neuraminidase  (New England Biolabs)


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    Name:
    a2 3 Neuraminidase S
    Description:

    Catalog Number:
    P0743
    Price:
    282
    Category:
    Glycosidases
    Applications:
    Proteomics & Glycomics
    Size:
    2000 units
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    Structured Review

    New England Biolabs neuraminidase
    a2 3 Neuraminidase S

    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, 2021-09
    94/100 stars

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    other:

    Article Title: Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses
    Article Snippet: Neuraminidase S (α2-3: New England Biolabs, Ipswich, MA, USA) and neuraminidase A (α2-3,6,8,9: New England Biolabs, Ipswich, MA, USA) were used to desialylate IgA1.

    Article Title: Evaluation of a glycoengineered monoclonal antibody via LC-MS analysis in combination with multiple enzymatic digestion
    Article Snippet: Trypsin-ultra (P8101S), PNGase F (P0708S), α2-3 Neuraminidase S (P0743S), α2-3,6,8,9 Neuraminidase A (P0722S), Remove-iT Endo S (P0741S) are products from New England Biolabs.

    Article Title: Detection and Characterization of Phosphorylation, Glycosylation, and Fatty Acid Bound to Fetuin A in Human Blood
    Article Snippet: The de-O-glycosylation of Fet A was performed with the commercial kit from BioLabs Neuraminidase a2-3, 6, 8, Neuraminidase + O-Glycosidase and for de-N-glycosylation of fetuin A PNGase F from BioLabs Inc (New England, Ipswich, MA, USA) was used.

    Article Title: Analyses of N-linked glycans of PrPSc revealed predominantly 2,6-linked sialic acid residues
    Article Snippet: The subsequent treatment with either Streptococcus pneumoniae (catalog no. P0743L, New England Biolabs) or Arthrobacter ureafaciens sialidase (catalog no. P0722L, New England Biolabs) was as follows.

    Article Title: A Novel Sialylation Site on Neisseria gonorrhoeae Lipooligosaccharide Links Heptose II Lactose Expression with Pathogenicity
    Article Snippet: Desialylation was carried out with α2-3-specific neuraminidase (catalog number P0743S; New England BioLabs).

    Article Title: A cell-free biosynthesis platform for modular construction of protein glycosylation pathways
    Article Snippet: The exoglycosidases and associated product numbers used in this study are: β1-4 Galactosidase S (P0745S); α1-3,6 Galactosidase (P0731S); α1-3,4 Fucosidase (P0769S); and α1-2 Fucosidase (P0724S); α1-3,4,6 Galactosidase (P0747S); β-N-Acetylglucosaminidase S (P0744S); α2-3 Neuraminidase S (P0743S); and α2-3,6,8 Neuraminidase (P0720S).

    Article Title: Evidence of Human Milk Oligosaccharides in Cord Blood and Maternal-to-Fetal Transport across the Placenta
    Article Snippet: Analysis of Human Milk Oligosaccharides by Enzymatic Digest To confirm the identity of individual peaks in the serum, 2AB-labelled samples were either treated with α2-3-neuraminidase (New England Biolabs, #P0743L) or α1-2-fucosidase (New England Biolabs, #P0724S) according to the manufacturer’s instructions.

    Incubation:

    Article Title: Analyses of N-linked glycans of PrPSc revealed predominantly 2,6-linked sialic acid residues
    Article Snippet: .. For sialidase treatment, after addition of 10% (v/v) sialidase buffer GlycoBuffer1 supplied by the enzyme manufacturer, 500 units/ml of sialidase or an equal volume of water for mock treatment was added, followed by incubation on a shaker at 37 °C for 12 h. The sialidases used were from Streptococcus pneumoniae (catalog no. P0743L, New England Biolabs, Ipswich, MA, USA), Clostridium perfringens (catalog no. P0720L, New England Biolabs), or Arthrobacter ureafaciens (catalog no. P0722L, New England Biolabs). ..

