fucosidase  (New England Biolabs)


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  • 95
    Name:
    alpha 1 2 Fucosidase
    Description:
    alpha 1 2 Fucosidase 5 000 units
    Catalog Number:
    P0724L
    Price:
    520
    Category:
    Glycosidases
    Size:
    5 000 units
    Buy from Supplier


    Structured Review

    New England Biolabs fucosidase
    alpha 1 2 Fucosidase
    alpha 1 2 Fucosidase 5 000 units
    https://www.bioz.com/result/fucosidase/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fucosidase - by Bioz Stars, 2021-06
    95/100 stars

    Images

    1) Product Images from "Human stem cell-derived retinal epithelial cells activate complement via collectin 11 in response to stress"

    Article Title: Human stem cell-derived retinal epithelial cells activate complement via collectin 11 in response to stress

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-15212-z

    C3d expression and MAC formation on hypoxia-stressed iPS-RPE cells following fucosidase treatment. ( a ) Representative immunofluorescence images showing C3d deposition on the surface of hypoxia-stressed iPS-RPE cells treated or not overnight with fucosidase. C3d (green), nuclei nuclei (blue) and phalloidin (grey) are shown. Scale bars, 50 μm. ( b ) Quantification of C3d expression level on hypoxia-stressed iPS- RPE cells compared to fucosidase-treated hypoxic cells using ImageJ software. ( c ) Representative immunofluorescence images showing MAC staining on the surface of hypoxia-stressed iPS-RPE cells treated or not overnight with fucosidase. MAC (red), nuclei (blue) and phalloidin (grey) are shown. Scale bars, 50 μm.
    Figure Legend Snippet: C3d expression and MAC formation on hypoxia-stressed iPS-RPE cells following fucosidase treatment. ( a ) Representative immunofluorescence images showing C3d deposition on the surface of hypoxia-stressed iPS-RPE cells treated or not overnight with fucosidase. C3d (green), nuclei nuclei (blue) and phalloidin (grey) are shown. Scale bars, 50 μm. ( b ) Quantification of C3d expression level on hypoxia-stressed iPS- RPE cells compared to fucosidase-treated hypoxic cells using ImageJ software. ( c ) Representative immunofluorescence images showing MAC staining on the surface of hypoxia-stressed iPS-RPE cells treated or not overnight with fucosidase. MAC (red), nuclei (blue) and phalloidin (grey) are shown. Scale bars, 50 μm.

    Techniques Used: Expressing, Immunofluorescence, Software, Staining

    2) Product Images from "TSTA3 facilitates esophageal squamous cell carcinoma progression through regulating fucosylation of LAMP2 and ERBB2"

    Article Title: TSTA3 facilitates esophageal squamous cell carcinoma progression through regulating fucosylation of LAMP2 and ERBB2

