p0704  (New England Biolabs)


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  • 99
    Name:
    PNGase F native
    Description:
    PNGase F native 75 000 units
    Catalog Number:
    p0704l
    Price:
    754
    Size:
    75 000 units
    Category:
    Glycosidases
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    Structured Review

    New England Biolabs p0704
    PNGase F native
    PNGase F native 75 000 units
    https://www.bioz.com/result/p0704/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p0704 - by Bioz Stars, 2020-07
    99/100 stars

    Related Products / Commonly Used Together

    pngase f
    deglycosylation

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    Related Articles

    Synthesized:

    Article Title: IRES-Mediated Translation of Membrane Proteins and Glycoproteins in Eukaryotic Cell-Free Systems
    Article Snippet: .. To confirm that the migration process of the bands above 21 kDa was due to glycosylation of the target protein, cell-free synthesized EPO was treated with PNGase F, an enzyme which removes N-linked glycans. .. After PNGase F treatment of EPO synthesized in the K562 cell extract, the upper bands were converted into a single band migrating at a lower apparent molecular mass, thus demonstrating the specific cleavage of sugar moieties that have been attached to the glycoprotein during cell-free protein synthesis.

    Purification:

    Article Title: Design of pH Sensitive Binding Proteins from the Hyperthermophilic Sso7d Scaffold
    Article Snippet: .. Western Blotting Analysis Purified forms of the four human IgG isotypes- hIgG1 , hIgG2 , hIgG3 and hIgG4 (Sigma Aldrich, St. Louis, MO), the composite hIgG (Equitech bio, Kerrville, TX), hIgG digested with PNGase F (NEB) and an undigested hIgG control were run on 8% SDS-PAGE gels using standard procedures. ..

    Produced:

    Article Title: Exposure of Trypanosoma brucei to an N-acetylglucosamine-Binding Lectin Induces VSG Switching and Glycosylation Defects Resulting in Reduced Infectivity
    Article Snippet: .. Treatment with Endo H produced a molecular mass shift only in the VSG of UDA15a, while PNGase F appears to release one or two N -glycans from UDA10a and UDA15a VSGs, respectively. .. Thus, UDA10a VSG has only one Endo H-resistant N -glycan while the sVSG purified from UDA15a has Endo H-resistant and Endo H-sensitive N -glycans ( ).

    Incubation:

    Article Title: Glycosylation of Candida albicans Cell Wall Proteins Is Critical for Induction of Innate Immune Responses and Apoptosis of Epithelial Cells
    Article Snippet: .. For protein deglycosylation, cell walls were incubated with 25 U PNGaseF (New England BioLabs) per 1 µg cell wall for 1 h at 37°C or with 1 volume 0.1 M NaOH for 6 h at room temperature through orbital shaking. .. Ethic Statement C57BL/6 wild-type mice were purchased from Charles River (Sulzfield, Germany), TLR2-deficient mice were a kind gift from C. Kirschning (Technical University Munich), TLR4-deficient and MyD88-deficient mice were kindly provided by Dr. S. Akira (Osaka University).

    other:

    Article Title: Solid Phase Extraction of N-linked Glycopeptides Using Hydrazide Tip
    Article Snippet: The tips were then washed extensively and glycopeptides were released with 1500 U PNGase F in 25 mM ammonium bicarbonate buffer for 1 h at RT.

    Migration:

    Article Title: IRES-Mediated Translation of Membrane Proteins and Glycoproteins in Eukaryotic Cell-Free Systems
    Article Snippet: .. To confirm that the migration process of the bands above 21 kDa was due to glycosylation of the target protein, cell-free synthesized EPO was treated with PNGase F, an enzyme which removes N-linked glycans. .. After PNGase F treatment of EPO synthesized in the K562 cell extract, the upper bands were converted into a single band migrating at a lower apparent molecular mass, thus demonstrating the specific cleavage of sugar moieties that have been attached to the glycoprotein during cell-free protein synthesis.

    Western Blot:

    Article Title: Design of pH Sensitive Binding Proteins from the Hyperthermophilic Sso7d Scaffold
    Article Snippet: .. Western Blotting Analysis Purified forms of the four human IgG isotypes- hIgG1 , hIgG2 , hIgG3 and hIgG4 (Sigma Aldrich, St. Louis, MO), the composite hIgG (Equitech bio, Kerrville, TX), hIgG digested with PNGase F (NEB) and an undigested hIgG control were run on 8% SDS-PAGE gels using standard procedures. ..

