endo s  (New England Biolabs)


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    Name:
    Endo S
    Description:
    Endo S 30 000 units
    Catalog Number:
    p0741l
    Price:
    762
    Size:
    30 000 units
    Category:
    Glycosidases
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    Structured Review

    New England Biolabs endo s
    Endo S
    Endo S 30 000 units
    https://www.bioz.com/result/endo s/product/New England Biolabs
    Average 96 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    endo s - by Bioz Stars, 2020-08
    96/100 stars

    Images

    1) Product Images from "Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG"

    Article Title: Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-17467-y

    SDS-PAGE analysis of the hydrolytic activities of recombinant proteins against rituximab and RNase B. Rituximab ( A ) or RNase B ( B ) was incubated separately with Endo-S, Endo-CC1, ORF1188, ORF1152, ORF3046 or ORF3750 proteins overnight. Reaction mixtures were then subjected to SDS-PAGE analysis using either a 12% (for rituximab) or a 15% (for RNase B) acrylamide gel. Untreated rituximab (IgG) and RNase B were used as negative controls in ( A ) and ( B ), respectively. After SDS-PAGE, gels were stained with CBB. In ( A ), the heavy chain of IgG migrated as at approximately 50 kDa protein.
    Figure Legend Snippet: SDS-PAGE analysis of the hydrolytic activities of recombinant proteins against rituximab and RNase B. Rituximab ( A ) or RNase B ( B ) was incubated separately with Endo-S, Endo-CC1, ORF1188, ORF1152, ORF3046 or ORF3750 proteins overnight. Reaction mixtures were then subjected to SDS-PAGE analysis using either a 12% (for rituximab) or a 15% (for RNase B) acrylamide gel. Untreated rituximab (IgG) and RNase B were used as negative controls in ( A ) and ( B ), respectively. After SDS-PAGE, gels were stained with CBB. In ( A ), the heavy chain of IgG migrated as at approximately 50 kDa protein.

    Techniques Used: SDS Page, Recombinant, Incubation, Acrylamide Gel Assay, Staining

    Characterization of Beauveria and Cordyceps ENGases. ( A ) Recombinant Beauveria and Cordyceps ENGases were expressed in E. coli and were purified. Protein samples (0.5 μg of each) were then subjected to SDS-PAGE using a 5–20% acrylamide gel, following which the gel was stained with CBB. ( B ) Effects of pH on the enzymatic activity of Beauveria and Cordyceps ENGases. The assay was carried out using 100 mM buffers at various pHs. ( C ) Rituximab (IgG) was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE. The CBB stained gel shows the heavy chain of IgG is migrating as a protein with MW of approximately 50 kDa. ( D ) RNase B was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE.
    Figure Legend Snippet: Characterization of Beauveria and Cordyceps ENGases. ( A ) Recombinant Beauveria and Cordyceps ENGases were expressed in E. coli and were purified. Protein samples (0.5 μg of each) were then subjected to SDS-PAGE using a 5–20% acrylamide gel, following which the gel was stained with CBB. ( B ) Effects of pH on the enzymatic activity of Beauveria and Cordyceps ENGases. The assay was carried out using 100 mM buffers at various pHs. ( C ) Rituximab (IgG) was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE. The CBB stained gel shows the heavy chain of IgG is migrating as a protein with MW of approximately 50 kDa. ( D ) RNase B was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE.

    Techniques Used: Recombinant, Purification, SDS Page, Acrylamide Gel Assay, Staining, Activity Assay, Incubation

    2) Product Images from "Generation of a Mutant Mucor hiemalis Endoglycosidase That Acts on Core-fucosylated N-Glycans *"

    Article Title: Generation of a Mutant Mucor hiemalis Endoglycosidase That Acts on Core-fucosylated N-Glycans *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M116.737395

    MALDI-TOF/MS analyses of the glycans from rituximab glycopeptides, released by treatment with various enzymes. Glycopeptides of rituximab were prepared and treated with PNGase F ( A ), wild-type Endo-M ( B ), W251N variant ( C ), and Endo-S (positive control)
    Figure Legend Snippet: MALDI-TOF/MS analyses of the glycans from rituximab glycopeptides, released by treatment with various enzymes. Glycopeptides of rituximab were prepared and treated with PNGase F ( A ), wild-type Endo-M ( B ), W251N variant ( C ), and Endo-S (positive control)

