β1 3 galactosidase  (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
  • 93
    Name:
    Beta1 3 4 Galactosidase
    Description:
    Beta1 3 4 Galactosidase 2 000 units
    Catalog Number:
    p0746l
    Price:
    518
    Size:
    2 000 units
    Category:
    Glycosidases
    Buy from Supplier


    Structured Review

    New England Biolabs β1 3 galactosidase
    Beta1 3 4 Galactosidase
    Beta1 3 4 Galactosidase 2 000 units
    https://www.bioz.com/result/β1 3 galactosidase/product/New England Biolabs
    Average 93 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    β1 3 galactosidase - by Bioz Stars, 2021-02
    93/100 stars

    Images

    1) Product Images from "New Tags for Recombinant Protein Detection and O-Glycosylation Reporters"

    Article Title: New Tags for Recombinant Protein Detection and O-Glycosylation Reporters

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0096700

    O-glycosylated tags. (A) WB of supernatants of 293T cells transfected with the reporter protein tagged with OG-tag, P-roTag or roTagO (previously indicated as 9–18, 11–21 and 9–21, respectively) treated (T) or not (Ctrl) with a glycosidase mix containing Neuraminidase, β1-3 Galactosidase and β-NAc-hexosaminidase. (B) WB of cellular extracts (E) and supernatants (S) of HEK 293T cells transfected with the reporter protein tagged with OG-tag and roTagO with or without the ER retention signal KDEL. In all panels blots were developed, as indicated, with anti-SV5 or anti-roTag/1F2.
    Figure Legend Snippet: O-glycosylated tags. (A) WB of supernatants of 293T cells transfected with the reporter protein tagged with OG-tag, P-roTag or roTagO (previously indicated as 9–18, 11–21 and 9–21, respectively) treated (T) or not (Ctrl) with a glycosidase mix containing Neuraminidase, β1-3 Galactosidase and β-NAc-hexosaminidase. (B) WB of cellular extracts (E) and supernatants (S) of HEK 293T cells transfected with the reporter protein tagged with OG-tag and roTagO with or without the ER retention signal KDEL. In all panels blots were developed, as indicated, with anti-SV5 or anti-roTag/1F2.

    Techniques Used: Western Blot, Transfection

    2) Product Images from "Release and utilization of N-acetyl-d-glucosamine from human milk oligosaccharides by Bifidobacterium longum subsp. infantis"

    Article Title: Release and utilization of N-acetyl-d-glucosamine from human milk oligosaccharides by Bifidobacterium longum subsp. infantis

    Journal: Anaerobe

    doi: 10.1016/j.anaerobe.2012.04.012

    Thin layer chromatography of co-incubations of B. infantis N-acetyl-β-D-hexosaminidases with LNT or LNH after treatment with β-galactosidases. Structures are illustrated below the figure. Lanes 1–8 and 26–28: standards (as indicated in the figure); lane 9: LNT with specific β1-3 galactosidase; lanes 10–12: LNT with a β1-3 galactosidase and Blon_0459, Blon_0732 or Blon_2355. Lane 13: LNH; lanes 14–16: LNH with either a β1-3, a β1-4 or both specific galactosidases; lanes 17–19: LNH with a β1-3 galactosidase and Blon_0459, Blon_0732 and Blon_2355, respectively; lanes 20–22: LNH with a β1-4 galactosidase and either Blon_0459, Blon_0732 and Blon_2355; lanes 23–25: LNH with both β1-3 and β1-4 galactosidase, as well as either Blon_0459, Blon_0732 and Blon_2355.
    Figure Legend Snippet: Thin layer chromatography of co-incubations of B. infantis N-acetyl-β-D-hexosaminidases with LNT or LNH after treatment with β-galactosidases. Structures are illustrated below the figure. Lanes 1–8 and 26–28: standards (as indicated in the figure); lane 9: LNT with specific β1-3 galactosidase; lanes 10–12: LNT with a β1-3 galactosidase and Blon_0459, Blon_0732 or Blon_2355. Lane 13: LNH; lanes 14–16: LNH with either a β1-3, a β1-4 or both specific galactosidases; lanes 17–19: LNH with a β1-3 galactosidase and Blon_0459, Blon_0732 and Blon_2355, respectively; lanes 20–22: LNH with a β1-4 galactosidase and either Blon_0459, Blon_0732 and Blon_2355; lanes 23–25: LNH with both β1-3 and β1-4 galactosidase, as well as either Blon_0459, Blon_0732 and Blon_2355.

