endo d  (New England Biolabs)


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  • 92
    Name:
    Endo D
    Description:
    Endo D 7 500 units
    Catalog Number:
    p0742l
    Price:
    760
    Size:
    7 500 units
    Category:
    Glycosidases
    Buy from Supplier


    Structured Review

    New England Biolabs endo d
    Endo D
    Endo D 7 500 units
    https://www.bioz.com/result/endo d/product/New England Biolabs
    Average 92 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    endo d - by Bioz Stars, 2021-02
    92/100 stars

    Images

    1) Product Images from "Neurodegeneration-associated mutant TREM2 proteins abortively cycle between the ER and ER–Golgi intermediate compartment"

    Article Title: Neurodegeneration-associated mutant TREM2 proteins abortively cycle between the ER and ER–Golgi intermediate compartment

    Journal: Molecular Biology of the Cell

    doi: 10.1091/mbc.E17-06-0423

    Mutant TREM2 gains access to a post-ER compartment in vivo. (A) Schematic illustrating the generation of a five-mannose-containing N -linked glycan by α-mannosidase-I in the ERGIC or cis -Golgi to produce a protein that is sensitive to cleavage by endo D. (B) CHO-Lec1 cells were cotransfected with either WT or Y38C HA-TREM2 plus Arf1 (T31N), Arf1 (Q71L), or empty vector. Cells were harvested 1 d after transfection and the lysates subjected to digest by endo D. WT TREM2 is sensitive to endo D, while mutant Y38C is normally insensitive. Expression of either Arf1 (T31N) or (Q71L) uncovers endo D sensitivity for TREM2 (Y38C). RPN I serves as a loading control. (C) The ER-resident protein RPN I remains insensitive to endo D under conditions that render TREM2 (Y38C) sensitive to endo D. RPN I cleavage by endo H is detectable under the same experimental conditions. Sec22B serves as a loading control.
    Figure Legend Snippet: Mutant TREM2 gains access to a post-ER compartment in vivo. (A) Schematic illustrating the generation of a five-mannose-containing N -linked glycan by α-mannosidase-I in the ERGIC or cis -Golgi to produce a protein that is sensitive to cleavage by endo D. (B) CHO-Lec1 cells were cotransfected with either WT or Y38C HA-TREM2 plus Arf1 (T31N), Arf1 (Q71L), or empty vector. Cells were harvested 1 d after transfection and the lysates subjected to digest by endo D. WT TREM2 is sensitive to endo D, while mutant Y38C is normally insensitive. Expression of either Arf1 (T31N) or (Q71L) uncovers endo D sensitivity for TREM2 (Y38C). RPN I serves as a loading control. (C) The ER-resident protein RPN I remains insensitive to endo D under conditions that render TREM2 (Y38C) sensitive to endo D. RPN I cleavage by endo H is detectable under the same experimental conditions. Sec22B serves as a loading control.

    Techniques Used: Mutagenesis, In Vivo, Plasmid Preparation, Transfection, Expressing

    2) Product Images from "Interplay between Disulfide Bonding and N-Glycosylation Defines SLC4 Na+-coupled Transporter Extracellular Topography *"

    Article Title: Interplay between Disulfide Bonding and N-Glycosylation Defines SLC4 Na+-coupled Transporter Extracellular Topography *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M114.619320