    Recombinant:

    Article Title: Cloning and functional characterization of a fructan 1-exohydrolase (1-FEH) in edible burdock (Arctium lappa L.)
    Article Snippet: .. To estimate molecular mass of polypeptide of recombinant protein, deglycosylated recombinant protein was prepared by PNGase F (NEB) as described in the protocol. .. Molecular cloning of 1-FEH from edible burdock From 1.0 g of edible burdock roots powder, which were ground in liquid nitrogen, total RNA was prepared using RNeasy Plant Mini Kit (Qiagen, USA).

    SDS Page:

    Article Title: Design of pH Sensitive Binding Proteins from the Hyperthermophilic Sso7d Scaffold
    Article Snippet: .. Western Blotting Analysis Purified forms of the four human IgG isotypes- hIgG1 , hIgG2 , hIgG3 and hIgG4 (Sigma Aldrich, St. Louis, MO), the composite hIgG (Equitech bio, Kerrville, TX), hIgG digested with PNGase F (NEB) and an undigested hIgG control were run on 8% SDS-PAGE gels using standard procedures. ..

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  • 99
    New England Biolabs pngase f
    Increased binding affinity to MUC16 is modulated by smaller Fc glycan structures (A) VRC01 (top), 2G12 (middle), and HIVIG (bottom) were digested with enzymes to produce G0, or aglycosylated Abs and binding affinity to MUC16 was determined by SPR. Raw SPR curves and bar graphs of K D values for indicated groups are shown. (B) RTX was digested with PNGaseF to produce aglycosylated Abs and binding affinity to MUC16 (top), protein A (middle) or FcγRIIIA (bottom) was determined by SPR. Raw SPR curves and bar graphs of K D values for indicated groups are shown. (C) N-glycans on MUC16 were removed by digestion with <t>PNGase</t> F and binding affinity of indicated Abs to digested MUC16 was determined by SPR. Raw SPR curves are shown.
    Pngase F, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 270 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 270 article reviews
    Price from $9.99 to $1999.99
    pngase f - by Bioz Stars, 2020-07
    99/100 stars
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    Increased binding affinity to MUC16 is modulated by smaller Fc glycan structures (A) VRC01 (top), 2G12 (middle), and HIVIG (bottom) were digested with enzymes to produce G0, or aglycosylated Abs and binding affinity to MUC16 was determined by SPR. Raw SPR curves and bar graphs of K D values for indicated groups are shown. (B) RTX was digested with PNGaseF to produce aglycosylated Abs and binding affinity to MUC16 (top), protein A (middle) or FcγRIIIA (bottom) was determined by SPR. Raw SPR curves and bar graphs of K D values for indicated groups are shown. (C) N-glycans on MUC16 were removed by digestion with PNGase F and binding affinity of indicated Abs to digested MUC16 was determined by SPR. Raw SPR curves are shown.

    Journal: Mucosal immunology

    Article Title: Enhanced binding of antibodies generated during chronic HIV infection to mucus component MUC16

    doi: 10.1038/mi.2016.8

    Figure Lengend Snippet: Increased binding affinity to MUC16 is modulated by smaller Fc glycan structures (A) VRC01 (top), 2G12 (middle), and HIVIG (bottom) were digested with enzymes to produce G0, or aglycosylated Abs and binding affinity to MUC16 was determined by SPR. Raw SPR curves and bar graphs of K D values for indicated groups are shown. (B) RTX was digested with PNGaseF to produce aglycosylated Abs and binding affinity to MUC16 (top), protein A (middle) or FcγRIIIA (bottom) was determined by SPR. Raw SPR curves and bar graphs of K D values for indicated groups are shown. (C) N-glycans on MUC16 were removed by digestion with PNGase F and binding affinity of indicated Abs to digested MUC16 was determined by SPR. Raw SPR curves are shown.

    Article Snippet: Glycans were digested with PNGase F (NEB), neuraminidase (NEB), and β1,4-galactosidase (EMD Millipore).

    Techniques: Binding Assay, SPR Assay

    Analysis of the VSG expressed in UDAa and UDAb resistant lines. A and B) VSG221 expression in parental and UDA-resistant parasites was monitored by immunofluorescence microscopy using a polyclonal antibody against VSG221. Nuclear and kinetoplast DNA was stained with DAPI. Bars, 10 μm. C and E) sVSG were purified from parental and resistant lines as described [ 29 , 30 ] and analyzed by SDS/PAGE and Coomassie blue staining. D and F) sVSG samples were digested with Endo H (that removes oligomannose N -linked glycans) or PNGase F (that removes all N -linked glycans), and the products of the reaction were subjected to SDS/PAGE and Coomassie blue staining.