    Techniques Used: Thin Layer Chromatography

    3) Product Images from "Changes in canine serum N-glycosylation as a result of infection with the heartworm parasite Dirofilaria immitis"

    Article Title: Changes in canine serum N-glycosylation as a result of infection with the heartworm parasite Dirofilaria immitis

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-35038-7

    Longitudinal serum N-glycosylation profiles of D. immitis infection in dogs. ( a ) HILIC-UPLC profiles of enzymatically released and fluorescently labeled serum N-glycans from dog ID 116 (longitudinal set) from weeks 0, 21, 23, 25 and 27 post-infection with D. immitis . Rel. abund., relative abundance. The glycan structures of the two dominant peaks are annotated. ( b ) Heatmap of the changes in the abundance of serum N-glycan classes in D. immitis infection. Adjusted p-values were determined using linear mixed-effects models. Blue, increase; red, decrease. Glycan classes were identified and quantified by exoglycosidase digestion with α1-2,4,6 Fucosidase, β1-4 Galactosidase or α2-3,6,8 Neuraminidase. (Supplementary Fig. S3 ; Table S4 ).
    Figure Legend Snippet: Longitudinal serum N-glycosylation profiles of D. immitis infection in dogs. ( a ) HILIC-UPLC profiles of enzymatically released and fluorescently labeled serum N-glycans from dog ID 116 (longitudinal set) from weeks 0, 21, 23, 25 and 27 post-infection with D. immitis . Rel. abund., relative abundance. The glycan structures of the two dominant peaks are annotated. ( b ) Heatmap of the changes in the abundance of serum N-glycan classes in D. immitis infection. Adjusted p-values were determined using linear mixed-effects models. Blue, increase; red, decrease. Glycan classes were identified and quantified by exoglycosidase digestion with α1-2,4,6 Fucosidase, β1-4 Galactosidase or α2-3,6,8 Neuraminidase. (Supplementary Fig. S3 ; Table S4 ).

    Techniques Used: Infection, Hydrophilic Interaction Liquid Chromatography, Labeling

    Significant changes of serum N-glycosylation in dogs with a patent D. immitis infection. Glycan peaks/classes were tested for significance using linear mixed-effects models. p-values were adjusted based on Benjamini and Hochberg method. The analysis is based on 5 biological and 2 technical replicates per group (healthy and disease; patent set). ( a ) Volcano Plot comparing serum N-glycan peaks from dogs infected with D. immitis to a healthy control group. Illustrated is the log2 fold change in glycan abundance and the negative log2 of adjusted p-values. The horizontal dashed line represents the adjusted p-value cutoff (0.05). The points above the dashed line are glycan peaks that decrease (red) and increase (blue) significantly. See Supplementary Table S4 for quantification data. ( b ) Significant changes in all analyzed glycan classes in dogs with a patent D. immitis infection. Glycan classes were identified and quantified by exoglycosidase digestion with α1-2,4,6 Fucosidase, β1-4 Galactosidase or α2-3,6,8 Neuraminidase. See Supplementary Fig. S4 for visualization of the glycan classes. Bar graphs show mean + s.d. Agalactosylation, adj. p-value = 0.001; galactosylation, adj. p-value = 0.003; core fucosylation, adj. p-value = 0.001; sialylation, adj. p-value = 0.001.
    Figure Legend Snippet: Significant changes of serum N-glycosylation in dogs with a patent D. immitis infection. Glycan peaks/classes were tested for significance using linear mixed-effects models. p-values were adjusted based on Benjamini and Hochberg method. The analysis is based on 5 biological and 2 technical replicates per group (healthy and disease; patent set). ( a ) Volcano Plot comparing serum N-glycan peaks from dogs infected with D. immitis to a healthy control group. Illustrated is the log2 fold change in glycan abundance and the negative log2 of adjusted p-values. The horizontal dashed line represents the adjusted p-value cutoff (0.05). The points above the dashed line are glycan peaks that decrease (red) and increase (blue) significantly. See Supplementary Table S4 for quantification data. ( b ) Significant changes in all analyzed glycan classes in dogs with a patent D. immitis infection. Glycan classes were identified and quantified by exoglycosidase digestion with α1-2,4,6 Fucosidase, β1-4 Galactosidase or α2-3,6,8 Neuraminidase. See Supplementary Fig. S4 for visualization of the glycan classes. Bar graphs show mean + s.d. Agalactosylation, adj. p-value = 0.001; galactosylation, adj. p-value = 0.003; core fucosylation, adj. p-value = 0.001; sialylation, adj. p-value = 0.001.

    Techniques Used: Infection

    4) Product Images from "Fucosyl-Agalactosyl IgG1 Induces Cholangiocarcinoma Metastasis and Early Recurrence by Activating Tumor-Associated Macrophage"

    Article Title: Fucosyl-Agalactosyl IgG1 Induces Cholangiocarcinoma Metastasis and Early Recurrence by Activating Tumor-Associated Macrophage