    Journal: Theranostics

    doi: 10.7150/thno.48225

    Identification of fucosylated glycoproteins in ESCC revealed regulators of invasion and metastasis. (A) Schematic illustration of the experimental approach showing affinity enrichment of core-fucosylated and α-1,2-fucosylated proteins by LCA and UEA-I lectin affinity chromatography respectively. (B) The effect of enriched fucosylated protein by UEA-I lectin with or without α-1,2-fucosidase on KYSE150 and KYSE450 cell invasion. (C) Coomassie brilliant blue (CBB) staining of gels of whole cell lysate proteins and LCA enriched fucosylated proteins in TSTA3-WT and control group. (D) Number of overlapping proteins between lectin enriched proteins identified by in gel mass spectrometry analysis and differentially expressed glycoproteins in N-glycoproteomics data. (E) LCA affinity chromatography of whole-cell lysates of ESCC cells transfected with TSTA3-WT and NC followed by western blot with LAMP2 antibody. (F) A representative western blot of LCA-affinity purified LAMP2. LCA-affinity purification was done in the absence or presence of various concentrations of α-L-fucose (0, 6, 30 and 60 mM). (G) LAMP2 immunoprecipitation from whole-cell lysates of KYSE150 and KYSE450 cells transfected with TSTA3-WT and NC. Anti-LAMP2 immunoprecipitate was treated with or without PNGase F and blotted with biotinylated LCA or LAMP2 antibody. (H) UEA-I affinity chromatography of whole-cell lysate of ESCC cells transfected with TSTA3-WT and NC followed by western blot with ERBB2 antibody. (I) A representative western blot of UEA-I-affinity purified ERBB2. UEA-I-affinity purification was done in the absence or presence of various concentrations of α-L-fucose. (J) ERBB2 immunoprecipitation from whole-cell lysates of KYSE150 and KYSE450 cells transfected with TSTA3-WT and NC. Anti-ERBB2 immunoprecipitate was treated with or without PNGase F and blotted with biotinylated UEA-I or ERBB2 antibody.
    Figure Legend Snippet: Identification of fucosylated glycoproteins in ESCC revealed regulators of invasion and metastasis. (A) Schematic illustration of the experimental approach showing affinity enrichment of core-fucosylated and α-1,2-fucosylated proteins by LCA and UEA-I lectin affinity chromatography respectively. (B) The effect of enriched fucosylated protein by UEA-I lectin with or without α-1,2-fucosidase on KYSE150 and KYSE450 cell invasion. (C) Coomassie brilliant blue (CBB) staining of gels of whole cell lysate proteins and LCA enriched fucosylated proteins in TSTA3-WT and control group. (D) Number of overlapping proteins between lectin enriched proteins identified by in gel mass spectrometry analysis and differentially expressed glycoproteins in N-glycoproteomics data. (E) LCA affinity chromatography of whole-cell lysates of ESCC cells transfected with TSTA3-WT and NC followed by western blot with LAMP2 antibody. (F) A representative western blot of LCA-affinity purified LAMP2. LCA-affinity purification was done in the absence or presence of various concentrations of α-L-fucose (0, 6, 30 and 60 mM). (G) LAMP2 immunoprecipitation from whole-cell lysates of KYSE150 and KYSE450 cells transfected with TSTA3-WT and NC. Anti-LAMP2 immunoprecipitate was treated with or without PNGase F and blotted with biotinylated LCA or LAMP2 antibody. (H) UEA-I affinity chromatography of whole-cell lysate of ESCC cells transfected with TSTA3-WT and NC followed by western blot with ERBB2 antibody. (I) A representative western blot of UEA-I-affinity purified ERBB2. UEA-I-affinity purification was done in the absence or presence of various concentrations of α-L-fucose. (J) ERBB2 immunoprecipitation from whole-cell lysates of KYSE150 and KYSE450 cells transfected with TSTA3-WT and NC. Anti-ERBB2 immunoprecipitate was treated with or without PNGase F and blotted with biotinylated UEA-I or ERBB2 antibody.

    Techniques Used: Affinity Chromatography, Staining, Mass Spectrometry, Transfection, Western Blot, Affinity Purification, Immunoprecipitation

    3) Product Images from "Analysis of serum protein glycosylation by a differential lectin immunosorbant assay (dLISA)"

    Article Title: Analysis of serum protein glycosylation by a differential lectin immunosorbant assay (dLISA)

    Journal: Clinical proteomics

    doi: 10.1186/1559-0275-10-12

    Slopes of the dose response curves established using the dLISA approach correlated with TIMP-1 fucosylation. (A) Dose–response curves of serum samples spiked with differentially fucosylated recombinant TIMP-1. Recombinant TIMP-1 was treated by α1, 2 fucosidase at different length of time (0, 15, 30, and 45 minutes) before they were spiked into with four serum aliquots. These aliquots came from the same pool of sera with endogenous TIMP-1 immuno-depleted (confirmed by the TIMP-1 immunoassay). After the recombinant protein spiked in, these serum samples underwent the dLISA approach. (B) A graph presentation of linear regression slopes of the dose–response curves versus the length of fucosidase treatment (minutes).
    Figure Legend Snippet: Slopes of the dose response curves established using the dLISA approach correlated with TIMP-1 fucosylation. (A) Dose–response curves of serum samples spiked with differentially fucosylated recombinant TIMP-1. Recombinant TIMP-1 was treated by α1, 2 fucosidase at different length of time (0, 15, 30, and 45 minutes) before they were spiked into with four serum aliquots. These aliquots came from the same pool of sera with endogenous TIMP-1 immuno-depleted (confirmed by the TIMP-1 immunoassay). After the recombinant protein spiked in, these serum samples underwent the dLISA approach. (B) A graph presentation of linear regression slopes of the dose–response curves versus the length of fucosidase treatment (minutes).

