α 1  (New England Biolabs)


Bioz Verified Symbol New England Biolabs is a verified supplier
Bioz Manufacturer Symbol New England Biolabs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94
    Name:
    alpha 1 6 Mannosidase
    Description:
    alpha 1 6 Mannosidase 4 000 units
    Catalog Number:
    p0727l
    Price:
    518
    Size:
    4 000 units
    Category:
    Glycosidases
    Buy from Supplier


    Structured Review

    New England Biolabs α 1
    alpha 1 6 Mannosidase
    alpha 1 6 Mannosidase 4 000 units
    https://www.bioz.com/result/α 1/product/New England Biolabs
    Average 94 stars, based on 18 article reviews
    Price from $9.99 to $1999.99
    α 1 - by Bioz Stars, 2020-07
    94/100 stars

    Images

    1) Product Images from "Mnn10 Maintains Pathogenicity in Candida albicans by Extending α-1,6-Mannose Backbone to Evade Host Dectin-1 Mediated Antifungal Immunity"

    Article Title: Mnn10 Maintains Pathogenicity in Candida albicans by Extending α-1,6-Mannose Backbone to Evade Host Dectin-1 Mediated Antifungal Immunity

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.1005617

    Mnn10 has mannosyltransferase activity and is required for α-1,6-mannose backbone length. (A) Mannosyltransferase activity assay of Mnn10. The reaction of expressed MBP-fused Mnn10 protein or MBP protein incubated with α-1,6-mannobiose (Man 2), GDP-mannose (GDP-Man) or controls. The reaction products were labeled with ANTS and separated by fluorophore-assisted carbohydrate gel electrophoresis (FACE). Man 3, mannotriose; Man 4, mannotetraose. (B) α-1,6-mannose assay. The reaction products of (A) were treated with or without α-1,6-mannosidase treatment, and then subjected to FACE. (C) Representative cell wall ultrastructures of SN152, mnn10Δ/Δ :: MNN10 and mnn10Δ/Δ strains were observed by transmission electron microscopy. The scale bar represents 0.2 μm. (D) Alcian Blue binding assay. The cells were incubated with Alcian Blue for 10 min and the amount of dye bound to the cell wall were calculated. Data represent the mean amount of dye bound per cell ± SD from triplicates of one representative experiment of three. (E) Cell surface hydrophobicity of the indicated C . albicans strains was measured by water-hydrocarbon two-phase assay. Data are means ± SD of triplicates of one representative experiment of three. **, P
    Figure Legend Snippet: Mnn10 has mannosyltransferase activity and is required for α-1,6-mannose backbone length. (A) Mannosyltransferase activity assay of Mnn10. The reaction of expressed MBP-fused Mnn10 protein or MBP protein incubated with α-1,6-mannobiose (Man 2), GDP-mannose (GDP-Man) or controls. The reaction products were labeled with ANTS and separated by fluorophore-assisted carbohydrate gel electrophoresis (FACE). Man 3, mannotriose; Man 4, mannotetraose. (B) α-1,6-mannose assay. The reaction products of (A) were treated with or without α-1,6-mannosidase treatment, and then subjected to FACE. (C) Representative cell wall ultrastructures of SN152, mnn10Δ/Δ :: MNN10 and mnn10Δ/Δ strains were observed by transmission electron microscopy. The scale bar represents 0.2 μm. (D) Alcian Blue binding assay. The cells were incubated with Alcian Blue for 10 min and the amount of dye bound to the cell wall were calculated. Data represent the mean amount of dye bound per cell ± SD from triplicates of one representative experiment of three. (E) Cell surface hydrophobicity of the indicated C . albicans strains was measured by water-hydrocarbon two-phase assay. Data are means ± SD of triplicates of one representative experiment of three. **, P

    Techniques Used: Activity Assay, Incubation, Labeling, Nucleic Acid Electrophoresis, Transmission Assay, Electron Microscopy, Binding Assay, Cell Surface Hydrophobicity

    2) Product Images from "Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis"