    Journal: Cancers

    doi: 10.3390/cancers10110460

    Induction of tumor-associated macrophage by agalactosylated IgG. ( A ) Numbers of CD163+ macrophages in the tumor foci of cholangiocarcinoma in patients with different tumor grades (left panel), with or without tumor metastasis (middle panel), or with different IgG 1 -G0F level (right panel) are shown in Tukey box-and-whisker plots. A P -value in the left panel is obtained from the Kruskal–Wallis test. P -values in the middle and right panels are obtained from Mann–Whitney U tests. ( B ) A schematic representation of the depletion of terminal sialic acid and galactose moieties on serum IgG using α2-3,6,8 neuraminidase and β1-4 galactosidase S, respectively. The proportion of each glycoform on normal or galactose-and-sialic acid-removed (asialyl-agalactosyl) IgG 1 and IgG 2 are shown. ( C ) Messenger RNA levels of the macrophage marker CD68 and tumor-associated macrophage markers CD163 and CD204 in U-937 cells after treatments with 10 ng/mL of phorbol 12-myristate 13-acetate for 2 days and 10 mg/mL of IgG (blue bar, mock; red bar, agalactosyl IgG; green bar, normal serum IgG) for another 3 or 6 days, are shown in bar graphs as means with standard deviations. Results are obtained from three independent experiments. p -values are obtained from one-way analysis of variance with Scheffé post hoc tests. Immunoblotting assays to detect protein levels of ( D ) CD68, CD163, and CD204 at day 6 post-treatment and ( E ) CD64 (FcγRI) and CD16 (FcγRIII) in macrophagic U-937 cells and human peripheral macrophages are shown. (* p
    Figure Legend Snippet: Induction of tumor-associated macrophage by agalactosylated IgG. ( A ) Numbers of CD163+ macrophages in the tumor foci of cholangiocarcinoma in patients with different tumor grades (left panel), with or without tumor metastasis (middle panel), or with different IgG 1 -G0F level (right panel) are shown in Tukey box-and-whisker plots. A P -value in the left panel is obtained from the Kruskal–Wallis test. P -values in the middle and right panels are obtained from Mann–Whitney U tests. ( B ) A schematic representation of the depletion of terminal sialic acid and galactose moieties on serum IgG using α2-3,6,8 neuraminidase and β1-4 galactosidase S, respectively. The proportion of each glycoform on normal or galactose-and-sialic acid-removed (asialyl-agalactosyl) IgG 1 and IgG 2 are shown. ( C ) Messenger RNA levels of the macrophage marker CD68 and tumor-associated macrophage markers CD163 and CD204 in U-937 cells after treatments with 10 ng/mL of phorbol 12-myristate 13-acetate for 2 days and 10 mg/mL of IgG (blue bar, mock; red bar, agalactosyl IgG; green bar, normal serum IgG) for another 3 or 6 days, are shown in bar graphs as means with standard deviations. Results are obtained from three independent experiments. p -values are obtained from one-way analysis of variance with Scheffé post hoc tests. Immunoblotting assays to detect protein levels of ( D ) CD68, CD163, and CD204 at day 6 post-treatment and ( E ) CD64 (FcγRI) and CD16 (FcγRIII) in macrophagic U-937 cells and human peripheral macrophages are shown. (* p

    Techniques Used: Whisker Assay, MANN-WHITNEY, Marker

    5) Product Images from "Glycosylation profiling of dog serum reveals differences compared to human serum"

    Article Title: Glycosylation profiling of dog serum reveals differences compared to human serum

    Journal: Glycobiology

    doi: 10.1093/glycob/cwy070

    Quantification of glycan classes of canine and human serum N -glycans. Representative HILIC-UPLC spectra of canine (left) and human (right) serum N -glycans are shown. The relative abundances of glycans containing core fucosylated (red; A , D ), free terminal β-galactoses (yellow; B , E ) or sialic acids (pink; Neu5Ac and Neu5Gc – C , Neu5Ac – F ) were determined by quantification of spectra before and after digestion with Fucosidase O, β1-4 Galactosidase and Neuraminidase, respectively. The bar graphs compare the relative abundances of dog (D) and human (H) serum. The error bars show mean + SD from the analysis of n ) and n = 4 (pooled human serum samples) biological replicates. Significances were determined by performing an unpaired t -test (fucosylation, P = 0.0481; galactosylation, P = 0.0016; sialylation, P = 0.0002).
    Figure Legend Snippet: Quantification of glycan classes of canine and human serum N -glycans. Representative HILIC-UPLC spectra of canine (left) and human (right) serum N -glycans are shown. The relative abundances of glycans containing core fucosylated (red; A , D ), free terminal β-galactoses (yellow; B , E ) or sialic acids (pink; Neu5Ac and Neu5Gc – C , Neu5Ac – F ) were determined by quantification of spectra before and after digestion with Fucosidase O, β1-4 Galactosidase and Neuraminidase, respectively. The bar graphs compare the relative abundances of dog (D) and human (H) serum. The error bars show mean + SD from the analysis of n ) and n = 4 (pooled human serum samples) biological replicates. Significances were determined by performing an unpaired t -test (fucosylation, P = 0.0481; galactosylation, P = 0.0016; sialylation, P = 0.0002).