    Techniques Used: Recombinant

    Related Articles

    Sonication:

    Article Title: Carbohydrate Sequence of the Prostate Cancer-associated Antigen F77 Assigned by a Mucin O-Glycome Designer Array *
    Article Snippet: .. After a brief sonication, 200 units of α1–2 fucosidase (New England Biolabs) were added, and the mixture was incubated at 37 °C for 48 h. The reaction mixture was purified by a C18 cartridge, and the products were eluted with CHCl3 /MeOH/H2 O, 30:70:30. .. Mass Spectrometry MALDI-MS of the oligosaccharides and the derived NGLs was carried out on a TOF Spec-2E (Waters) or an AXIMA Assurance (Shimadzu, Manchester, UK) instrument.

    Incubation:

    Article Title: Carbohydrate Sequence of the Prostate Cancer-associated Antigen F77 Assigned by a Mucin O-Glycome Designer Array *
    Article Snippet: .. After a brief sonication, 200 units of α1–2 fucosidase (New England Biolabs) were added, and the mixture was incubated at 37 °C for 48 h. The reaction mixture was purified by a C18 cartridge, and the products were eluted with CHCl3 /MeOH/H2 O, 30:70:30. .. Mass Spectrometry MALDI-MS of the oligosaccharides and the derived NGLs was carried out on a TOF Spec-2E (Waters) or an AXIMA Assurance (Shimadzu, Manchester, UK) instrument.

    Purification:

    Article Title: Carbohydrate Sequence of the Prostate Cancer-associated Antigen F77 Assigned by a Mucin O-Glycome Designer Array *
    Article Snippet: .. After a brief sonication, 200 units of α1–2 fucosidase (New England Biolabs) were added, and the mixture was incubated at 37 °C for 48 h. The reaction mixture was purified by a C18 cartridge, and the products were eluted with CHCl3 /MeOH/H2 O, 30:70:30. .. Mass Spectrometry MALDI-MS of the oligosaccharides and the derived NGLs was carried out on a TOF Spec-2E (Waters) or an AXIMA Assurance (Shimadzu, Manchester, UK) instrument.

    Isolation:

    Article Title: Site-specific Glycoforms of Haptoglobin in Liver Cirrhosis and Hepatocellular Carcinoma *
    Article Snippet: Two microliters of each exoglycosidase (100 units of neuraminidase and 16 units of galactosidase) were added to the sample based on the manufacturer's recommendation and incubated at 37°C for 20 h. We have verified that each glycosidase reaction reaches completeness by inspection of the spectra (disappearance of the peaks) of known glycoforms. .. 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.

    Recombinant:

    Article Title: Glycan Epitopes on 201B7 Human-Induced Pluripotent Stem Cells Using R-10G and R-17F Marker Antibodies
    Article Snippet: Anti-human iPSC/ESC, R-10G (mouse IgG1), and R-17F (mouse IgG1) antibodies were prepared as described previously [ , ]. .. Peptide N-glycanase (PNGase F; recombinant protein from Escherichia coli ) was obtained from Roche Diagnostics GmbH (Mannheim, Germany), neuraminidase (Arthrobacter ureafaciens ) from Nacalai Tesque (Kyoto, Japan), α1-3/4 fucosidase from TaKaRa Bio, Inc. (Shiga, Japan), and α1-2 fucosidase from New England Biolabs (Ipswich, MA, USA). .. Chondroitinase ABC (Proteus vulgaris ), heparinase mixture (heparinase, heparitinase I, and heparitinase II), keratanase (Pseudomonas sp.), keratanase II (Bacillus sp.), and endo-β-galactosidase (Escherichia freundii) were obtained from Seikagaku Biobusiness (Tokyo, Japan).

    Article Title: Analysis of serum protein glycosylation by a differential lectin immunosorbant assay (dLISA)
    Article Snippet: .. Production of the differential fucosylated recombinant TIMP-1 Four microliter of the recombinant TIMP-1 (10 μg/mL prepared in PBS + 1% BSA buffer) was mixed with 4 μL of α1, 2 fucosidase (Catalog# P0724, New England Biolabs, Ipswich, MA). .. The mixture (8 μL) was then diluted 5 times in the 32 μL of the Reaction buffer (50 mM Sodium Citrate, 100 mM Sodium Chloride, pH 6.0) for incubation of 0, 15, 30, or 45 minutes with shaking at 37°C.