    Techniques Used: Mass Spectrometry, Variant Assay, Positive Control

    Hydrolysis of the N -glycans of human lactoferrin by the W251N variant. A , MALDI-TOF/MS spectrum of permethylated N -glycans released from the tryptic glycopeptides of human lactoferrin by PNGase F. B , hLF (10 μg) was treated with either Endo-S
    Figure Legend Snippet: Hydrolysis of the N -glycans of human lactoferrin by the W251N variant. A , MALDI-TOF/MS spectrum of permethylated N -glycans released from the tryptic glycopeptides of human lactoferrin by PNGase F. B , hLF (10 μg) was treated with either Endo-S

    Techniques Used: Variant Assay, Mass Spectrometry

    3) Product Images from "Evaluation of a glycoengineered monoclonal antibody via LC-MS analysis in combination with multiple enzymatic digestion"

    Article Title: Evaluation of a glycoengineered monoclonal antibody via LC-MS analysis in combination with multiple enzymatic digestion

    Journal: mAbs

    doi: 10.1080/19420862.2015.1113361

    HPLC-FLD profile of procainamide labeled N -glycans from rituximab and the glycoengineered rituximab with α2,6 linked sialic acid. A). HPLC profile of rituximab N -glycans with major species shown. B). The glycan profile from the glycoengineered rituximab prepared by Endo S digestion. The major glycan is G2FS2 with α2,6 linked sialic acid. C). The glycan profile from the glycoengineered rituximab after α2-3 Neuraminidase S treatment. D). The glycan profile from the glycoengineered rituximab after α2-3,6,8,9 Neuraminidase A treatment. E). The glycan profile from the glycoengineered rituximab prepared by Endo S2 digestion.
    Figure Legend Snippet: HPLC-FLD profile of procainamide labeled N -glycans from rituximab and the glycoengineered rituximab with α2,6 linked sialic acid. A). HPLC profile of rituximab N -glycans with major species shown. B). The glycan profile from the glycoengineered rituximab prepared by Endo S digestion. The major glycan is G2FS2 with α2,6 linked sialic acid. C). The glycan profile from the glycoengineered rituximab after α2-3 Neuraminidase S treatment. D). The glycan profile from the glycoengineered rituximab after α2-3,6,8,9 Neuraminidase A treatment. E). The glycan profile from the glycoengineered rituximab prepared by Endo S2 digestion.

    Techniques Used: High Performance Liquid Chromatography, Labeling

    4) Product Images from "Generation and Comparative Kinetic Analysis of New Glycosynthase Mutants from Streptococcus pyogenes Endoglycosidases for Antibody Glycoengineering"

    Article Title: Generation and Comparative Kinetic Analysis of New Glycosynthase Mutants from Streptococcus pyogenes Endoglycosidases for Antibody Glycoengineering

    Journal: Biochemistry

    doi: 10.1021/acs.biochem.8b00719

    Comparison of the transglycosylation reaction of Endo-S D233M and previously reported Endo-S D233Q and D233A using SCT-Oxa as the substrate. The reaction was conducted by incubating the deglycosylated antibody and SCT-Oxa with a fixed concentration of each enzyme (0.05 mg/mL). The molar ratio of antibody to oxazoline was controlled at 1/20. The data sets presented here are representative of three independent experiments.
    Figure Legend Snippet: Comparison of the transglycosylation reaction of Endo-S D233M and previously reported Endo-S D233Q and D233A using SCT-Oxa as the substrate. The reaction was conducted by incubating the deglycosylated antibody and SCT-Oxa with a fixed concentration of each enzyme (0.05 mg/mL). The molar ratio of antibody to oxazoline was controlled at 1/20. The data sets presented here are representative of three independent experiments.