    Deglycosylation analysis of NBCe1-A with various Asn substitutions in EL-3. A , plasma membranes of HEK 293 cells expressing various Asn substitutions in EL-3 were isolated, lysed in 2× SDS sample buffer with 2% β-ME, and resolved by 7.5% SDS-PAGE. A portion of the membrane pellet was lysed in Endo-F digestion buffer and incubated with Endo-F for 2 h at 37 °C following the manufacturer's protocol. Protein samples were then mixed with 2× SDS samples buffer with β-ME and processed as described above. B , membrane pellets containing either 9C − or NBCe1-A were lysed in the Endo-F or Endo-H digestion buffer and digested with Endo-F or Endo-H following the manufacturer's protocol. Each experiment was performed at least three times.
    Figure Legend Snippet: Deglycosylation analysis of NBCe1-A with various Asn substitutions in EL-3. A , plasma membranes of HEK 293 cells expressing various Asn substitutions in EL-3 were isolated, lysed in 2× SDS sample buffer with 2% β-ME, and resolved by 7.5% SDS-PAGE. A portion of the membrane pellet was lysed in Endo-F digestion buffer and incubated with Endo-F for 2 h at 37 °C following the manufacturer's protocol. Protein samples were then mixed with 2× SDS samples buffer with β-ME and processed as described above. B , membrane pellets containing either 9C − or NBCe1-A were lysed in the Endo-F or Endo-H digestion buffer and digested with Endo-F or Endo-H following the manufacturer's protocol. Each experiment was performed at least three times.

    Techniques Used: Expressing, Isolation, SDS Page, Incubation

    3) Product Images from "Unlocking the mystery of the hard-to-sequence phage genome: PaP1 methylome and bacterial immunity"

    Article Title: Unlocking the mystery of the hard-to-sequence phage genome: PaP1 methylome and bacterial immunity

    Journal: BMC Genomics

    doi: 10.1186/1471-2164-15-803

    Agarose gel electropherogram of Endo V digestion. (A) Digestion of the PaP1 genomic DNA by Endo V or Eco RI. Endo V digestion of the PaP1 genomic DNA produced a smear band in the gel. (B) Digestion of the PaP3 genomic DNA by Endo V or EcoRI. The PaP3 genome had been successfully sequenced using the shotgun method before. Unlike the PaP1 genomic DNA, Endo V digestion of the PaP3 genomic DNA gave no smear band in the gel.
    Figure Legend Snippet: Agarose gel electropherogram of Endo V digestion. (A) Digestion of the PaP1 genomic DNA by Endo V or Eco RI. Endo V digestion of the PaP1 genomic DNA produced a smear band in the gel. (B) Digestion of the PaP3 genomic DNA by Endo V or EcoRI. The PaP3 genome had been successfully sequenced using the shotgun method before. Unlike the PaP1 genomic DNA, Endo V digestion of the PaP3 genomic DNA gave no smear band in the gel.

    Techniques Used: Agarose Gel Electrophoresis, Produced

    4) Product Images from "Building of the Tetraspanin Web: Distinct Structural Domains of CD81 Function in Different Cellular Compartments †"

    Article Title: Building of the Tetraspanin Web: Distinct Structural Domains of CD81 Function in Different Cellular Compartments †

    Journal: Molecular and Cellular Biology

    doi: 10.1128/MCB.26.4.1373-1385.2006

    CD81 associates with both the precursor and the mature CD19 glycoforms. 1C8/hCD81 cells were lysed in the indicated lysis buffer, immunoprecipitated (IP), and immunoblotted (IB) with the indicated MAbs. Lanes contain either 10 μl of cell lysates or immunoprecipitated molecules from 400 μl of lysate. (a) The anti-CD81 MAb coprecipitates both pCD19 and mCD19 under mild (Brij 97), but not harsh (NP-40) lysis conditions. The data represent two independent experiments. (b) Cell lysates of 1C8/hCD81 or 1C8/VI(TM2-C′) cells, immunoprecipitated with the indicated MAbs, were digested by either endo-H or endo-F, and CD19 molecules were immunoblotted. The anti-hCD81 MAb coprecipitates pCD19 molecules, which are sensitive to endo-H digestion and migrate similarly to the endo-F-deglycosylated CD19. IC, isotype control.
    Figure Legend Snippet: CD81 associates with both the precursor and the mature CD19 glycoforms. 1C8/hCD81 cells were lysed in the indicated lysis buffer, immunoprecipitated (IP), and immunoblotted (IB) with the indicated MAbs. Lanes contain either 10 μl of cell lysates or immunoprecipitated molecules from 400 μl of lysate. (a) The anti-CD81 MAb coprecipitates both pCD19 and mCD19 under mild (Brij 97), but not harsh (NP-40) lysis conditions. The data represent two independent experiments. (b) Cell lysates of 1C8/hCD81 or 1C8/VI(TM2-C′) cells, immunoprecipitated with the indicated MAbs, were digested by either endo-H or endo-F, and CD19 molecules were immunoblotted. The anti-hCD81 MAb coprecipitates pCD19 molecules, which are sensitive to endo-H digestion and migrate similarly to the endo-F-deglycosylated CD19. IC, isotype control.