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Exposure of Trypanosoma brucei to an N-acetylglucosamine-Binding Lectin Induces VSG Switching and Glycosylation Defects Resulting in Reduced Infectivity

    doi: 10.1371/journal.pntd.0003612

    Figure Lengend Snippet: Analysis of the VSG expressed in UDAa and UDAb resistant lines. A and B) VSG221 expression in parental and UDA-resistant parasites was monitored by immunofluorescence microscopy using a polyclonal antibody against VSG221. Nuclear and kinetoplast DNA was stained with DAPI. Bars, 10 μm. C and E) sVSG were purified from parental and resistant lines as described [ 29 , 30 ] and analyzed by SDS/PAGE and Coomassie blue staining. D and F) sVSG samples were digested with Endo H (that removes oligomannose N -linked glycans) or PNGase F (that removes all N -linked glycans), and the products of the reaction were subjected to SDS/PAGE and Coomassie blue staining.

    Article Snippet: Treatment with Endo H produced a molecular mass shift only in the VSG of UDA15a, while PNGase F appears to release one or two N -glycans from UDA10a and UDA15a VSGs, respectively.

    Techniques: Expressing, Immunofluorescence, Microscopy, Staining, Purification, SDS Page

    Biophysical characterization of hFc binding Sso7d mutants and western blotting analysis. ( A ) Size exclusion chromatography of Sso7d mutants purified by immobilized metal affinity chromatography (IMAC). The dashed box indicates elution peak for Sso7d mutants. Mutants were loaded on the column at a concentration of 2 m g/ml. Molecular weight estimates based on the retention time of Sso7d mutants in the column are consistent with the mutants being present in monomeric form. The other peak corresponds to a minor impurity with higher molar absorptivity than the Sso7d mutants (see   Figure S3 ; SDS-PAGE analysis of fractions corresponding to the other peak do not show any detectable protein). ( B ) Circular dichroism spectra for Sso7d-hFc, Sso7d-his-hFc and Sso7d-ev-hFc at pH 7.4 and pH 4.5. The spectra at both pH values is essentially the same confirming that there is no change in secondary structure when the pH is lowered from 7.4 to 4.5 ( C ) Sso7d-hFc recognizes all four hIgG isotypes as well as the deglycosylated form of hIgG, when used as a primary reagent for detection in western blotting analysis. Lane 1: hIgG 1 , lane 2: hIgG 2 , lane 3: hIgG 3 , lane 4: hIgG 4 , lane 5: hIgG digested with PNGase F, lane 6: undigested hIgG (control). Similar results were observed with Sso7d-his-hFc and Sso7d-ev-hFc (data not shown).

    Journal: PLoS ONE

    Article Title: Design of pH Sensitive Binding Proteins from the Hyperthermophilic Sso7d Scaffold

    doi: 10.1371/journal.pone.0048928

    Figure Lengend Snippet: Biophysical characterization of hFc binding Sso7d mutants and western blotting analysis. ( A ) Size exclusion chromatography of Sso7d mutants purified by immobilized metal affinity chromatography (IMAC). The dashed box indicates elution peak for Sso7d mutants. Mutants were loaded on the column at a concentration of 2 m g/ml. Molecular weight estimates based on the retention time of Sso7d mutants in the column are consistent with the mutants being present in monomeric form. The other peak corresponds to a minor impurity with higher molar absorptivity than the Sso7d mutants (see Figure S3 ; SDS-PAGE analysis of fractions corresponding to the other peak do not show any detectable protein). ( B ) Circular dichroism spectra for Sso7d-hFc, Sso7d-his-hFc and Sso7d-ev-hFc at pH 7.4 and pH 4.5. The spectra at both pH values is essentially the same confirming that there is no change in secondary structure when the pH is lowered from 7.4 to 4.5 ( C ) Sso7d-hFc recognizes all four hIgG isotypes as well as the deglycosylated form of hIgG, when used as a primary reagent for detection in western blotting analysis. Lane 1: hIgG 1 , lane 2: hIgG 2 , lane 3: hIgG 3 , lane 4: hIgG 4 , lane 5: hIgG digested with PNGase F, lane 6: undigested hIgG (control). Similar results were observed with Sso7d-his-hFc and Sso7d-ev-hFc (data not shown).

    Article Snippet: Western Blotting Analysis Purified forms of the four human IgG isotypes- hIgG1 , hIgG2 , hIgG3 and hIgG4 (Sigma Aldrich, St. Louis, MO), the composite hIgG (Equitech bio, Kerrville, TX), hIgG digested with PNGase F (NEB) and an undigested hIgG control were run on 8% SDS-PAGE gels using standard procedures.