    Techniques Used: Hydrophilic Interaction Liquid Chromatography

    6) Product Images from "Glycosylation profiling of dog serum reveals differences compared to human serum"

    Article Title: Glycosylation profiling of dog serum reveals differences compared to human serum

    Journal: Glycobiology

    doi: 10.1093/glycob/cwy070

    Quantification of glycan classes of canine and human serum N -glycans. Representative HILIC-UPLC spectra of canine (left) and human (right) serum N -glycans are shown. The relative abundances of glycans containing core fucosylated (red; A , D ), free terminal β-galactoses (yellow; B , E ) or sialic acids (pink; Neu5Ac and Neu5Gc – C , Neu5Ac – F ) were determined by quantification of spectra before and after digestion with Fucosidase O, β1-4 Galactosidase and Neuraminidase, respectively. The bar graphs compare the relative abundances of dog (D) and human (H) serum. The error bars show mean + SD from the analysis of n = 5 (canine serum samples; see Figure S3 ) and n = 4 (pooled human serum samples) biological replicates. Significances were determined by performing an unpaired t -test (fucosylation, P = 0.0481; galactosylation, P = 0.0016; sialylation, P = 0.0002).
    Figure Legend Snippet: Quantification of glycan classes of canine and human serum N -glycans. Representative HILIC-UPLC spectra of canine (left) and human (right) serum N -glycans are shown. The relative abundances of glycans containing core fucosylated (red; A , D ), free terminal β-galactoses (yellow; B , E ) or sialic acids (pink; Neu5Ac and Neu5Gc – C , Neu5Ac – F ) were determined by quantification of spectra before and after digestion with Fucosidase O, β1-4 Galactosidase and Neuraminidase, respectively. The bar graphs compare the relative abundances of dog (D) and human (H) serum. The error bars show mean + SD from the analysis of n = 5 (canine serum samples; see Figure S3 ) and n = 4 (pooled human serum samples) biological replicates. Significances were determined by performing an unpaired t -test (fucosylation, P = 0.0481; galactosylation, P = 0.0016; sialylation, P = 0.0002).

    Techniques Used: Hydrophilic Interaction Liquid Chromatography

    7) Product Images from "Site-specific Glycoforms of Haptoglobin in Liver Cirrhosis and Hepatocellular Carcinoma *"

    Article Title: Site-specific Glycoforms of Haptoglobin in Liver Cirrhosis and Hepatocellular Carcinoma *

    Journal: Molecular & Cellular Proteomics : MCP

    doi: 10.1074/mcp.M112.023259

    A , select site-specific glycoforms of the T3 peptide at m / z 938.4 and at m / z 978.9 after neuraminidase and β1,4-galactosidase treatment consistent with the observed results in pooled HCC ( left ) and pooled cirrhosis ( right ) samples. The presented
    Figure Legend Snippet: A , select site-specific glycoforms of the T3 peptide at m / z 938.4 and at m / z 978.9 after neuraminidase and β1,4-galactosidase treatment consistent with the observed results in pooled HCC ( left ) and pooled cirrhosis ( right ) samples. The presented

    Techniques Used:

    8) Product Images from "Products of Chemoenzymatic Synthesis Representing MUC1 Tandem Repeat Unit with T-, ST- or STn-antigen Revealed Distinct Specificities of Anti-MUC1 Antibodies"

    Article Title: Products of Chemoenzymatic Synthesis Representing MUC1 Tandem Repeat Unit with T-, ST- or STn-antigen Revealed Distinct Specificities of Anti-MUC1 Antibodies

    Journal: Scientific Reports

    doi: 10.1038/s41598-019-53052-1

    Enzymatic synthesis of MUC1 STn-Ser 19 . ( a ) Schematic representation of the synthesis. ( b ) MALDI-TOF MS analysis. ( c ) HPLC analysis. Within each figure, (i), (ii) and (iii) correspond to MUC1 T-Ser 19 , α2,6-sialylated MUC1 T-Ser 19 (in reaction mixture) and MUC1 STn-Ser 19 (in reaction mixture), respectively. The final reaction with β1-3,4 galactosidase was performed on the purified α2,6-sialylated MUC1 T-Ser 19 .
    Figure Legend Snippet: Enzymatic synthesis of MUC1 STn-Ser 19 . ( a ) Schematic representation of the synthesis. ( b ) MALDI-TOF MS analysis. ( c ) HPLC analysis. Within each figure, (i), (ii) and (iii) correspond to MUC1 T-Ser 19 , α2,6-sialylated MUC1 T-Ser 19 (in reaction mixture) and MUC1 STn-Ser 19 (in reaction mixture), respectively. The final reaction with β1-3,4 galactosidase was performed on the purified α2,6-sialylated MUC1 T-Ser 19 .