    Techniques Used: Concentration Assay

    5) Product Images from "Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG"

    Article Title: Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-17467-y

    SDS-PAGE analysis of the hydrolytic activities of recombinant proteins against rituximab and RNase B. Rituximab ( A ) or RNase B ( B ) was incubated separately with Endo-S, Endo-CC1, ORF1188, ORF1152, ORF3046 or ORF3750 proteins overnight. Reaction mixtures were then subjected to SDS-PAGE analysis using either a 12% (for rituximab) or a 15% (for RNase B) acrylamide gel. Untreated rituximab (IgG) and RNase B were used as negative controls in ( A ) and ( B ), respectively. After SDS-PAGE, gels were stained with CBB. In ( A ), the heavy chain of IgG migrated as at approximately 50 kDa protein.
    Figure Legend Snippet: SDS-PAGE analysis of the hydrolytic activities of recombinant proteins against rituximab and RNase B. Rituximab ( A ) or RNase B ( B ) was incubated separately with Endo-S, Endo-CC1, ORF1188, ORF1152, ORF3046 or ORF3750 proteins overnight. Reaction mixtures were then subjected to SDS-PAGE analysis using either a 12% (for rituximab) or a 15% (for RNase B) acrylamide gel. Untreated rituximab (IgG) and RNase B were used as negative controls in ( A ) and ( B ), respectively. After SDS-PAGE, gels were stained with CBB. In ( A ), the heavy chain of IgG migrated as at approximately 50 kDa protein.

    Techniques Used: SDS Page, Recombinant, Incubation, Acrylamide Gel Assay, Staining

    Characterization of Beauveria and Cordyceps ENGases. ( A ) Recombinant Beauveria and Cordyceps ENGases were expressed in E. coli and were purified. Protein samples (0.5 μg of each) were then subjected to SDS-PAGE using a 5–20% acrylamide gel, following which the gel was stained with CBB. ( B ) Effects of pH on the enzymatic activity of Beauveria and Cordyceps ENGases. The assay was carried out using 100 mM buffers at various pHs. ( C ) Rituximab (IgG) was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE. The CBB stained gel shows the heavy chain of IgG is migrating as a protein with MW of approximately 50 kDa. ( D ) RNase B was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE.
    Figure Legend Snippet: Characterization of Beauveria and Cordyceps ENGases. ( A ) Recombinant Beauveria and Cordyceps ENGases were expressed in E. coli and were purified. Protein samples (0.5 μg of each) were then subjected to SDS-PAGE using a 5–20% acrylamide gel, following which the gel was stained with CBB. ( B ) Effects of pH on the enzymatic activity of Beauveria and Cordyceps ENGases. The assay was carried out using 100 mM buffers at various pHs. ( C ) Rituximab (IgG) was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE. The CBB stained gel shows the heavy chain of IgG is migrating as a protein with MW of approximately 50 kDa. ( D ) RNase B was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE.

    Techniques Used: Recombinant, Purification, SDS Page, Acrylamide Gel Assay, Staining, Activity Assay, Incubation

    Related Articles

    Magnetic Beads:

    Article Title: CD32a antibodies induce thrombocytopenia and type II hypersensitivity reactions in FCGR2A mice
    Article Snippet: .. IV.3 was deglycosylated with Endo S (NEB), which was then removed by chitin magnetic beads (NEB), followed by dialysis in PBS. .. For certain experiments, aglycosyl-IV.3 was labeled with AlexaFluor488 .

    Mutagenesis:

    Article Title: Generation and Comparative Kinetic Analysis of New Glycosynthase Mutants from Streptococcus pyogenes Endoglycosidases for Antibody Glycoengineering
    Article Snippet: .. The Endo-S mutants were generated using the Q5 Site-Directed Mutagenesis Kit (NEB) by the manufacturer’s instructions. .. For systematic mutagenesis at Asp-233, the following two degenerate primers were used: 5′-CGTAAATTCGTGCTCAATNNNAATATCTAGTCCATCGACACCACGATCAGTT-3′ (forward) and 5′AACTGATCGTGGTGTCGATGGACTAGATATTNNN- ATTGAGCACGAATTTACG-3′ (reverse).

    Autoradiography:

    Article Title: Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation
    Article Snippet: .. For Endo H and Endo F digestions, the washed immunoprecipitate was divided into two and the Endo H/F (New England Biolabs) added to one of the samples (according to the manufacturer’s instructions), and incubated for 1 h at 37°C before analysis by SDS–PAGE and autoradiography. .. HeLa-M and HeLa-M KK3 cells were grown overnight onto 13 mm glass coverslips, transiently transfected the next day with 0.5 µg of the HLA-A2 construct DNA using Fugene (Roche) and analysed 48 h later.