    Article Title: Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis

    Journal: Open Biology

    doi: 10.1098/rsob.130022

    Synergy of Sc Mnn9 and Sc Van1. ( a ) FACE gel of ANTS-labelled reaction products of the reaction of Sc Mnn9 (M9), Sc Van1 (V1), GDP-Man, α-1,6-mannobiose (Man2) and MnCl 2 . First lane: Sc Mnn9-D236N and Sc Van1 wild-type were incubated together, the reaction was stopped and the products were labelled before the separation on a FACE gel. The faint band above Man2 is assumed to be leakage from lane 2 (noted on other gels, not shown). Second and third lanes: Sc Mnn9 WT was used in absence of Sc Van1; Sc Mnn9 WT was then removed using a 10 000 MWCO filter, and Sc Van1 WT alone (second lane) or Sc Mnn9-D236N and Sc Van1 WT (third lane) were added to the reaction. The second step of the reaction was stopped and the products were labelled before being separated on a FACE gel. Fourth lane: control in which the substrates were incubated in the absence of enzymes, spun through the filter and subsequently the reaction was carried out by addition of the enzymes. The products formed due to the presence of substrates and GTs. Fifth lane: control in which the enzymes were incubated in the absence of the substrates, removed by the filter and the filtrate was enriched with the substrates. Products did not form due to the absence of GTs. ( b ) Sc Mnn9, Sc Van1, GDP-Man, α-1,6-mannobiose and MnCl 2 were incubated, and the reaction products were either treated (+) or not treated (–) with the B. circulans Aman6 α-1,6-mannosidase. The products after the reaction were labelled with ANTS and run on a FACE gel.
    Figure Legend Snippet: Synergy of Sc Mnn9 and Sc Van1. ( a ) FACE gel of ANTS-labelled reaction products of the reaction of Sc Mnn9 (M9), Sc Van1 (V1), GDP-Man, α-1,6-mannobiose (Man2) and MnCl 2 . First lane: Sc Mnn9-D236N and Sc Van1 wild-type were incubated together, the reaction was stopped and the products were labelled before the separation on a FACE gel. The faint band above Man2 is assumed to be leakage from lane 2 (noted on other gels, not shown). Second and third lanes: Sc Mnn9 WT was used in absence of Sc Van1; Sc Mnn9 WT was then removed using a 10 000 MWCO filter, and Sc Van1 WT alone (second lane) or Sc Mnn9-D236N and Sc Van1 WT (third lane) were added to the reaction. The second step of the reaction was stopped and the products were labelled before being separated on a FACE gel. Fourth lane: control in which the substrates were incubated in the absence of enzymes, spun through the filter and subsequently the reaction was carried out by addition of the enzymes. The products formed due to the presence of substrates and GTs. Fifth lane: control in which the enzymes were incubated in the absence of the substrates, removed by the filter and the filtrate was enriched with the substrates. Products did not form due to the absence of GTs. ( b ) Sc Mnn9, Sc Van1, GDP-Man, α-1,6-mannobiose and MnCl 2 were incubated, and the reaction products were either treated (+) or not treated (–) with the B. circulans Aman6 α-1,6-mannosidase. The products after the reaction were labelled with ANTS and run on a FACE gel.

    Techniques Used: Incubation

    Activity assay of Sc Mnn9 wild-type and mutants. ( a ) FACE gel of the reaction products of Sc Mnn9 wild-type incubated with GDP-Man, α-1,6-mannobiose (Man2) and MnCl 2 or controls. ( b ) Same as ( a ), but incubated with wild-type or mutants of Sc Mnn9. ( c ) Same as ( a ), but incubated with 10 mM of MnCl 2 , other divalent cations or EDTA. ( d ) FACE gel of a reaction containing Sc Mnn9, mannose, GDP-Man and MnCl 2 . The reaction products were either treated or not treated with an α-1,6-mannosidase. ( e ) Diagram of the chemical reaction that is the foundation for the coupled enzyme assay to determine steady-state kinetics for Sc Mnn9. 4MU-Man is extended by Sc Mnn9 to 4MU-Man2, which in turn acts as a minimal substrate for B. circulans Aman6, an α-1,6-mannosidase. The release of fluorescent 4MU was measured at an excitation wavelength of 360 nm and an emission wavelength of 460 nm. ( f ) Bar chart of the measured 4MU released after the reaction of Sc Mnn9 wild-type, D236N and D280N in presence and absence of GDP-Man and Aman6 mannosidase. Error bars indicate the standard error of the mean (s.e.m.), n = 3. ( g , h ) Steady-state kinetics of Sc Mnn9 ( g ) in the presence of GDP-Man (1.2 mM) and variable 4MU-Man concentrations or ( h ) in the presence of 4MU-Man (10 mM) and variable GDP-Man concentrations. Error bars indicate s.e.m., n = 3.
    Figure Legend Snippet: Activity assay of Sc Mnn9 wild-type and mutants. ( a ) FACE gel of the reaction products of Sc Mnn9 wild-type incubated with GDP-Man, α-1,6-mannobiose (Man2) and MnCl 2 or controls. ( b ) Same as ( a ), but incubated with wild-type or mutants of Sc Mnn9. ( c ) Same as ( a ), but incubated with 10 mM of MnCl 2 , other divalent cations or EDTA. ( d ) FACE gel of a reaction containing Sc Mnn9, mannose, GDP-Man and MnCl 2 . The reaction products were either treated or not treated with an α-1,6-mannosidase. ( e ) Diagram of the chemical reaction that is the foundation for the coupled enzyme assay to determine steady-state kinetics for Sc Mnn9. 4MU-Man is extended by Sc Mnn9 to 4MU-Man2, which in turn acts as a minimal substrate for B. circulans Aman6, an α-1,6-mannosidase. The release of fluorescent 4MU was measured at an excitation wavelength of 360 nm and an emission wavelength of 460 nm. ( f ) Bar chart of the measured 4MU released after the reaction of Sc Mnn9 wild-type, D236N and D280N in presence and absence of GDP-Man and Aman6 mannosidase. Error bars indicate the standard error of the mean (s.e.m.), n = 3. ( g , h ) Steady-state kinetics of Sc Mnn9 ( g ) in the presence of GDP-Man (1.2 mM) and variable 4MU-Man concentrations or ( h ) in the presence of 4MU-Man (10 mM) and variable GDP-Man concentrations. Error bars indicate s.e.m., n = 3.