    Techniques Used: Lysis, Immunoprecipitation

    Related Articles

    Centrifugation:

    Article Title: Effects of terminal galactose residues in mannose α1-6 arm of Fc-glycan on the effector functions of therapeutic monoclonal antibodies
    Article Snippet: .. For truncating Fc-N-glycans, anti-CD20 mAb was digested with immobilized Halo-tagged wild-type Endo S and Remove-iT Endo D (Cat. No. P0742S, New England Biolabs) at 37°C for 4 h. Immobilized Endo S was removed from the reaction mixture by centrifugation; subsequently, Endo D was removed using affinity chromatography using chitin resin (New England Biolabs). mAbs containing (±Fucα1-6)GlcNAcβ1-Asn groups were isolated on Ab-Capcher Mag beads (ProteNova, Kagawa, Japan). .. The isolated mAbs, as glycan acceptors, were mixed with oxazolinated glycans (G2-Oxa, G1a-Oxa, G1b-Oxa, or G0-Oxa), as glycan donors (donor/acceptor molar ratio, 100:1), and glycosynthase Endo F3 (D165Q) in 50 mM Tris-HCl buffer (pH 7.0) at 37°C for 1 h. The mAbs in the reaction mixture were isolated on Ab-Capcher ExTra beads (ProteNova).

    Affinity Chromatography:

    Article Title: Effects of terminal galactose residues in mannose α1-6 arm of Fc-glycan on the effector functions of therapeutic monoclonal antibodies
    Article Snippet: .. For truncating Fc-N-glycans, anti-CD20 mAb was digested with immobilized Halo-tagged wild-type Endo S and Remove-iT Endo D (Cat. No. P0742S, New England Biolabs) at 37°C for 4 h. Immobilized Endo S was removed from the reaction mixture by centrifugation; subsequently, Endo D was removed using affinity chromatography using chitin resin (New England Biolabs). mAbs containing (±Fucα1-6)GlcNAcβ1-Asn groups were isolated on Ab-Capcher Mag beads (ProteNova, Kagawa, Japan). .. The isolated mAbs, as glycan acceptors, were mixed with oxazolinated glycans (G2-Oxa, G1a-Oxa, G1b-Oxa, or G0-Oxa), as glycan donors (donor/acceptor molar ratio, 100:1), and glycosynthase Endo F3 (D165Q) in 50 mM Tris-HCl buffer (pH 7.0) at 37°C for 1 h. The mAbs in the reaction mixture were isolated on Ab-Capcher ExTra beads (ProteNova).

    Isolation:

    Article Title: Effects of terminal galactose residues in mannose α1-6 arm of Fc-glycan on the effector functions of therapeutic monoclonal antibodies
    Article Snippet: .. For truncating Fc-N-glycans, anti-CD20 mAb was digested with immobilized Halo-tagged wild-type Endo S and Remove-iT Endo D (Cat. No. P0742S, New England Biolabs) at 37°C for 4 h. Immobilized Endo S was removed from the reaction mixture by centrifugation; subsequently, Endo D was removed using affinity chromatography using chitin resin (New England Biolabs). mAbs containing (±Fucα1-6)GlcNAcβ1-Asn groups were isolated on Ab-Capcher Mag beads (ProteNova, Kagawa, Japan). .. The isolated mAbs, as glycan acceptors, were mixed with oxazolinated glycans (G2-Oxa, G1a-Oxa, G1b-Oxa, or G0-Oxa), as glycan donors (donor/acceptor molar ratio, 100:1), and glycosynthase Endo F3 (D165Q) in 50 mM Tris-HCl buffer (pH 7.0) at 37°C for 1 h. The mAbs in the reaction mixture were isolated on Ab-Capcher ExTra beads (ProteNova).