    Techniques Used: Mass Spectrometry, High Performance Liquid Chromatography, Purification

    9) Product Images from "Release and utilization of N-acetyl-d-glucosamine from human milk oligosaccharides by Bifidobacterium longum subsp. infantis"

    Article Title: Release and utilization of N-acetyl-d-glucosamine from human milk oligosaccharides by Bifidobacterium longum subsp. infantis

    Journal: Anaerobe

    doi: 10.1016/j.anaerobe.2012.04.012

    Thin layer chromatography of co-incubations of B. infantis N-acetyl-β-D-hexosaminidases with LNT or LNH after treatment with β-galactosidases. Structures are illustrated below the figure. Lanes 1–8 and 26–28: standards (as indicated in the figure); lane 9: LNT with specific β1-3 galactosidase; lanes 10–12: LNT with a β1-3 galactosidase and Blon_0459, Blon_0732 or Blon_2355. Lane 13: LNH; lanes 14–16: LNH with either a β1-3, a β1-4 or both specific galactosidases; lanes 17–19: LNH with a β1-3 galactosidase and Blon_0459, Blon_0732 and Blon_2355, respectively; lanes 20–22: LNH with a β1-4 galactosidase and either Blon_0459, Blon_0732 and Blon_2355; lanes 23–25: LNH with both β1-3 and β1-4 galactosidase, as well as either Blon_0459, Blon_0732 and Blon_2355.
    Figure Legend Snippet: Thin layer chromatography of co-incubations of B. infantis N-acetyl-β-D-hexosaminidases with LNT or LNH after treatment with β-galactosidases. Structures are illustrated below the figure. Lanes 1–8 and 26–28: standards (as indicated in the figure); lane 9: LNT with specific β1-3 galactosidase; lanes 10–12: LNT with a β1-3 galactosidase and Blon_0459, Blon_0732 or Blon_2355. Lane 13: LNH; lanes 14–16: LNH with either a β1-3, a β1-4 or both specific galactosidases; lanes 17–19: LNH with a β1-3 galactosidase and Blon_0459, Blon_0732 and Blon_2355, respectively; lanes 20–22: LNH with a β1-4 galactosidase and either Blon_0459, Blon_0732 and Blon_2355; lanes 23–25: LNH with both β1-3 and β1-4 galactosidase, as well as either Blon_0459, Blon_0732 and Blon_2355.

    Techniques Used: Thin Layer Chromatography

    Related Articles

    Protein Binding:

    Article Title: Glycosylation profiling of dog serum reveals differences compared to human serum
    Article Snippet: .. Glycans were digested with α2-3,6,8 Neuraminidase, α2-3 Neuraminidase, α1-2,4,6 Fucosidase O, β1-4 Galactosidase, β - N -Acetyl-Glucosaminidase, α1-2,3,6 Mannnosidase, α1-3,4,6 Galactosidase (all from New England Biolabs) according to the manufacturer’s instructions, then extracted using a 96-well hydrophobic polyvinyl fluoride (PVDF) protein-binding membrane plate as recommended (Merck Millipore). .. LC-ESI MS profiling of procainamide-labeled glycans was performed using an UltiMate 3000 UHPLC (Thermo Fisher Scientific) equipped with an 8 μL fluorescent cell coupled to a LTQ Velos Pro (Thermo Fisher Scientific) mass spectrometer (see ).

    Article Title: Glycosylation profiling of dog serum reveals differences compared to human serum
    Article Snippet: .. Glycans were digested with α2-3,6,8 Neuraminidase, α2-3 Neuraminidase, α1-2,4,6 Fucosidase O, β1-4 Galactosidase, β-N -Acetyl-Glucosaminidase, α1-2,3,6 Mannnosidase, α1-3,4,6 Galactosidase (all from New England Biolabs) according to the manufacturer’s instructions, then extracted using a 96-well hydrophobic polyvinyl fluoride (PVDF) protein-binding membrane plate as recommended (Merck Millipore). .. LC-ESI MS of N -glycans LC-ESI MS profiling of procainamide-labeled glycans was performed using an UltiMate 3000 UHPLC (Thermo Fisher Scientific) equipped with an 8 μL fluorescent cell coupled to a LTQ Velos Pro (Thermo Fisher Scientific) mass spectrometer (see ).

    Isolation:

    Article Title: Site-specific Glycoforms of Haptoglobin in Liver Cirrhosis and Hepatocellular Carcinoma *
    Article Snippet: .. For structural characterization of glycopeptides, Hp (2.5 μg) isolated from pooled plasma samples of HCC patients and healthy controls was digested with trypsin as described above, desalted, and treated with exoglycosidases in the following order: α2/3,6,8-neuraminidase (100 units) from C. perfringens overexpressed in E. coli (New England Biolabs); α1/2-fucosidase (20 units) from Xanthomonas manihotis (New England Biolabs); α1/3,4-fucosidase (16 microunits) from almond meal (Prozyme, Hayward, CA); β1,4-galactosidase (16 units) from B. fragilis expressed in E. coli (New England Biolabs); and β1,3-galactosidase (20 units) from X. manihotis expressed in E. coli (New England Biolabs). .. Between each exoglycosidase treatment, glycopeptides were desalted by a microtrap device, eluted with 50% ACN + 0.1% TFA, dried, and an aliquot was resuspended in solvent A (0.1% formic acid in 2% acetonitrile) for MS analysis as described below.