    Generated:

    Article Title: Generation and Comparative Kinetic Analysis of New Glycosynthase Mutants from Streptococcus pyogenes Endoglycosidases for Antibody Glycoengineering
    Article Snippet: .. The Endo-S mutants were generated using the Q5 Site-Directed Mutagenesis Kit (NEB) by the manufacturer’s instructions. .. For systematic mutagenesis at Asp-233, the following two degenerate primers were used: 5′-CGTAAATTCGTGCTCAATNNNAATATCTAGTCCATCGACACCACGATCAGTT-3′ (forward) and 5′AACTGATCGTGGTGTCGATGGACTAGATATTNNN- ATTGAGCACGAATTTACG-3′ (reverse).

    Incubation:

    Article Title: Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation
    Article Snippet: .. For Endo H and Endo F digestions, the washed immunoprecipitate was divided into two and the Endo H/F (New England Biolabs) added to one of the samples (according to the manufacturer’s instructions), and incubated for 1 h at 37°C before analysis by SDS–PAGE and autoradiography. .. HeLa-M and HeLa-M KK3 cells were grown overnight onto 13 mm glass coverslips, transiently transfected the next day with 0.5 µg of the HLA-A2 construct DNA using Fugene (Roche) and analysed 48 h later.

    Article Title: Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG
    Article Snippet: .. In addition, 200 unit of Endo-S (NEB) was incubated in parallel either with 10 μg of RNase B or with 10 μg of rituximab in 50 μL of 1x GlycoBuffer 1 overnight at 37 °C. .. Subsequently, all reaction samples were subjected to SDS-PAGE, following which gels were stained with Coomassie Brilliant Blue (CBB) EzStain AQua (Atto).

    other:

    Article Title: Profiling of core fucosylated N-glycans using a novel bacterial lectin that specifically recognizes α1,6 fucosylated chitobiose
    Article Snippet: Rapid Peptide-N-Glycosidase (PNGase F), Remove-iT® Endo S, α1-2,4,6 Fucosidase, and Proteinase K were from New England Biolabs (Ipswich, MA).

    Article Title: Generation of a Mutant Mucor hiemalis Endoglycosidase That Acts on Core-fucosylated N-Glycans *
    Article Snippet: Endo-S was purchased from New England BioLabs (Ipswich, MA).

    SDS Page:

    Article Title: Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation
    Article Snippet: .. For Endo H and Endo F digestions, the washed immunoprecipitate was divided into two and the Endo H/F (New England Biolabs) added to one of the samples (according to the manufacturer’s instructions), and incubated for 1 h at 37°C before analysis by SDS–PAGE and autoradiography. .. HeLa-M and HeLa-M KK3 cells were grown overnight onto 13 mm glass coverslips, transiently transfected the next day with 0.5 µg of the HLA-A2 construct DNA using Fugene (Roche) and analysed 48 h later.

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  • 96
    New England Biolabs endo s
    SDS-PAGE analysis of the hydrolytic activities of recombinant proteins against rituximab and RNase B. Rituximab ( A ) or RNase B ( B ) was incubated separately with <t>Endo-S,</t> Endo-CC1, ORF1188, ORF1152, ORF3046 or ORF3750 proteins overnight. Reaction mixtures were then subjected to SDS-PAGE analysis using either a 12% (for rituximab) or a 15% (for RNase B) acrylamide gel. Untreated rituximab (IgG) and RNase B were used as negative controls in ( A ) and ( B ), respectively. After SDS-PAGE, gels were stained with CBB. In ( A ), the heavy chain of IgG migrated as at approximately 50 kDa protein.
    Endo S, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/endo s/product/New England Biolabs
    Average 96 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    endo s - by Bioz Stars, 2020-08
    96/100 stars
      Buy from Supplier

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    SDS-PAGE analysis of the hydrolytic activities of recombinant proteins against rituximab and RNase B. Rituximab ( A ) or RNase B ( B ) was incubated separately with Endo-S, Endo-CC1, ORF1188, ORF1152, ORF3046 or ORF3750 proteins overnight. Reaction mixtures were then subjected to SDS-PAGE analysis using either a 12% (for rituximab) or a 15% (for RNase B) acrylamide gel. Untreated rituximab (IgG) and RNase B were used as negative controls in ( A ) and ( B ), respectively. After SDS-PAGE, gels were stained with CBB. In ( A ), the heavy chain of IgG migrated as at approximately 50 kDa protein.

