p0704  (New England Biolabs)


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    Name:
    PNGase F native
    Description:
    PNGase F native 75 000 units
    Catalog Number:
    p0704l
    Price:
    754
    Category:
    Glycosidases
    Size:
    75 000 units
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    New England Biolabs p0704
    PNGase F native
    PNGase F native 75 000 units
    https://www.bioz.com/result/p0704/product/New England Biolabs
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p0704 - by Bioz Stars, 2021-03
    98/100 stars

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    Related Articles

    Centrifugation:

    Article Title: Lectin microarray and mass spectrometric analysis of hepatitis C proteins reveals N-linked glycosylation
    Article Snippet: The ultrafiltration retentate was digested with sequencing-grade trypsin (Promega, Madison, WI) overnight at 37°C. .. The resulting polypeptides were collected by centrifugation and further digested with PNGase F (New England BioLabs, Ipswich, MA) overnight at 37°C. .. The envelope protein of purified HCVcc was digested with glycosidase as described in the Supplementary Materials and Methods sections.

    other:

    Article Title: Organelle-specific Subunit Interactions of the Vertebrate Two-pore Channel Family *
    Article Snippet: Strikingly, although the ∼85-kDa band in the mCherry-hTPC2 pulldown sample was reduced in size by treatment with PNGase F, indicating glycosylation of HA-hTPC2, those in the mCherry-hTPC1, rTPC3, and cTPC3 pulldown samples were largely unaffected ( B , right panel ).

    Incubation:

    Article Title: Biochemical properties of thyroid peroxidase (TPO) expressed in human breast and mammary-derived cell lines
    Article Snippet: .. Finally, the reaction mixture was supplemented with PNGase F (New England Biolabs, Hitchin, UK) and incubated at 37°C for 16 hours. .. Control reactions were performed without PNGase F using the same assay conditions.

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    New England Biolabs pngase f
    MALDI mass spectra of the glycans released from chicken ovalbumin. After <t>PNGase</t> F treatment of chicken ovalbumin, the released oligosaccharides were passed through the microcon YM-10 columns and analyzed by MALDI mass spectrometry. Only the peaks of interest
    Pngase F, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pngase f/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pngase f - by Bioz Stars, 2021-03
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    MALDI mass spectra of the glycans released from chicken ovalbumin. After PNGase F treatment of chicken ovalbumin, the released oligosaccharides were passed through the microcon YM-10 columns and analyzed by MALDI mass spectrometry. Only the peaks of interest

    Journal:

    Article Title: Direct Identification of Nonreducing GlcNAc Residues on N-Glycans of Glycoproteins Using a Novel Chemoenzymatic Method

    doi: 10.1021/bc060341n

    Figure Lengend Snippet: MALDI mass spectra of the glycans released from chicken ovalbumin. After PNGase F treatment of chicken ovalbumin, the released oligosaccharides were passed through the microcon YM-10 columns and analyzed by MALDI mass spectrometry. Only the peaks of interest

    Article Snippet: The samples were then digested for 18 h at 37 °C with 2500 units of PNGase F (NEB) in 50 mM sodium phosphate buffer.

    Techniques: Mass Spectrometry

    Coupling to IgG via N-glycan chains. Selective labeling of the asialo-IgG1 molecule confirmed by PNGase F treatment. (A) Schematic diagram of an IgG molecule with the N-glycan structures attached at the Fc region. (B) The C2 keto galactose moiety was

    Journal:

    Article Title: Direct Identification of Nonreducing GlcNAc Residues on N-Glycans of Glycoproteins Using a Novel Chemoenzymatic Method

    doi: 10.1021/bc060341n

    Figure Lengend Snippet: Coupling to IgG via N-glycan chains. Selective labeling of the asialo-IgG1 molecule confirmed by PNGase F treatment. (A) Schematic diagram of an IgG molecule with the N-glycan structures attached at the Fc region. (B) The C2 keto galactose moiety was

    Article Snippet: The samples were then digested for 18 h at 37 °C with 2500 units of PNGase F (NEB) in 50 mM sodium phosphate buffer.

    Techniques: Labeling

    The biochemical properties of TPO protein expressed in breast tissues (A and B) and breast-derived cell lines (C).  (A) N-linked glycan content in TPO expressed in breast tissues. Total cell extract was digested with PNGase F, then subjected to 8% SDS-PAGE, followed by Western blotting, and probing with TPO-specific mAb 47 monoclonal antibody. Controls were processed under the same conditions as the samples except that no enzyme was added. One representative immunoblot out of at least three independent experiments is shown. (B) Enzymatic activity of TPO expressed in breast tissues. Tissue lysate was incubated with TPO-specific mAb A4, then protein A agarose was added to precipitate immune complexes. TPO-antibody complexes bound to agarose were incubated with luminol in the presence of hydrogen peroxide. The intensity of luminescencent signal was measured and results were expressed as relative light units (RLU). As positive control, TPO immunoprecipitated from human thyroid tissue lysate (Graves’ disease case) was used to measure luminol oxidation. Agarose A incubated with mAb A4 alone (lysate omitted) was used as negative control. One representative of three independent experiments is shown. (C) TPO protein expression in breast epithelial normal (184A1) and cancer cell lines (MCF-7 and MDA-MB-231). Western blotting was used to detect TPO protein presence. The specificity of the reaction was verified by preabsorption of ab76935 antibody with the excess of highly purified human TPO. NTHY was used as a positive control. β-actin-specific Ab was used as a loading control. BN: peri-tumoral breast tissue; BC: breast cancer tissue; G-B: Graves’ disease thyroid tissue; NTHY: NTHY-ori 3–1 cell line; PNGase F: Peptide-N-Glycosidase F; RLU: relative light units.