    Techniques Used: Activity Assay, Incubation, Enzymatic Assay

    Related Articles

    High Performance Liquid Chromatography:

    Article Title: Salmonella Typhimurium Enzymatically Landscapes the Host Intestinal Epithelial Cell (IEC) Surface Glycome to Increase Invasion *
    Article Snippet: .. Reduced glycan compounds were fractionated from the total released glycans using HPLC and digested with highly specific exoglycosidase mixtures, including α-2,3-neuraminidase, α-1,2/3-mannosidase, β- N -acetylglucosaminidase (GlcNAcase), β-1,4-galactosidase, and α-1,3/4-fucosidase (New England Biolabs). ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94
    New England Biolabs α 1
    Mnn10 has mannosyltransferase activity and is required for <t>α-1,6-mannose</t> backbone length. (A) Mannosyltransferase activity assay of Mnn10. The reaction of expressed MBP-fused Mnn10 protein or MBP protein incubated with α-1,6-mannobiose (Man 2), GDP-mannose (GDP-Man) or controls. The reaction products were labeled with ANTS and separated by fluorophore-assisted carbohydrate gel electrophoresis (FACE). Man 3, mannotriose; Man 4, mannotetraose. (B) α-1,6-mannose assay. The reaction products of (A) were treated with or without <t>α-1,6-mannosidase</t> treatment, and then subjected to FACE. (C) Representative cell wall ultrastructures of SN152, mnn10Δ/Δ :: MNN10 and mnn10Δ/Δ strains were observed by transmission electron microscopy. The scale bar represents 0.2 μm. (D) Alcian Blue binding assay. The cells were incubated with Alcian Blue for 10 min and the amount of dye bound to the cell wall were calculated. Data represent the mean amount of dye bound per cell ± SD from triplicates of one representative experiment of three. (E) Cell surface hydrophobicity of the indicated C . albicans strains was measured by water-hydrocarbon two-phase assay. Data are means ± SD of triplicates of one representative experiment of three. **, P
    α 1, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α 1/product/New England Biolabs
    Average 94 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    α 1 - by Bioz Stars, 2020-07
    94/100 stars
      Buy from Supplier

    Image Search Results


    Mnn10 has mannosyltransferase activity and is required for α-1,6-mannose backbone length. (A) Mannosyltransferase activity assay of Mnn10. The reaction of expressed MBP-fused Mnn10 protein or MBP protein incubated with α-1,6-mannobiose (Man 2), GDP-mannose (GDP-Man) or controls. The reaction products were labeled with ANTS and separated by fluorophore-assisted carbohydrate gel electrophoresis (FACE). Man 3, mannotriose; Man 4, mannotetraose. (B) α-1,6-mannose assay. The reaction products of (A) were treated with or without α-1,6-mannosidase treatment, and then subjected to FACE. (C) Representative cell wall ultrastructures of SN152, mnn10Δ/Δ :: MNN10 and mnn10Δ/Δ strains were observed by transmission electron microscopy. The scale bar represents 0.2 μm. (D) Alcian Blue binding assay. The cells were incubated with Alcian Blue for 10 min and the amount of dye bound to the cell wall were calculated. Data represent the mean amount of dye bound per cell ± SD from triplicates of one representative experiment of three. (E) Cell surface hydrophobicity of the indicated C . albicans strains was measured by water-hydrocarbon two-phase assay. Data are means ± SD of triplicates of one representative experiment of three. **, P