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  • 94
    New England Biolabs pngase f native
    Altered mobility of α-DG in COG-deficient CHO cells is a function of COG-dependent defects in O- glycosylation. A , representative Western blotting of WT CHO and ldlB cell lysates with or without <t>PNGase</t> F digestion ( n = 2). The cells were treated with or without V. cholerae neuraminidase (120 milliunits/ml) prior to lysis. B , cells were cultured with increasing concentrations of a furin inhibitor, and Western blotting analysis was performed on lysates using an anti-DG (core) antibody ( n = 2). Furin inhibition results in a comparable increase in the apparent molecular weight of α-DG in both WT CHO and ldlB cells. C , cells were treated with two different amounts (60 or 120 milliunits/ml) of V. cholerae neuraminidase, and Western blotting analysis was performed. D , Western blotting of α-DG in WT, ldlB, and cog1 -corrected ldlB cells treated with or without V. cholerae neuraminidase ( n = 2). IB , immunoblot.
    Pngase F Native, 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/pngase f native/product/New England Biolabs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    86
    New England Biolabs sialidase activity
    Composition of substitution mutations with respect to consensus sequences. Percentages represent the mean across eight M. synoviae strains for nanI , nagA , nanA , nagC , nanE , and nagB genes of the <t>sialidase</t> locus, and three M. hyopneumoniae strains for housekeeping genes dnaA and ftsY .
    Sialidase Activity, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    95
    New England Biolabs α2 3 neuraminidase
    EICs of A2G2S2, A2G2S1 and A2G2 glycopeptides in non-treated (a-c) , <t>α2–3</t> neuraminidase treated (d-f) and α2–3,6,8,9 neuraminidase treated samples (g-i) . The peaks at 37.3 min and 39.2 min in (a) showed sensitivity for α2–3 neuraminidase, which disappeared after enzymatic digestion (d) , indicating these two peaks were containing at least one sialic acid that were α2–3 linked to galactose. Upon α2–3 neuraminidase digestion, A2G2S1 can be detected (e) , which were not originally in sample (b) . Since the 35.5 min peak in (a) remained after α2–3 neuraminidase digestion (d) , both the sialic acid linkages can be assigned α2–6. Comparing the intensities between (e) and (f) , the 37.3 min peak in (a) .
    α2 3 Neuraminidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, 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 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α2 3 neuraminidase - by Bioz Stars, 2021-09
    95/100 stars
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    Altered mobility of α-DG in COG-deficient CHO cells is a function of COG-dependent defects in O- glycosylation. A , representative Western blotting of WT CHO and ldlB cell lysates with or without PNGase F digestion ( n = 2). The cells were treated with or without V. cholerae neuraminidase (120 milliunits/ml) prior to lysis. B , cells were cultured with increasing concentrations of a furin inhibitor, and Western blotting analysis was performed on lysates using an anti-DG (core) antibody ( n = 2). Furin inhibition results in a comparable increase in the apparent molecular weight of α-DG in both WT CHO and ldlB cells. C , cells were treated with two different amounts (60 or 120 milliunits/ml) of V. cholerae neuraminidase, and Western blotting analysis was performed. D , Western blotting of α-DG in WT, ldlB, and cog1 -corrected ldlB cells treated with or without V. cholerae neuraminidase ( n = 2). IB , immunoblot.

    Journal: The Journal of Biological Chemistry

    Article Title: Defective mucin-type glycosylation on α-dystroglycan in COG-deficient cells increases its susceptibility to bacterial proteases

    doi: 10.1074/jbc.RA118.003014

    Figure Lengend Snippet: Altered mobility of α-DG in COG-deficient CHO cells is a function of COG-dependent defects in O- glycosylation. A , representative Western blotting of WT CHO and ldlB cell lysates with or without PNGase F digestion ( n = 2). The cells were treated with or without V. cholerae neuraminidase (120 milliunits/ml) prior to lysis. B , cells were cultured with increasing concentrations of a furin inhibitor, and Western blotting analysis was performed on lysates using an anti-DG (core) antibody ( n = 2). Furin inhibition results in a comparable increase in the apparent molecular weight of α-DG in both WT CHO and ldlB cells. C , cells were treated with two different amounts (60 or 120 milliunits/ml) of V. cholerae neuraminidase, and Western blotting analysis was performed. D , Western blotting of α-DG in WT, ldlB, and cog1 -corrected ldlB cells treated with or without V. cholerae neuraminidase ( n = 2). IB , immunoblot.