    Journal: Scientific Reports

    Article Title: Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG

    doi: 10.1038/s41598-017-17467-y

    Figure Lengend Snippet: SDS-PAGE analysis of the hydrolytic activities of recombinant proteins against rituximab and RNase B. Rituximab ( A ) or RNase B ( B ) was incubated separately with Endo-S, Endo-CC1, ORF1188, ORF1152, ORF3046 or ORF3750 proteins overnight. Reaction mixtures were then subjected to SDS-PAGE analysis using either a 12% (for rituximab) or a 15% (for RNase B) acrylamide gel. Untreated rituximab (IgG) and RNase B were used as negative controls in ( A ) and ( B ), respectively. After SDS-PAGE, gels were stained with CBB. In ( A ), the heavy chain of IgG migrated as at approximately 50 kDa protein.

    Article Snippet: In addition, 200 unit of Endo-S (NEB) was incubated in parallel either with 10 μg of RNase B or with 10 μg of rituximab in 50 μL of 1x GlycoBuffer 1 overnight at 37 °C.

    Techniques: SDS Page, Recombinant, Incubation, Acrylamide Gel Assay, Staining

    Characterization of Beauveria and Cordyceps ENGases. ( A ) Recombinant Beauveria and Cordyceps ENGases were expressed in E. coli and were purified. Protein samples (0.5 μg of each) were then subjected to SDS-PAGE using a 5–20% acrylamide gel, following which the gel was stained with CBB. ( B ) Effects of pH on the enzymatic activity of Beauveria and Cordyceps ENGases. The assay was carried out using 100 mM buffers at various pHs. ( C ) Rituximab (IgG) was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE. The CBB stained gel shows the heavy chain of IgG is migrating as a protein with MW of approximately 50 kDa. ( D ) RNase B was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE.

    Journal: Scientific Reports

    Article Title: Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG

    doi: 10.1038/s41598-017-17467-y

    Figure Lengend Snippet: Characterization of Beauveria and Cordyceps ENGases. ( A ) Recombinant Beauveria and Cordyceps ENGases were expressed in E. coli and were purified. Protein samples (0.5 μg of each) were then subjected to SDS-PAGE using a 5–20% acrylamide gel, following which the gel was stained with CBB. ( B ) Effects of pH on the enzymatic activity of Beauveria and Cordyceps ENGases. The assay was carried out using 100 mM buffers at various pHs. ( C ) Rituximab (IgG) was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE. The CBB stained gel shows the heavy chain of IgG is migrating as a protein with MW of approximately 50 kDa. ( D ) RNase B was incubated separately with Endo-S, Endo-CC1, recombinant Beauveria ENGase and recombinant Cordyceps ENGase overnight and subsequently analyzed by SDS-PAGE.

    Article Snippet: In addition, 200 unit of Endo-S (NEB) was incubated in parallel either with 10 μg of RNase B or with 10 μg of rituximab in 50 μL of 1x GlycoBuffer 1 overnight at 37 °C.

    Techniques: Recombinant, Purification, SDS Page, Acrylamide Gel Assay, Staining, Activity Assay, Incubation

    MALDI-TOF/MS analyses of the glycans from rituximab glycopeptides, released by treatment with various enzymes. Glycopeptides of rituximab were prepared and treated with PNGase F ( A ), wild-type Endo-M ( B ), W251N variant ( C ), and Endo-S (positive control)

    Journal: The Journal of Biological Chemistry

    Article Title: Generation of a Mutant Mucor hiemalis Endoglycosidase That Acts on Core-fucosylated N-Glycans *

    doi: 10.1074/jbc.M116.737395

    Figure Lengend Snippet: MALDI-TOF/MS analyses of the glycans from rituximab glycopeptides, released by treatment with various enzymes. Glycopeptides of rituximab were prepared and treated with PNGase F ( A ), wild-type Endo-M ( B ), W251N variant ( C ), and Endo-S (positive control)

    Article Snippet: Endo-S was purchased from New England BioLabs (Ipswich, MA).