    Journal: PLoS Pathogens

    Article Title: Mnn10 Maintains Pathogenicity in Candida albicans by Extending α-1,6-Mannose Backbone to Evade Host Dectin-1 Mediated Antifungal Immunity

    doi: 10.1371/journal.ppat.1005617

    Figure Lengend Snippet: Mnn10 has mannosyltransferase activity and is required for α-1,6-mannose backbone length. (A) Mannosyltransferase activity assay of Mnn10. The reaction of expressed MBP-fused Mnn10 protein or MBP protein incubated with α-1,6-mannobiose (Man 2), GDP-mannose (GDP-Man) or controls. The reaction products were labeled with ANTS and separated by fluorophore-assisted carbohydrate gel electrophoresis (FACE). Man 3, mannotriose; Man 4, mannotetraose. (B) α-1,6-mannose assay. The reaction products of (A) were treated with or without α-1,6-mannosidase treatment, and then subjected to FACE. (C) Representative cell wall ultrastructures of SN152, mnn10Δ/Δ :: MNN10 and mnn10Δ/Δ strains were observed by transmission electron microscopy. The scale bar represents 0.2 μm. (D) Alcian Blue binding assay. The cells were incubated with Alcian Blue for 10 min and the amount of dye bound to the cell wall were calculated. Data represent the mean amount of dye bound per cell ± SD from triplicates of one representative experiment of three. (E) Cell surface hydrophobicity of the indicated C . albicans strains was measured by water-hydrocarbon two-phase assay. Data are means ± SD of triplicates of one representative experiment of three. **, P

    Article Snippet: The reaction products were then digested with α-1,6-mannosidase (NEB) overnight at 37°C according to manufacturer’s instructions, and analyzed by FACE.

    Techniques: Activity Assay, Incubation, Labeling, Nucleic Acid Electrophoresis, Transmission Assay, Electron Microscopy, Binding Assay, Cell Surface Hydrophobicity

    Synergy of Sc Mnn9 and Sc Van1. ( a ) FACE gel of ANTS-labelled reaction products of the reaction of Sc Mnn9 (M9), Sc Van1 (V1), GDP-Man, α-1,6-mannobiose (Man2) and MnCl 2 . First lane: Sc Mnn9-D236N and Sc Van1 wild-type were incubated together, the reaction was stopped and the products were labelled before the separation on a FACE gel. The faint band above Man2 is assumed to be leakage from lane 2 (noted on other gels, not shown). Second and third lanes: Sc Mnn9 WT was used in absence of Sc Van1; Sc Mnn9 WT was then removed using a 10 000 MWCO filter, and Sc Van1 WT alone (second lane) or Sc Mnn9-D236N and Sc Van1 WT (third lane) were added to the reaction. The second step of the reaction was stopped and the products were labelled before being separated on a FACE gel. Fourth lane: control in which the substrates were incubated in the absence of enzymes, spun through the filter and subsequently the reaction was carried out by addition of the enzymes. The products formed due to the presence of substrates and GTs. Fifth lane: control in which the enzymes were incubated in the absence of the substrates, removed by the filter and the filtrate was enriched with the substrates. Products did not form due to the absence of GTs. ( b ) Sc Mnn9, Sc Van1, GDP-Man, α-1,6-mannobiose and MnCl 2 were incubated, and the reaction products were either treated (+) or not treated (–) with the B. circulans Aman6 α-1,6-mannosidase. The products after the reaction were labelled with ANTS and run on a FACE gel.