    Article Snippet: A. ureafaciens neuraminidase (P0722) PNGase F (P0704S) were purchased from New England Biolabs.

    Techniques: Western Blot, Lysis, Cell Culture, Inhibition, Molecular Weight

    Composition of substitution mutations with respect to consensus sequences. Percentages represent the mean across eight M. synoviae strains for nanI , nagA , nanA , nagC , nanE , and nagB genes of the sialidase locus, and three M. hyopneumoniae strains for housekeeping genes dnaA and ftsY .

    Journal: Microbial pathogenesis

    Article Title: Genetic Variation in Sialidase and Linkage to N-acetylneuraminate Catabolism in Mycoplasma synoviae

    doi: 10.1016/j.micpath.2008.02.002

    Figure Lengend Snippet: Composition of substitution mutations with respect to consensus sequences. Percentages represent the mean across eight M. synoviae strains for nanI , nagA , nanA , nagC , nanE , and nagB genes of the sialidase locus, and three M. hyopneumoniae strains for housekeeping genes dnaA and ftsY .

    Article Snippet: Genomic DNA from the strains with the highest (WVU1853T ) and lowest (K4907A and K5395B) levels of sialidase activity was digested with endonuclease Vsp I (New England Biolabs, Ipswich, Massachusetts), then separated on a 0.6% agarose gel.

    Techniques:

    EICs of A2G2S2, A2G2S1 and A2G2 glycopeptides in non-treated (a-c) , α2–3 neuraminidase treated (d-f) and α2–3,6,8,9 neuraminidase treated samples (g-i) . The peaks at 37.3 min and 39.2 min in (a) showed sensitivity for α2–3 neuraminidase, which disappeared after enzymatic digestion (d) , indicating these two peaks were containing at least one sialic acid that were α2–3 linked to galactose. Upon α2–3 neuraminidase digestion, A2G2S1 can be detected (e) , which were not originally in sample (b) . Since the 35.5 min peak in (a) remained after α2–3 neuraminidase digestion (d) , both the sialic acid linkages can be assigned α2–6. Comparing the intensities between (e) and (f) , the 37.3 min peak in (a) .

    Journal: Analytical chemistry

    Article Title: Isomeric Separation of N-Glycopeptides Derived from Glycoproteins by Porous Graphitic Carbon (PGC) LC-MS/MS

    doi: 10.1021/acs.analchem.0c00668

    Figure Lengend Snippet: EICs of A2G2S2, A2G2S1 and A2G2 glycopeptides in non-treated (a-c) , α2–3 neuraminidase treated (d-f) and α2–3,6,8,9 neuraminidase treated samples (g-i) . The peaks at 37.3 min and 39.2 min in (a) showed sensitivity for α2–3 neuraminidase, which disappeared after enzymatic digestion (d) , indicating these two peaks were containing at least one sialic acid that were α2–3 linked to galactose. Upon α2–3 neuraminidase digestion, A2G2S1 can be detected (e) , which were not originally in sample (b) . Since the 35.5 min peak in (a) remained after α2–3 neuraminidase digestion (d) , both the sialic acid linkages can be assigned α2–6. Comparing the intensities between (e) and (f) , the 37.3 min peak in (a) .

    Article Snippet: Murine IgG1 (Intact mAb Mass Check Standard) was obtained from Waters Corporation (Milford, MA). α2–3 neuraminidase, α2–3,6,8,9 neuraminidase, β1–3 galactosidase, β1–4 galactosidase and β1–3,4 galactosidase were acquired from New England Biolabs (Ipswich, MA).

    Techniques:

    N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with α2-3 linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.