    Flow Cytometry:

    Article Title: Structural insights into cGAMP degradation by Ecto-nucleotide pyrophosphatase phosphodiesterase 1
    Article Snippet: .. The mixture was passed through a Ni-NTA column (Qiagen) to remove the His-tagged proteases, and then the flow-through fraction was mixed with Endo H glycosidase (NEB) at 20 °C overnight. .. The ENPP1-ΔSMB T238A protein was further purified using Mono Q (GE Healthcare) and HiLoad Superdex200 16/60 columns (GE Healthcare).

    Size-exclusion Chromatography:

    Article Title: The Antiviral Activity of the Cellular Glycoprotein LGALS3BP/90K Is Species Specific
    Article Snippet: .. In addition, human BTB was enzymatically deglycosylated using endoglycosidase D (New England Biolabs, Frankfurt, Germany) according to the manufacturer's instructions, followed by removal of the glycosidase and the cleaved sugar chains by SEC. .. Crystallization and structure determination.

    Incubation:

    Article Title: Effect of Hemagglutinin Glycosylation on Influenza Virus Susceptibility to Neuraminidase Inhibitors
    Article Snippet: .. The denatured proteins were then incubated with either endo H glycosidase (500 U; New England Biolabs, Beverly, MA) or PNGase F for 12 h. At the end of the digestions, the samples and the control incubations without enzyme were examined by 8% SDS-PAGE, followed by fluorography. .. Generation of viruses lacking NA activity was done by transfection of 293T cells cocultured with MDCK cells, essentially as described above.

    other:

    Article Title: Neurodegeneration-associated mutant TREM2 proteins abortively cycle between the ER and ER–Golgi intermediate compartment
    Article Snippet: Endoglycosidase digests Endo D, endo H, and PNGase F were obtained from NEB.

    SDS Page:

    Article Title: Effect of Hemagglutinin Glycosylation on Influenza Virus Susceptibility to Neuraminidase Inhibitors
    Article Snippet: .. The denatured proteins were then incubated with either endo H glycosidase (500 U; New England Biolabs, Beverly, MA) or PNGase F for 12 h. At the end of the digestions, the samples and the control incubations without enzyme were examined by 8% SDS-PAGE, followed by fluorography. .. Generation of viruses lacking NA activity was done by transfection of 293T cells cocultured with MDCK cells, essentially as described above.

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  • 92
    New England Biolabs endo d
    Mutant TREM2 gains access to a post-ER compartment in vivo. (A) Schematic illustrating the generation of a five-mannose-containing N -linked glycan by α-mannosidase-I in the ERGIC or cis -Golgi to produce a protein that is sensitive to cleavage by <t>endo</t> D. (B) CHO-Lec1 cells were cotransfected with either WT or Y38C HA-TREM2 plus Arf1 (T31N), Arf1 (Q71L), or empty vector. Cells were harvested 1 d after transfection and the lysates subjected to digest by endo D. WT TREM2 is sensitive to endo D, while mutant Y38C is normally insensitive. Expression of either Arf1 (T31N) or (Q71L) uncovers <t>endo</t> D sensitivity for TREM2 (Y38C). RPN I serves as a loading control. (C) The ER-resident protein RPN I remains insensitive to endo D under conditions that render TREM2 (Y38C) sensitive to endo D. RPN I cleavage by endo H is detectable under the same experimental conditions. Sec22B serves as a loading control.
    Endo D, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/endo d/product/New England Biolabs
    Average 92 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    endo d - by Bioz Stars, 2021-02
    92/100 stars
      Buy from Supplier