    Techniques: Binding Assay, Western Blot, Size-exclusion Chromatography, Purification, Affinity Chromatography, Concentration Assay, Molecular Weight, SDS Page

    Epithelial cytokine induction is independent of TLR2, TLR4, dectin-1 and MR. Human epithelial cells (1×10 6 ) were pre-incubated with ( A ) 10 µg/ml anti-TLR2, anti-TLR4, anti-MR antibodies, laminarin (100 µg/ml) or S. cerevisiae mannan (40 µg/ml) 2 h before epithelial cells were stimulated with C. albicans walls (1×10 8 ) for 24 h. ( B ) Oral epithelial cells (3×10 5 ) isolated from wild-type and MyD88−/− mice were incubated for 24 h with isolated walls (3×10 7 ). ( C ) Human epithelial cells (1×10 6 ) were incubated with 5 µM cytochalasin D for 30 min prior stimulation with C. albicans walls (1×10 8 ) for 24 h ( D and E ) Cell wall mannoproteins were deproteinized by incubating C. albicans walls (1×10 8 ) with proteinase K or deglycosylated by PNGaseF digestion (cleaves N- glycosylation) or NaOH treatment (alkaline β-elimination reduces O -glycosylation). Human epithelial cells (1×10 6 ) were incubated for 24 h with isolated walls (as positive control) or proteinase K-, PNGaseF- and NaOH-treated walls. ( F and G ) Epithelial cells (1×10 6 ) were incubated for 24 h with cell walls (1×10 8 ) isolated from C. albicans wild type (SC5314), N- glycosylation ( och1Δ ), O -glycosylation ( mnt1Δ/mnt2Δ ), N−/O -glycosylation ( pmr1Δ ) mutant strains or non- pathogenic S. cerevisiae . Human GM-CSF and mouse MIP-2 were quantified by ELISA. TLR4 mRNA up regulation in epithelial cells was determined by quantitative RT-PCR. Data are given as relative mRNA expression compared to mRNA expression of PBS-treated control cells (control = 1.0). ( A–G ), n = 3 (± SEM ), * p

    Journal: PLoS ONE

    Article Title: Glycosylation of Candida albicans Cell Wall Proteins Is Critical for Induction of Innate Immune Responses and Apoptosis of Epithelial Cells

    doi: 10.1371/journal.pone.0050518

    Figure Lengend Snippet: Epithelial cytokine induction is independent of TLR2, TLR4, dectin-1 and MR. Human epithelial cells (1×10 6 ) were pre-incubated with ( A ) 10 µg/ml anti-TLR2, anti-TLR4, anti-MR antibodies, laminarin (100 µg/ml) or S. cerevisiae mannan (40 µg/ml) 2 h before epithelial cells were stimulated with C. albicans walls (1×10 8 ) for 24 h. ( B ) Oral epithelial cells (3×10 5 ) isolated from wild-type and MyD88−/− mice were incubated for 24 h with isolated walls (3×10 7 ). ( C ) Human epithelial cells (1×10 6 ) were incubated with 5 µM cytochalasin D for 30 min prior stimulation with C. albicans walls (1×10 8 ) for 24 h ( D and E ) Cell wall mannoproteins were deproteinized by incubating C. albicans walls (1×10 8 ) with proteinase K or deglycosylated by PNGaseF digestion (cleaves N- glycosylation) or NaOH treatment (alkaline β-elimination reduces O -glycosylation). Human epithelial cells (1×10 6 ) were incubated for 24 h with isolated walls (as positive control) or proteinase K-, PNGaseF- and NaOH-treated walls. ( F and G ) Epithelial cells (1×10 6 ) were incubated for 24 h with cell walls (1×10 8 ) isolated from C. albicans wild type (SC5314), N- glycosylation ( och1Δ ), O -glycosylation ( mnt1Δ/mnt2Δ ), N−/O -glycosylation ( pmr1Δ ) mutant strains or non- pathogenic S. cerevisiae . Human GM-CSF and mouse MIP-2 were quantified by ELISA. TLR4 mRNA up regulation in epithelial cells was determined by quantitative RT-PCR. Data are given as relative mRNA expression compared to mRNA expression of PBS-treated control cells (control = 1.0). ( A–G ), n = 3 (± SEM ), * p

    Article Snippet: For protein deglycosylation, cell walls were incubated with 25 U PNGaseF (New England BioLabs) per 1 µg cell wall for 1 h at 37°C or with 1 volume 0.1 M NaOH for 6 h at room temperature through orbital shaking.

    Techniques: Incubation, Isolation, Mouse Assay, Positive Control, Mutagenesis, Enzyme-linked Immunosorbent Assay, Quantitative RT-PCR, Expressing