β1 3 galactosidase (New England Biolabs)


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

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
Related Products / Commonly Used Together
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

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

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

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

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

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

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

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

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

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

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, 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, 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); |