    Image Search Results


    Mutant TREM2 gains access to a post-ER compartment in vivo. (A) Schematic illustrating the generation of a five-mannose-containing N -linked glycan by α-mannosidase-I in the ERGIC or cis -Golgi to produce a protein that is sensitive to cleavage by endo D. (B) CHO-Lec1 cells were cotransfected with either WT or Y38C HA-TREM2 plus Arf1 (T31N), Arf1 (Q71L), or empty vector. Cells were harvested 1 d after transfection and the lysates subjected to digest by endo D. WT TREM2 is sensitive to endo D, while mutant Y38C is normally insensitive. Expression of either Arf1 (T31N) or (Q71L) uncovers endo D sensitivity for TREM2 (Y38C). RPN I serves as a loading control. (C) The ER-resident protein RPN I remains insensitive to endo D under conditions that render TREM2 (Y38C) sensitive to endo D. RPN I cleavage by endo H is detectable under the same experimental conditions. Sec22B serves as a loading control.

    Journal: Molecular Biology of the Cell

    Article Title: Neurodegeneration-associated mutant TREM2 proteins abortively cycle between the ER and ER–Golgi intermediate compartment

    doi: 10.1091/mbc.E17-06-0423

    Figure Lengend Snippet: Mutant TREM2 gains access to a post-ER compartment in vivo. (A) Schematic illustrating the generation of a five-mannose-containing N -linked glycan by α-mannosidase-I in the ERGIC or cis -Golgi to produce a protein that is sensitive to cleavage by endo D. (B) CHO-Lec1 cells were cotransfected with either WT or Y38C HA-TREM2 plus Arf1 (T31N), Arf1 (Q71L), or empty vector. Cells were harvested 1 d after transfection and the lysates subjected to digest by endo D. WT TREM2 is sensitive to endo D, while mutant Y38C is normally insensitive. Expression of either Arf1 (T31N) or (Q71L) uncovers endo D sensitivity for TREM2 (Y38C). RPN I serves as a loading control. (C) The ER-resident protein RPN I remains insensitive to endo D under conditions that render TREM2 (Y38C) sensitive to endo D. RPN I cleavage by endo H is detectable under the same experimental conditions. Sec22B serves as a loading control.

    Article Snippet: Endoglycosidase digests Endo D, endo H, and PNGase F were obtained from NEB.

    Techniques: Mutagenesis, In Vivo, Plasmid Preparation, Transfection, Expressing

    Deglycosylation analysis of NBCe1-A with various Asn substitutions in EL-3. A , plasma membranes of HEK 293 cells expressing various Asn substitutions in EL-3 were isolated, lysed in 2× SDS sample buffer with 2% β-ME, and resolved by 7.5% SDS-PAGE. A portion of the membrane pellet was lysed in Endo-F digestion buffer and incubated with Endo-F for 2 h at 37 °C following the manufacturer's protocol. Protein samples were then mixed with 2× SDS samples buffer with β-ME and processed as described above. B , membrane pellets containing either 9C − or NBCe1-A were lysed in the Endo-F or Endo-H digestion buffer and digested with Endo-F or Endo-H following the manufacturer's protocol. Each experiment was performed at least three times.

    Journal: The Journal of Biological Chemistry

    Article Title: Interplay between Disulfide Bonding and N-Glycosylation Defines SLC4 Na+-coupled Transporter Extracellular Topography *

    doi: 10.1074/jbc.M114.619320

    Figure Lengend Snippet: Deglycosylation analysis of NBCe1-A with various Asn substitutions in EL-3. A , plasma membranes of HEK 293 cells expressing various Asn substitutions in EL-3 were isolated, lysed in 2× SDS sample buffer with 2% β-ME, and resolved by 7.5% SDS-PAGE. A portion of the membrane pellet was lysed in Endo-F digestion buffer and incubated with Endo-F for 2 h at 37 °C following the manufacturer's protocol. Protein samples were then mixed with 2× SDS samples buffer with β-ME and processed as described above. B , membrane pellets containing either 9C − or NBCe1-A were lysed in the Endo-F or Endo-H digestion buffer and digested with Endo-F or Endo-H following the manufacturer's protocol. Each experiment was performed at least three times.

