a ) and SMA560 ( b ) glioma cells. Representative histograms were obtained from flow cytometric analysis of 10,000 cells and show isotype control (light grey line); control cells (dropped line) and cells exposed to Dex (black line). d, e each column presents mean ± SD of 3–5 independent experiments. The histograms ( c ) and appropriate bar graphs ( f ) showing cells treated with α-neuraminidase used here as positive control are also included (light grey line); control cells (dropped line) and α-neuraminidase treated cells (black line). Data are presented as a percentage of control group (100%); * p

    Journal: Molecular and Cellular Biochemistry

    Article Title: Sialic acids as cellular markers of immunomodulatory action of dexamethasone on glioma cells of different immunogenicity

    doi: 10.1007/s11010-018-3478-6

    Figure Lengend Snippet: The binding of Siglec-F/Fc Chimera to GL261 ( a ) and SMA560 ( b ) glioma cells. Representative histograms were obtained from flow cytometric analysis of 10,000 cells and show isotype control (light grey line); control cells (dropped line) and cells exposed to Dex (black line). d, e each column presents mean ± SD of 3–5 independent experiments. The histograms ( c ) and appropriate bar graphs ( f ) showing cells treated with α-neuraminidase used here as positive control are also included (light grey line); control cells (dropped line) and α-neuraminidase treated cells (black line). Data are presented as a percentage of control group (100%); * p

    Article Snippet: Briefly, the growing cells were incubated with α-neuraminidase (100 U/ml, from Clostridium perfringens , New England Biolabs) for 24 h at 37 °C.

    Techniques: Binding Assay, Flow Cytometry, Positive Control

    MALDI-TOF mass spectrometry of intact immunopurified VDBP and enzymatically released glycans diagnostic capacity. A. MALDI-TOF mass spectrometry of immunoprecipitated and linearized VDBP from a representative pool of study patients. The peak intensity represented in as an individual ‘densitometry’ lane below the chart, reflects higher plasma concentrations of VDBP. The majority of intact forms of VDBP from plasma and synovial fluid have a peak mass of 52,900 m / z (represented by the red dashed line). A peak shift towards the right resulting in a ‘shoulder’ is apparent, indicating higher mass variants or isoforms of VDBP are also present in both fluids. B. MALDI-TOF mass spectrometry of HILIC enriched glycan released by α2-3 neuraminidase digest from immunopurified VDBP from the synovial fluid of oligoarticular patients. Glycan peaks at 237.65 m / z and 435.58 m / z , representing release of sialic acid residues, are indicated by the red encircled bands within individual patient ‘densitometry’ lanes. There is a significant 72.4 fold difference in the normalized 237.65 m / z peak heights between persistent and extended-to-be oligoarticular patients, signifying few sialic acid modifications detected in the VDBP taken from the latter patients ( p = 0.0014). C. Receiver operator characteristic curves to test the sensitivity and specificity of VDBP (black line) and CRP (red line) ELISA concentration values and DIGE derived normalized volumes for spot 873 (green line) and sialic acid (peak 237.65 m / z ; blue line) released from VDBP to discern patients at risk of disease spread. Area under the curve and p values for each test are also included in the accompanying table.

    Journal: Journal of Proteomics

    Article Title: Vitamin D binding protein isoforms as candidate predictors of disease extension in childhood arthritis

    doi: 10.1016/j.jprot.2012.06.024

    Figure Lengend Snippet: MALDI-TOF mass spectrometry of intact immunopurified VDBP and enzymatically released glycans diagnostic capacity. A. MALDI-TOF mass spectrometry of immunoprecipitated and linearized VDBP from a representative pool of study patients. The peak intensity represented in as an individual ‘densitometry’ lane below the chart, reflects higher plasma concentrations of VDBP. The majority of intact forms of VDBP from plasma and synovial fluid have a peak mass of 52,900 m / z (represented by the red dashed line). A peak shift towards the right resulting in a ‘shoulder’ is apparent, indicating higher mass variants or isoforms of VDBP are also present in both fluids. B. MALDI-TOF mass spectrometry of HILIC enriched glycan released by α2-3 neuraminidase digest from immunopurified VDBP from the synovial fluid of oligoarticular patients. Glycan peaks at 237.65 m / z and 435.58 m / z , representing release of sialic acid residues, are indicated by the red encircled bands within individual patient ‘densitometry’ lanes. There is a significant 72.4 fold difference in the normalized 237.65 m / z peak heights between persistent and extended-to-be oligoarticular patients, signifying few sialic acid modifications detected in the VDBP taken from the latter patients ( p = 0.0014). C. Receiver operator characteristic curves to test the sensitivity and specificity of VDBP (black line) and CRP (red line) ELISA concentration values and DIGE derived normalized volumes for spot 873 (green line) and sialic acid (peak 237.65 m / z ; blue line) released from VDBP to discern patients at risk of disease spread. Area under the curve and p values for each test are also included in the accompanying table.

    Article Snippet: Equal quantities of denatured VDBP were treated with α2-3 neuraminidase (sialidase) overnight at 4 °C to remove sialic acid residues (New England Biolabs Inc., Ipswich, MA, USA).

    Techniques: Mass Spectrometry, Diagnostic Assay, Immunoprecipitation, Hydrophilic Interaction Liquid Chromatography, Enzyme-linked Immunosorbent Assay, Concentration Assay, Derivative Assay