    Journal: Open Biology

    Article Title: Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis

    doi: 10.1098/rsob.130022

    Figure Lengend Snippet: Synergy of Sc Mnn9 and Sc Van1. ( a ) FACE gel of ANTS-labelled reaction products of the reaction of Sc Mnn9 (M9), Sc Van1 (V1), GDP-Man, α-1,6-mannobiose (Man2) and MnCl 2 . First lane: Sc Mnn9-D236N and Sc Van1 wild-type were incubated together, the reaction was stopped and the products were labelled before the separation on a FACE gel. The faint band above Man2 is assumed to be leakage from lane 2 (noted on other gels, not shown). Second and third lanes: Sc Mnn9 WT was used in absence of Sc Van1; Sc Mnn9 WT was then removed using a 10 000 MWCO filter, and Sc Van1 WT alone (second lane) or Sc Mnn9-D236N and Sc Van1 WT (third lane) were added to the reaction. The second step of the reaction was stopped and the products were labelled before being separated on a FACE gel. Fourth lane: control in which the substrates were incubated in the absence of enzymes, spun through the filter and subsequently the reaction was carried out by addition of the enzymes. The products formed due to the presence of substrates and GTs. Fifth lane: control in which the enzymes were incubated in the absence of the substrates, removed by the filter and the filtrate was enriched with the substrates. Products did not form due to the absence of GTs. ( b ) Sc Mnn9, Sc Van1, GDP-Man, α-1,6-mannobiose and MnCl 2 were incubated, and the reaction products were either treated (+) or not treated (–) with the B. circulans Aman6 α-1,6-mannosidase. The products after the reaction were labelled with ANTS and run on a FACE gel.

    Article Snippet: The products were digested with α-1,6-mannosidase (NEB) according to the manufacturer's instructions.

    Techniques: Incubation

    Activity assay of Sc Mnn9 wild-type and mutants. ( a ) FACE gel of the reaction products of Sc Mnn9 wild-type incubated with GDP-Man, α-1,6-mannobiose (Man2) and MnCl 2 or controls. ( b ) Same as ( a ), but incubated with wild-type or mutants of Sc Mnn9. ( c ) Same as ( a ), but incubated with 10 mM of MnCl 2 , other divalent cations or EDTA. ( d ) FACE gel of a reaction containing Sc Mnn9, mannose, GDP-Man and MnCl 2 . The reaction products were either treated or not treated with an α-1,6-mannosidase. ( e ) Diagram of the chemical reaction that is the foundation for the coupled enzyme assay to determine steady-state kinetics for Sc Mnn9. 4MU-Man is extended by Sc Mnn9 to 4MU-Man2, which in turn acts as a minimal substrate for B. circulans Aman6, an α-1,6-mannosidase. The release of fluorescent 4MU was measured at an excitation wavelength of 360 nm and an emission wavelength of 460 nm. ( f ) Bar chart of the measured 4MU released after the reaction of Sc Mnn9 wild-type, D236N and D280N in presence and absence of GDP-Man and Aman6 mannosidase. Error bars indicate the standard error of the mean (s.e.m.), n = 3. ( g , h ) Steady-state kinetics of Sc Mnn9 ( g ) in the presence of GDP-Man (1.2 mM) and variable 4MU-Man concentrations or ( h ) in the presence of 4MU-Man (10 mM) and variable GDP-Man concentrations. Error bars indicate s.e.m., n = 3.

    Journal: Open Biology

    Article Title: Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis

    doi: 10.1098/rsob.130022

    Figure Lengend Snippet: Activity assay of Sc Mnn9 wild-type and mutants. ( a ) FACE gel of the reaction products of Sc Mnn9 wild-type incubated with GDP-Man, α-1,6-mannobiose (Man2) and MnCl 2 or controls. ( b ) Same as ( a ), but incubated with wild-type or mutants of Sc Mnn9. ( c ) Same as ( a ), but incubated with 10 mM of MnCl 2 , other divalent cations or EDTA. ( d ) FACE gel of a reaction containing Sc Mnn9, mannose, GDP-Man and MnCl 2 . The reaction products were either treated or not treated with an α-1,6-mannosidase. ( e ) Diagram of the chemical reaction that is the foundation for the coupled enzyme assay to determine steady-state kinetics for Sc Mnn9. 4MU-Man is extended by Sc Mnn9 to 4MU-Man2, which in turn acts as a minimal substrate for B. circulans Aman6, an α-1,6-mannosidase. The release of fluorescent 4MU was measured at an excitation wavelength of 360 nm and an emission wavelength of 460 nm. ( f ) Bar chart of the measured 4MU released after the reaction of Sc Mnn9 wild-type, D236N and D280N in presence and absence of GDP-Man and Aman6 mannosidase. Error bars indicate the standard error of the mean (s.e.m.), n = 3. ( g , h ) Steady-state kinetics of Sc Mnn9 ( g ) in the presence of GDP-Man (1.2 mM) and variable 4MU-Man concentrations or ( h ) in the presence of 4MU-Man (10 mM) and variable GDP-Man concentrations. Error bars indicate s.e.m., n = 3.

    Article Snippet: The products were digested with α-1,6-mannosidase (NEB) according to the manufacturer's instructions.

    Techniques: Activity Assay, Incubation, Enzymatic Assay