    Article Snippet: Endo-F (peptide- N -glycosidase F) and Endo-H were from New England Biolabs.

    Techniques: Expressing, Isolation, SDS Page, Incubation

    Agarose gel electropherogram of Endo V digestion. (A) Digestion of the PaP1 genomic DNA by Endo V or Eco RI. Endo V digestion of the PaP1 genomic DNA produced a smear band in the gel. (B) Digestion of the PaP3 genomic DNA by Endo V or EcoRI. The PaP3 genome had been successfully sequenced using the shotgun method before. Unlike the PaP1 genomic DNA, Endo V digestion of the PaP3 genomic DNA gave no smear band in the gel.

    Journal: BMC Genomics

    Article Title: Unlocking the mystery of the hard-to-sequence phage genome: PaP1 methylome and bacterial immunity

    doi: 10.1186/1471-2164-15-803

    Figure Lengend Snippet: Agarose gel electropherogram of Endo V digestion. (A) Digestion of the PaP1 genomic DNA by Endo V or Eco RI. Endo V digestion of the PaP1 genomic DNA produced a smear band in the gel. (B) Digestion of the PaP3 genomic DNA by Endo V or EcoRI. The PaP3 genome had been successfully sequenced using the shotgun method before. Unlike the PaP1 genomic DNA, Endo V digestion of the PaP3 genomic DNA gave no smear band in the gel.

    Article Snippet: The commercial Endo V, or the products of E. coli gene nfi , was purchased from New England Biolabs, Ipswich, MA, USA.

    Techniques: Agarose Gel Electrophoresis, Produced

    CD81 associates with both the precursor and the mature CD19 glycoforms. 1C8/hCD81 cells were lysed in the indicated lysis buffer, immunoprecipitated (IP), and immunoblotted (IB) with the indicated MAbs. Lanes contain either 10 μl of cell lysates or immunoprecipitated molecules from 400 μl of lysate. (a) The anti-CD81 MAb coprecipitates both pCD19 and mCD19 under mild (Brij 97), but not harsh (NP-40) lysis conditions. The data represent two independent experiments. (b) Cell lysates of 1C8/hCD81 or 1C8/VI(TM2-C′) cells, immunoprecipitated with the indicated MAbs, were digested by either endo-H or endo-F, and CD19 molecules were immunoblotted. The anti-hCD81 MAb coprecipitates pCD19 molecules, which are sensitive to endo-H digestion and migrate similarly to the endo-F-deglycosylated CD19. IC, isotype control.

    Journal: Molecular and Cellular Biology

    Article Title: Building of the Tetraspanin Web: Distinct Structural Domains of CD81 Function in Different Cellular Compartments †

    doi: 10.1128/MCB.26.4.1373-1385.2006

    Figure Lengend Snippet: CD81 associates with both the precursor and the mature CD19 glycoforms. 1C8/hCD81 cells were lysed in the indicated lysis buffer, immunoprecipitated (IP), and immunoblotted (IB) with the indicated MAbs. Lanes contain either 10 μl of cell lysates or immunoprecipitated molecules from 400 μl of lysate. (a) The anti-CD81 MAb coprecipitates both pCD19 and mCD19 under mild (Brij 97), but not harsh (NP-40) lysis conditions. The data represent two independent experiments. (b) Cell lysates of 1C8/hCD81 or 1C8/VI(TM2-C′) cells, immunoprecipitated with the indicated MAbs, were digested by either endo-H or endo-F, and CD19 molecules were immunoblotted. The anti-hCD81 MAb coprecipitates pCD19 molecules, which are sensitive to endo-H digestion and migrate similarly to the endo-F-deglycosylated CD19. IC, isotype control.

    Article Snippet: Endo-F digestion of total N -glycan chains was performed using the 704S kit (New England Biolabs, Beverly, MA), and endo-H cleavage of high-mannose structures was performed using the PO703S kit (New England Biolabs).

    Techniques: Lysis, Immunoprecipitation