    Journal: PLoS ONE

    Article Title: Biochemical properties of thyroid peroxidase (TPO) expressed in human breast and mammary-derived cell lines

    doi: 10.1371/journal.pone.0193624

    Figure Lengend Snippet: The biochemical properties of TPO protein expressed in breast tissues (A and B) and breast-derived cell lines (C). (A) N-linked glycan content in TPO expressed in breast tissues. Total cell extract was digested with PNGase F, then subjected to 8% SDS-PAGE, followed by Western blotting, and probing with TPO-specific mAb 47 monoclonal antibody. Controls were processed under the same conditions as the samples except that no enzyme was added. One representative immunoblot out of at least three independent experiments is shown. (B) Enzymatic activity of TPO expressed in breast tissues. Tissue lysate was incubated with TPO-specific mAb A4, then protein A agarose was added to precipitate immune complexes. TPO-antibody complexes bound to agarose were incubated with luminol in the presence of hydrogen peroxide. The intensity of luminescencent signal was measured and results were expressed as relative light units (RLU). As positive control, TPO immunoprecipitated from human thyroid tissue lysate (Graves’ disease case) was used to measure luminol oxidation. Agarose A incubated with mAb A4 alone (lysate omitted) was used as negative control. One representative of three independent experiments is shown. (C) TPO protein expression in breast epithelial normal (184A1) and cancer cell lines (MCF-7 and MDA-MB-231). Western blotting was used to detect TPO protein presence. The specificity of the reaction was verified by preabsorption of ab76935 antibody with the excess of highly purified human TPO. NTHY was used as a positive control. β-actin-specific Ab was used as a loading control. BN: peri-tumoral breast tissue; BC: breast cancer tissue; G-B: Graves’ disease thyroid tissue; NTHY: NTHY-ori 3–1 cell line; PNGase F: Peptide-N-Glycosidase F; RLU: relative light units.

    Article Snippet: Finally, the reaction mixture was supplemented with PNGase F (New England Biolabs, Hitchin, UK) and incubated at 37°C for 16 hours.

    Techniques: Derivative Assay, SDS Page, Western Blot, Activity Assay, Incubation, Positive Control, Immunoprecipitation, Negative Control, Expressing, Multiple Displacement Amplification, Purification

    3.4. Analysis of glycans released from HCVcc by PNGase F

    Journal: Medicine

    Article Title: Lectin microarray and mass spectrometric analysis of hepatitis C proteins reveals N-linked glycosylation

    doi: 10.1097/MD.0000000000010208

    Figure Lengend Snippet: 3.4. Analysis of glycans released from HCVcc by PNGase F

    Article Snippet: The resulting polypeptides were collected by centrifugation and further digested with PNGase F (New England BioLabs, Ipswich, MA) overnight at 37°C.

    Techniques:

    TMEM258 Interacts with the OST Complex and Regulates Protein N-linked Glycosylation (A) TMEM258 interaction partners were identified in BV-2 cells (left) and BW5147 cells (right) expressing V5-tagged TMEM258. High-performance liquid chromatography-mass spectrometry was employed to detect proteins after immunoprecipitation with anti-V5 antibody. (B) Network analysis integrating TMEM258 interaction partners with the OST complex and ER stress response. (C) TMEM258 was knocked down in HeLa cells, and glycoproteins were detected by surface staining with FITC-labeled concanavalin A (ConA) followed by FACS. (D) Measurement of N-linked glycosylation on the prototypical glycoprotein basigen (BSG) was monitored by western blot. Where indicated, samples were deglycosylated with PNGaseF. Knockdown of TMEM258 in HeLa cells was verified by qPCR. shCtrl, control shRNA. Data represent mean and SD. .

    Journal: Cell reports

    Article Title: TMEM258 Is a Component of the Oligosaccharyltransferase Complex Controlling ER Stress and Intestinal Inflammation

    doi: 10.1016/j.celrep.2016.11.042

    Figure Lengend Snippet: TMEM258 Interacts with the OST Complex and Regulates Protein N-linked Glycosylation (A) TMEM258 interaction partners were identified in BV-2 cells (left) and BW5147 cells (right) expressing V5-tagged TMEM258. High-performance liquid chromatography-mass spectrometry was employed to detect proteins after immunoprecipitation with anti-V5 antibody. (B) Network analysis integrating TMEM258 interaction partners with the OST complex and ER stress response. (C) TMEM258 was knocked down in HeLa cells, and glycoproteins were detected by surface staining with FITC-labeled concanavalin A (ConA) followed by FACS. (D) Measurement of N-linked glycosylation on the prototypical glycoprotein basigen (BSG) was monitored by western blot. Where indicated, samples were deglycosylated with PNGaseF. Knockdown of TMEM258 in HeLa cells was verified by qPCR. shCtrl, control shRNA. Data represent mean and SD. .

    Article Snippet: Designated samples were deglycosylated with PNGaseF according to the manufacturer’s protocol (NEB).

    Techniques: Expressing, High Performance Liquid Chromatography, Mass Spectrometry, Immunoprecipitation, Staining, Labeling, FACS, Western Blot, Real-time Polymerase Chain Reaction, shRNA