    Blocking Assay:

    Article Title: Bacterial AB5 toxins inhibit the growth of gut bacteria by targeting ganglioside-like glycoconjugates
    Article Snippet: Slides were blocked for 1 h using blocking buffer (PBS containing: 0.2% Triton X-100, 0.05% Tween, 1% bovine serum albumin, 5% donkey serum). .. Where indicated, slides were treated with α1-2-fucosidase (NEB, P0724S) following antigen retrieval in sodium citrate buffer, but prior to blocking with donkey serum buffer. .. Slides were treated for 1 h, with 1 μl (20 units) of α1-2-fucosidase in 10 μl of 1× Glycobuffer (supplied by the manufacturer), at 37 °C, followed by a PBS wash. Each slide was then treated with CTB (1 mM, Sigma, Cat. No. C9903) for 1 h, followed by either α-CTB antibody (1:100) or α-GM1 antibody (1:100, Abcam) for 1 h. Slides were visualized using Alexa Fluor 488-conjugated donkey α-rabbit IgG (1:1000, Invitrogen).

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    New England Biolabs fucosidase
    C3d expression and MAC formation on hypoxia-stressed iPS-RPE cells following <t>fucosidase</t> treatment. ( a ) Representative immunofluorescence images showing C3d deposition on the surface of hypoxia-stressed iPS-RPE cells treated or not overnight with fucosidase. C3d (green), nuclei nuclei (blue) and phalloidin (grey) are shown. Scale bars, 50 μm. ( b ) Quantification of C3d expression level on hypoxia-stressed iPS- RPE cells compared to fucosidase-treated hypoxic cells using ImageJ software. ( c ) Representative immunofluorescence images showing MAC staining on the surface of hypoxia-stressed iPS-RPE cells treated or not overnight with fucosidase. MAC (red), nuclei (blue) and phalloidin (grey) are shown. Scale bars, 50 μm.
    Fucosidase, 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/fucosidase/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fucosidase - by Bioz Stars, 2021-06
    95/100 stars
      Buy from Supplier

    Image Search Results


    C3d expression and MAC formation on hypoxia-stressed iPS-RPE cells following fucosidase treatment. ( a ) Representative immunofluorescence images showing C3d deposition on the surface of hypoxia-stressed iPS-RPE cells treated or not overnight with fucosidase. C3d (green), nuclei nuclei (blue) and phalloidin (grey) are shown. Scale bars, 50 μm. ( b ) Quantification of C3d expression level on hypoxia-stressed iPS- RPE cells compared to fucosidase-treated hypoxic cells using ImageJ software. ( c ) Representative immunofluorescence images showing MAC staining on the surface of hypoxia-stressed iPS-RPE cells treated or not overnight with fucosidase. MAC (red), nuclei (blue) and phalloidin (grey) are shown. Scale bars, 50 μm.

    Journal: Scientific Reports

    Article Title: Human stem cell-derived retinal epithelial cells activate complement via collectin 11 in response to stress

    doi: 10.1038/s41598-017-15212-z

    Figure Lengend Snippet: C3d expression and MAC formation on hypoxia-stressed iPS-RPE cells following fucosidase treatment. ( a ) Representative immunofluorescence images showing C3d deposition on the surface of hypoxia-stressed iPS-RPE cells treated or not overnight with fucosidase. C3d (green), nuclei nuclei (blue) and phalloidin (grey) are shown. Scale bars, 50 μm. ( b ) Quantification of C3d expression level on hypoxia-stressed iPS- RPE cells compared to fucosidase-treated hypoxic cells using ImageJ software. ( c ) Representative immunofluorescence images showing MAC staining on the surface of hypoxia-stressed iPS-RPE cells treated or not overnight with fucosidase. MAC (red), nuclei (blue) and phalloidin (grey) are shown. Scale bars, 50 μm.

    Article Snippet: To remove L-fucose from cell surface, iPS-RPE cells were put under hypoxic conditions for 24 hours, fixed in 4% paraformaldehyde for 1 hour at room temperature and treated then with α1-2,3,4,6 fucosidase (New England BioLabs) at 37 °C overnight.