    Journal: Frontiers in Oncology

    Article Title: Alterations of the Human Skin N- and O-Glycome in Basal Cell Carcinoma and Squamous Cell Carcinoma

    doi: 10.3389/fonc.2018.00070

    Figure Lengend Snippet: N -glycosylation changes in squamous cell carcinoma (SCC). (A) Supervised hierarchical cluster analysis of healthy and tumor skin. Rows display each of the 15 patient glycan data (T, tumor tissue; C, healthy control). Columns indicate the N -glycan ID. Five clusters can be observed: in healthy tissue N -glycans with α2-3 linked N -acetylneuraminic acid (NeuAc) appeared to be present in increased levels whereas α2-6-NeuAc and oligomannose N -glycan levels were higher in tumor tissue. (B) Statistical evaluation of sialylated and oligomannose N -glycans uncovered significant changes [ p ≤ 0.04, using a t -test, indicated by an asterisk (*)]. Oligomannose N -glycans were upregulated whereas α2-3 linked NeuAc carrying N -glycans were down regulated in SCC.

    Article Snippet: The glycan sample was reconstituted in 10 μL 25 mM ammonium acetate buffer (pH 5.5) and 25 U of a α2-3-specific neuraminidase (NEB, Ipswitch, MA, USA) were added.

    Techniques:

    Healthy human skin N -glycome. (A) Bean diagram representing the 10 most abundant N -glycans determined from 14 patients. Green bars indicate individual data points, the black line represents the median, and the gray area depicts the data density. Columns indicate the glycan structures given by their glycan ID (Table S1 in Supplementary Material). (B) Relative N -glycan class abundances found in healthy skin biopsies. Sialylated and fucosylated structures were the major components representing the human skin N -glycome. (C) Relative abundances of different structure features found on sialylated N -glycans. Blue bars represent sialylated N -glycans with and without core fucose depending on their sialic acid linkage, showing that core fucosylation was a more abundant feature on N -glycans carrying one or two α2-3 linked N -acetylneuraminic acid (NeuAc) residues (if both, α2-3 and α2-6 linkages were present on one N- glycan, this N -glycan was considered in both linkage categories). Overall, α2-6-linked NeuAc was a slightly more abundant feature compared with α2-3-linked NeuAc. Most of the sialylated N -glycans carried two NeuAc residues. Tri-antennary species were below 3% and rather low abundant using porous graphitized carbon, while multiplexed capillary gel electrophoresis with laser induced fluorescence detection (xCGE-LIF) detected slightly higher levels of tri- and tetra-antennary N -glycans (see Supplementary file “xCGE-LIF quant.xlsx” in Supplementary Material).

    Journal: Frontiers in Oncology

    Article Title: Alterations of the Human Skin N- and O-Glycome in Basal Cell Carcinoma and Squamous Cell Carcinoma

    doi: 10.3389/fonc.2018.00070

    Figure Lengend Snippet: Healthy human skin N -glycome. (A) Bean diagram representing the 10 most abundant N -glycans determined from 14 patients. Green bars indicate individual data points, the black line represents the median, and the gray area depicts the data density. Columns indicate the glycan structures given by their glycan ID (Table S1 in Supplementary Material). (B) Relative N -glycan class abundances found in healthy skin biopsies. Sialylated and fucosylated structures were the major components representing the human skin N -glycome. (C) Relative abundances of different structure features found on sialylated N -glycans. Blue bars represent sialylated N -glycans with and without core fucose depending on their sialic acid linkage, showing that core fucosylation was a more abundant feature on N -glycans carrying one or two α2-3 linked N -acetylneuraminic acid (NeuAc) residues (if both, α2-3 and α2-6 linkages were present on one N- glycan, this N -glycan was considered in both linkage categories). Overall, α2-6-linked NeuAc was a slightly more abundant feature compared with α2-3-linked NeuAc. Most of the sialylated N -glycans carried two NeuAc residues. Tri-antennary species were below 3% and rather low abundant using porous graphitized carbon, while multiplexed capillary gel electrophoresis with laser induced fluorescence detection (xCGE-LIF) detected slightly higher levels of tri- and tetra-antennary N -glycans (see Supplementary file “xCGE-LIF quant.xlsx” in Supplementary Material).

    Article Snippet: The glycan sample was reconstituted in 10 μL 25 mM ammonium acetate buffer (pH 5.5) and 25 U of a α2-3-specific neuraminidase (NEB, Ipswitch, MA, USA) were added.

    Techniques: Nucleic Acid Electrophoresis, Fluorescence