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93
    New England Biolabs β1 3 galactosidase
    O-glycosylated tags. (A) WB of supernatants of 293T cells transfected with the reporter protein tagged with OG-tag, P-roTag or roTagO (previously indicated as 9–18, 11–21 and 9–21, respectively) treated (T) or not (Ctrl) with a glycosidase mix containing Neuraminidase, <t>β1-3</t> Galactosidase and β-NAc-hexosaminidase. (B) WB of cellular extracts (E) and supernatants (S) of HEK 293T cells transfected with the reporter protein tagged with OG-tag and roTagO with or without the ER retention signal KDEL. In all panels blots were developed, as indicated, with anti-SV5 or anti-roTag/1F2.
    β1 3 Galactosidase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/β1 3 galactosidase/product/New England Biolabs
    Average 93 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    β1 3 galactosidase - by Bioz Stars, 2021-02
    93/100 stars
      Buy from Supplier

    Image Search Results


    O-glycosylated tags. (A) WB of supernatants of 293T cells transfected with the reporter protein tagged with OG-tag, P-roTag or roTagO (previously indicated as 9–18, 11–21 and 9–21, respectively) treated (T) or not (Ctrl) with a glycosidase mix containing Neuraminidase, β1-3 Galactosidase and β-NAc-hexosaminidase. (B) WB of cellular extracts (E) and supernatants (S) of HEK 293T cells transfected with the reporter protein tagged with OG-tag and roTagO with or without the ER retention signal KDEL. In all panels blots were developed, as indicated, with anti-SV5 or anti-roTag/1F2.

    Journal: PLoS ONE

    Article Title: New Tags for Recombinant Protein Detection and O-Glycosylation Reporters

    doi: 10.1371/journal.pone.0096700

    Figure Lengend Snippet: O-glycosylated tags. (A) WB of supernatants of 293T cells transfected with the reporter protein tagged with OG-tag, P-roTag or roTagO (previously indicated as 9–18, 11–21 and 9–21, respectively) treated (T) or not (Ctrl) with a glycosidase mix containing Neuraminidase, β1-3 Galactosidase and β-NAc-hexosaminidase. (B) WB of cellular extracts (E) and supernatants (S) of HEK 293T cells transfected with the reporter protein tagged with OG-tag and roTagO with or without the ER retention signal KDEL. In all panels blots were developed, as indicated, with anti-SV5 or anti-roTag/1F2.

    Article Snippet: Where indicated samples were treated 2 hours at 37°C with a mix of Neuraminidase, β1-3 Galactosidase and β -N-Ac-hexosaminidase (New England Biolabs) in buffer 50 mM sodium citrate pH 4.5 according to manufacturer indications.

    Techniques: Western Blot, Transfection

    Thin layer chromatography of co-incubations of B. infantis N-acetyl-β-D-hexosaminidases with LNT or LNH after treatment with β-galactosidases. Structures are illustrated below the figure. Lanes 1–8 and 26–28: standards (as indicated in the figure); lane 9: LNT with specific β1-3 galactosidase; lanes 10–12: LNT with a β1-3 galactosidase and Blon_0459, Blon_0732 or Blon_2355. Lane 13: LNH; lanes 14–16: LNH with either a β1-3, a β1-4 or both specific galactosidases; lanes 17–19: LNH with a β1-3 galactosidase and Blon_0459, Blon_0732 and Blon_2355, respectively; lanes 20–22: LNH with a β1-4 galactosidase and either Blon_0459, Blon_0732 and Blon_2355; lanes 23–25: LNH with both β1-3 and β1-4 galactosidase, as well as either Blon_0459, Blon_0732 and Blon_2355.

    Journal: Anaerobe

    Article Title: Release and utilization of N-acetyl-d-glucosamine from human milk oligosaccharides by Bifidobacterium longum subsp. infantis

    doi: 10.1016/j.anaerobe.2012.04.012

    Figure Lengend Snippet: Thin layer chromatography of co-incubations of B. infantis N-acetyl-β-D-hexosaminidases with LNT or LNH after treatment with β-galactosidases. Structures are illustrated below the figure. Lanes 1–8 and 26–28: standards (as indicated in the figure); lane 9: LNT with specific β1-3 galactosidase; lanes 10–12: LNT with a β1-3 galactosidase and Blon_0459, Blon_0732 or Blon_2355. Lane 13: LNH; lanes 14–16: LNH with either a β1-3, a β1-4 or both specific galactosidases; lanes 17–19: LNH with a β1-3 galactosidase and Blon_0459, Blon_0732 and Blon_2355, respectively; lanes 20–22: LNH with a β1-4 galactosidase and either Blon_0459, Blon_0732 and Blon_2355; lanes 23–25: LNH with both β1-3 and β1-4 galactosidase, as well as either Blon_0459, Blon_0732 and Blon_2355.