    Techniques: Expressing, Immunofluorescence, Software, Staining

    Identification of fucosylated glycoproteins in ESCC revealed regulators of invasion and metastasis. (A) Schematic illustration of the experimental approach showing affinity enrichment of core-fucosylated and α-1,2-fucosylated proteins by LCA and UEA-I lectin affinity chromatography respectively. (B) The effect of enriched fucosylated protein by UEA-I lectin with or without α-1,2-fucosidase on KYSE150 and KYSE450 cell invasion. (C) Coomassie brilliant blue (CBB) staining of gels of whole cell lysate proteins and LCA enriched fucosylated proteins in TSTA3-WT and control group. (D) Number of overlapping proteins between lectin enriched proteins identified by in gel mass spectrometry analysis and differentially expressed glycoproteins in N-glycoproteomics data. (E) LCA affinity chromatography of whole-cell lysates of ESCC cells transfected with TSTA3-WT and NC followed by western blot with LAMP2 antibody. (F) A representative western blot of LCA-affinity purified LAMP2. LCA-affinity purification was done in the absence or presence of various concentrations of α-L-fucose (0, 6, 30 and 60 mM). (G) LAMP2 immunoprecipitation from whole-cell lysates of KYSE150 and KYSE450 cells transfected with TSTA3-WT and NC. Anti-LAMP2 immunoprecipitate was treated with or without PNGase F and blotted with biotinylated LCA or LAMP2 antibody. (H) UEA-I affinity chromatography of whole-cell lysate of ESCC cells transfected with TSTA3-WT and NC followed by western blot with ERBB2 antibody. (I) A representative western blot of UEA-I-affinity purified ERBB2. UEA-I-affinity purification was done in the absence or presence of various concentrations of α-L-fucose. (J) ERBB2 immunoprecipitation from whole-cell lysates of KYSE150 and KYSE450 cells transfected with TSTA3-WT and NC. Anti-ERBB2 immunoprecipitate was treated with or without PNGase F and blotted with biotinylated UEA-I or ERBB2 antibody.

    Journal: Theranostics

    Article Title: TSTA3 facilitates esophageal squamous cell carcinoma progression through regulating fucosylation of LAMP2 and ERBB2

    doi: 10.7150/thno.48225

    Figure Lengend Snippet: Identification of fucosylated glycoproteins in ESCC revealed regulators of invasion and metastasis. (A) Schematic illustration of the experimental approach showing affinity enrichment of core-fucosylated and α-1,2-fucosylated proteins by LCA and UEA-I lectin affinity chromatography respectively. (B) The effect of enriched fucosylated protein by UEA-I lectin with or without α-1,2-fucosidase on KYSE150 and KYSE450 cell invasion. (C) Coomassie brilliant blue (CBB) staining of gels of whole cell lysate proteins and LCA enriched fucosylated proteins in TSTA3-WT and control group. (D) Number of overlapping proteins between lectin enriched proteins identified by in gel mass spectrometry analysis and differentially expressed glycoproteins in N-glycoproteomics data. (E) LCA affinity chromatography of whole-cell lysates of ESCC cells transfected with TSTA3-WT and NC followed by western blot with LAMP2 antibody. (F) A representative western blot of LCA-affinity purified LAMP2. LCA-affinity purification was done in the absence or presence of various concentrations of α-L-fucose (0, 6, 30 and 60 mM). (G) LAMP2 immunoprecipitation from whole-cell lysates of KYSE150 and KYSE450 cells transfected with TSTA3-WT and NC. Anti-LAMP2 immunoprecipitate was treated with or without PNGase F and blotted with biotinylated LCA or LAMP2 antibody. (H) UEA-I affinity chromatography of whole-cell lysate of ESCC cells transfected with TSTA3-WT and NC followed by western blot with ERBB2 antibody. (I) A representative western blot of UEA-I-affinity purified ERBB2. UEA-I-affinity purification was done in the absence or presence of various concentrations of α-L-fucose. (J) ERBB2 immunoprecipitation from whole-cell lysates of KYSE150 and KYSE450 cells transfected with TSTA3-WT and NC. Anti-ERBB2 immunoprecipitate was treated with or without PNGase F and blotted with biotinylated UEA-I or ERBB2 antibody.

    Article Snippet: Alternatively, samples were treated with fucosidase (NEB) according to the manufacturer's protocol at 37 °C for 4 h.