    Techniques: Mass Spectrometry, Variant Assay, Positive Control

    Hydrolysis of the N -glycans of human lactoferrin by the W251N variant. A , MALDI-TOF/MS spectrum of permethylated N -glycans released from the tryptic glycopeptides of human lactoferrin by PNGase F. B , hLF (10 μg) was treated with either Endo-S

    Journal: The Journal of Biological Chemistry

    Article Title: Generation of a Mutant Mucor hiemalis Endoglycosidase That Acts on Core-fucosylated N-Glycans *

    doi: 10.1074/jbc.M116.737395

    Figure Lengend Snippet: Hydrolysis of the N -glycans of human lactoferrin by the W251N variant. A , MALDI-TOF/MS spectrum of permethylated N -glycans released from the tryptic glycopeptides of human lactoferrin by PNGase F. B , hLF (10 μg) was treated with either Endo-S

    Article Snippet: Endo-S was purchased from New England BioLabs (Ipswich, MA).

    Techniques: Variant Assay, Mass Spectrometry

    HPLC-FLD profile of procainamide labeled N -glycans from rituximab and the glycoengineered rituximab with α2,6 linked sialic acid. A). HPLC profile of rituximab N -glycans with major species shown. B). The glycan profile from the glycoengineered rituximab prepared by Endo S digestion. The major glycan is G2FS2 with α2,6 linked sialic acid. C). The glycan profile from the glycoengineered rituximab after α2-3 Neuraminidase S treatment. D). The glycan profile from the glycoengineered rituximab after α2-3,6,8,9 Neuraminidase A treatment. E). The glycan profile from the glycoengineered rituximab prepared by Endo S2 digestion.

    Journal: mAbs

    Article Title: Evaluation of a glycoengineered monoclonal antibody via LC-MS analysis in combination with multiple enzymatic digestion

    doi: 10.1080/19420862.2015.1113361

    Figure Lengend Snippet: HPLC-FLD profile of procainamide labeled N -glycans from rituximab and the glycoengineered rituximab with α2,6 linked sialic acid. A). HPLC profile of rituximab N -glycans with major species shown. B). The glycan profile from the glycoengineered rituximab prepared by Endo S digestion. The major glycan is G2FS2 with α2,6 linked sialic acid. C). The glycan profile from the glycoengineered rituximab after α2-3 Neuraminidase S treatment. D). The glycan profile from the glycoengineered rituximab after α2-3,6,8,9 Neuraminidase A treatment. E). The glycan profile from the glycoengineered rituximab prepared by Endo S2 digestion.

    Article Snippet: Trypsin-ultra (P8101S), PNGase F (P0708S), α2-3 Neuraminidase S (P0743S), α2-3,6,8,9 Neuraminidase A (P0722S), Remove-iT Endo S (P0741S) are products from New England Biolabs.

    Techniques: High Performance Liquid Chromatography, Labeling

    Comparison of the transglycosylation reaction of Endo-S D233M and previously reported Endo-S D233Q and D233A using SCT-Oxa as the substrate. The reaction was conducted by incubating the deglycosylated antibody and SCT-Oxa with a fixed concentration of each enzyme (0.05 mg/mL). The molar ratio of antibody to oxazoline was controlled at 1/20. The data sets presented here are representative of three independent experiments.

    Journal: Biochemistry

    Article Title: Generation and Comparative Kinetic Analysis of New Glycosynthase Mutants from Streptococcus pyogenes Endoglycosidases for Antibody Glycoengineering

    doi: 10.1021/acs.biochem.8b00719

    Figure Lengend Snippet: Comparison of the transglycosylation reaction of Endo-S D233M and previously reported Endo-S D233Q and D233A using SCT-Oxa as the substrate. The reaction was conducted by incubating the deglycosylated antibody and SCT-Oxa with a fixed concentration of each enzyme (0.05 mg/mL). The molar ratio of antibody to oxazoline was controlled at 1/20. The data sets presented here are representative of three independent experiments.

    Article Snippet: The Endo-S mutants were generated using the Q5 Site-Directed Mutagenesis Kit (NEB) by the manufacturer’s instructions.

    Techniques: Concentration Assay