    Article Snippet: Reactions were carried out for 60 min at 37 °C, and products were inactivated at 95 °C for 5 min. LNT and lacto-N-hexaose (LNH) at 1 mg/ml (0.5 μg final) were also coincubated with these enzymes, but with and without the addition of 10 units of β1-3 or β1-4 galactosidase, or both (New Englands Biolabs), for 1 h at 37 °C and pH 5.5.

    Techniques: Thin Layer Chromatography

    Longitudinal serum N-glycosylation profiles of D. immitis infection in dogs. ( a ) HILIC-UPLC profiles of enzymatically released and fluorescently labeled serum N-glycans from dog ID 116 (longitudinal set) from weeks 0, 21, 23, 25 and 27 post-infection with D. immitis . Rel. abund., relative abundance. The glycan structures of the two dominant peaks are annotated. ( b ) Heatmap of the changes in the abundance of serum N-glycan classes in D. immitis infection. Adjusted p-values were determined using linear mixed-effects models. Blue, increase; red, decrease. Glycan classes were identified and quantified by exoglycosidase digestion with α1-2,4,6 Fucosidase, β1-4 Galactosidase or α2-3,6,8 Neuraminidase. (Supplementary Fig. S3 ; Table S4 ).

    Journal: Scientific Reports

    Article Title: Changes in canine serum N-glycosylation as a result of infection with the heartworm parasite Dirofilaria immitis

    doi: 10.1038/s41598-018-35038-7

    Figure Lengend Snippet: Longitudinal serum N-glycosylation profiles of D. immitis infection in dogs. ( a ) HILIC-UPLC profiles of enzymatically released and fluorescently labeled serum N-glycans from dog ID 116 (longitudinal set) from weeks 0, 21, 23, 25 and 27 post-infection with D. immitis . Rel. abund., relative abundance. The glycan structures of the two dominant peaks are annotated. ( b ) Heatmap of the changes in the abundance of serum N-glycan classes in D. immitis infection. Adjusted p-values were determined using linear mixed-effects models. Blue, increase; red, decrease. Glycan classes were identified and quantified by exoglycosidase digestion with α1-2,4,6 Fucosidase, β1-4 Galactosidase or α2-3,6,8 Neuraminidase. (Supplementary Fig. S3 ; Table S4 ).

    Article Snippet: In brief, glycans were digested with α2-3,6,8 Neuraminidase, α1-2,4,6 Fucosidase O, β1-4 Galactosidase, β-N -Acetyl-Glucosaminidase and α1-2,3,6 Mannnosidase (all from New England Biolabs) according to the manufacturer’s instructions.

    Techniques: Infection, Hydrophilic Interaction Liquid Chromatography, Labeling

    Significant changes of serum N-glycosylation in dogs with a patent D. immitis infection. Glycan peaks/classes were tested for significance using linear mixed-effects models. p-values were adjusted based on Benjamini and Hochberg method. The analysis is based on 5 biological and 2 technical replicates per group (healthy and disease; patent set). ( a ) Volcano Plot comparing serum N-glycan peaks from dogs infected with D. immitis to a healthy control group. Illustrated is the log2 fold change in glycan abundance and the negative log2 of adjusted p-values. The horizontal dashed line represents the adjusted p-value cutoff (0.05). The points above the dashed line are glycan peaks that decrease (red) and increase (blue) significantly. See Supplementary Table S4 for quantification data. ( b ) Significant changes in all analyzed glycan classes in dogs with a patent D. immitis infection. Glycan classes were identified and quantified by exoglycosidase digestion with α1-2,4,6 Fucosidase, β1-4 Galactosidase or α2-3,6,8 Neuraminidase. See Supplementary Fig. S4 for visualization of the glycan classes. Bar graphs show mean + s.d. Agalactosylation, adj. p-value = 0.001; galactosylation, adj. p-value = 0.003; core fucosylation, adj. p-value = 0.001; sialylation, adj. p-value = 0.001.

    Journal: Scientific Reports

    Article Title: Changes in canine serum N-glycosylation as a result of infection with the heartworm parasite Dirofilaria immitis

    doi: 10.1038/s41598-018-35038-7

    Figure Lengend Snippet: Significant changes of serum N-glycosylation in dogs with a patent D. immitis infection. Glycan peaks/classes were tested for significance using linear mixed-effects models. p-values were adjusted based on Benjamini and Hochberg method. The analysis is based on 5 biological and 2 technical replicates per group (healthy and disease; patent set). ( a ) Volcano Plot comparing serum N-glycan peaks from dogs infected with D. immitis to a healthy control group. Illustrated is the log2 fold change in glycan abundance and the negative log2 of adjusted p-values. The horizontal dashed line represents the adjusted p-value cutoff (0.05). The points above the dashed line are glycan peaks that decrease (red) and increase (blue) significantly. See Supplementary Table S4 for quantification data. ( b ) Significant changes in all analyzed glycan classes in dogs with a patent D. immitis infection. Glycan classes were identified and quantified by exoglycosidase digestion with α1-2,4,6 Fucosidase, β1-4 Galactosidase or α2-3,6,8 Neuraminidase. See Supplementary Fig. S4 for visualization of the glycan classes. Bar graphs show mean + s.d. Agalactosylation, adj. p-value = 0.001; galactosylation, adj. p-value = 0.003; core fucosylation, adj. p-value = 0.001; sialylation, adj. p-value = 0.001.