    Techniques: Affinity Chromatography, Staining, Mass Spectrometry, Transfection, Western Blot, Affinity Purification, Immunoprecipitation

    Characterization of the purified R-10G-binding protein by glycosidase digestion and Western blotting. Purified R-10G-binding protein (0.5–4 ng) incubated with (+) or without (−) glycosidases was subjected to SDS-PAGE on a 4–15% gradient polyacrylamide gel under non-reducing conditions. The exception was PNGase F digestion, which requires preheating under reducing conditions. Western blotting using R-10G was subsequently conducted. ( A ) Purified R-10G-binding protein from 201B7 cells was digested with PNGase F (lane 1), chondroitinase ABC (lane 2), a heparinase mixture (lane 3), α1-3/4 fucosidase (lane 4), α1-2 fucosidase (lane 5), neuraminidase (lane 6), and keratanase (lane 7), and the digests were analyzed by Western blotting using R-10G. ( B ) Purified R-10G-binding protein from 201B7 (lanes 1, 3) and Tic (lanes 2, 4) cells incubated with (+) or without (−) endo-β-galactosidase (lanes 1, 2) or keratanase II (lanes 3, 4) was analyzed by Western blotting using R-10G.

    Journal: Biomolecules

    Article Title: Glycan Epitopes on 201B7 Human-Induced Pluripotent Stem Cells Using R-10G and R-17F Marker Antibodies

    doi: 10.3390/biom11040508

    Figure Lengend Snippet: Characterization of the purified R-10G-binding protein by glycosidase digestion and Western blotting. Purified R-10G-binding protein (0.5–4 ng) incubated with (+) or without (−) glycosidases was subjected to SDS-PAGE on a 4–15% gradient polyacrylamide gel under non-reducing conditions. The exception was PNGase F digestion, which requires preheating under reducing conditions. Western blotting using R-10G was subsequently conducted. ( A ) Purified R-10G-binding protein from 201B7 cells was digested with PNGase F (lane 1), chondroitinase ABC (lane 2), a heparinase mixture (lane 3), α1-3/4 fucosidase (lane 4), α1-2 fucosidase (lane 5), neuraminidase (lane 6), and keratanase (lane 7), and the digests were analyzed by Western blotting using R-10G. ( B ) Purified R-10G-binding protein from 201B7 (lanes 1, 3) and Tic (lanes 2, 4) cells incubated with (+) or without (−) endo-β-galactosidase (lanes 1, 2) or keratanase II (lanes 3, 4) was analyzed by Western blotting using R-10G.

    Article Snippet: Peptide N-glycanase (PNGase F; recombinant protein from Escherichia coli ) was obtained from Roche Diagnostics GmbH (Mannheim, Germany), neuraminidase (Arthrobacter ureafaciens ) from Nacalai Tesque (Kyoto, Japan), α1-3/4 fucosidase from TaKaRa Bio, Inc. (Shiga, Japan), and α1-2 fucosidase from New England Biolabs (Ipswich, MA, USA).

    Techniques: Purification, Binding Assay, Western Blot, Incubation, SDS Page

    MALDI-MS analysis of NGL 4M-f1 before ( A ) and after ( B ) treatment with α1–2 fucosidase. The change in molecular ion [MH] + from m / z 2035 ( A ) to 1889 ( B ) indicated the capping sequence Fucα1–2Gal in 4M-f1. Abbreviations are as in legend to Fig. 4 .

    Journal: The Journal of Biological Chemistry

    Article Title: Carbohydrate Sequence of the Prostate Cancer-associated Antigen F77 Assigned by a Mucin O-Glycome Designer Array *

    doi: 10.1074/jbc.M114.558932

    Figure Lengend Snippet: MALDI-MS analysis of NGL 4M-f1 before ( A ) and after ( B ) treatment with α1–2 fucosidase. The change in molecular ion [MH] + from m / z 2035 ( A ) to 1889 ( B ) indicated the capping sequence Fucα1–2Gal in 4M-f1. Abbreviations are as in legend to Fig. 4 .

    Article Snippet: After a brief sonication, 200 units of α1–2 fucosidase (New England Biolabs) were added, and the mixture was incubated at 37 °C for 48 h. The reaction mixture was purified by a C18 cartridge, and the products were eluted with CHCl3 /MeOH/H2 O, 30:70:30.

    Techniques: Mass Spectrometry, Sequencing