    Article Snippet: In brief, glycans were digested with α2-3,6,8 Neuraminidase, α1-2,4,6 Fucosidase O, β1-4 Galactosidase, β-N -Acetyl-Glucosaminidase and α1-2,3,6 Mannnosidase (all from New England Biolabs) according to the manufacturer’s instructions.

    Techniques: Infection

    Induction of tumor-associated macrophage by agalactosylated IgG. ( A ) Numbers of CD163+ macrophages in the tumor foci of cholangiocarcinoma in patients with different tumor grades (left panel), with or without tumor metastasis (middle panel), or with different IgG 1 -G0F level (right panel) are shown in Tukey box-and-whisker plots. A P -value in the left panel is obtained from the Kruskal–Wallis test. P -values in the middle and right panels are obtained from Mann–Whitney U tests. ( B ) A schematic representation of the depletion of terminal sialic acid and galactose moieties on serum IgG using α2-3,6,8 neuraminidase and β1-4 galactosidase S, respectively. The proportion of each glycoform on normal or galactose-and-sialic acid-removed (asialyl-agalactosyl) IgG 1 and IgG 2 are shown. ( C ) Messenger RNA levels of the macrophage marker CD68 and tumor-associated macrophage markers CD163 and CD204 in U-937 cells after treatments with 10 ng/mL of phorbol 12-myristate 13-acetate for 2 days and 10 mg/mL of IgG (blue bar, mock; red bar, agalactosyl IgG; green bar, normal serum IgG) for another 3 or 6 days, are shown in bar graphs as means with standard deviations. Results are obtained from three independent experiments. p -values are obtained from one-way analysis of variance with Scheffé post hoc tests. Immunoblotting assays to detect protein levels of ( D ) CD68, CD163, and CD204 at day 6 post-treatment and ( E ) CD64 (FcγRI) and CD16 (FcγRIII) in macrophagic U-937 cells and human peripheral macrophages are shown. (* p

    Journal: Cancers

    Article Title: Fucosyl-Agalactosyl IgG1 Induces Cholangiocarcinoma Metastasis and Early Recurrence by Activating Tumor-Associated Macrophage

    doi: 10.3390/cancers10110460

    Figure Lengend Snippet: Induction of tumor-associated macrophage by agalactosylated IgG. ( A ) Numbers of CD163+ macrophages in the tumor foci of cholangiocarcinoma in patients with different tumor grades (left panel), with or without tumor metastasis (middle panel), or with different IgG 1 -G0F level (right panel) are shown in Tukey box-and-whisker plots. A P -value in the left panel is obtained from the Kruskal–Wallis test. P -values in the middle and right panels are obtained from Mann–Whitney U tests. ( B ) A schematic representation of the depletion of terminal sialic acid and galactose moieties on serum IgG using α2-3,6,8 neuraminidase and β1-4 galactosidase S, respectively. The proportion of each glycoform on normal or galactose-and-sialic acid-removed (asialyl-agalactosyl) IgG 1 and IgG 2 are shown. ( C ) Messenger RNA levels of the macrophage marker CD68 and tumor-associated macrophage markers CD163 and CD204 in U-937 cells after treatments with 10 ng/mL of phorbol 12-myristate 13-acetate for 2 days and 10 mg/mL of IgG (blue bar, mock; red bar, agalactosyl IgG; green bar, normal serum IgG) for another 3 or 6 days, are shown in bar graphs as means with standard deviations. Results are obtained from three independent experiments. p -values are obtained from one-way analysis of variance with Scheffé post hoc tests. Immunoblotting assays to detect protein levels of ( D ) CD68, CD163, and CD204 at day 6 post-treatment and ( E ) CD64 (FcγRI) and CD16 (FcγRIII) in macrophagic U-937 cells and human peripheral macrophages are shown. (* p

    Article Snippet: To generate sialic acids and galactose-free (asialyl-agalactosyl) IgG, normal serum IgG was treated with α2-3,6,8 neuraminidase and β1-4 galactosidase S (New England Biolabs, Ipswich, MA, USA) at 37 °C for 24 h. Normal serum IgG and asialyl-agalactosyl IgG were heated at 60 °C for 1 hour to generate aggregated IgG complexes.

    Techniques: Whisker Assay, MANN-WHITNEY, Marker