neuraminidase  (New England Biolabs)


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    Name:
    O Glycosidase and Neuraminidase Bundle
    Description:
    O Glycosidase and Neuraminidase Bundle
    Catalog Number:
    E0540S
    Price:
    191
    Category:
    Glycosidases
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    Structured Review

    New England Biolabs neuraminidase
    O Glycosidase and Neuraminidase Bundle
    O Glycosidase and Neuraminidase Bundle
    https://www.bioz.com/result/neuraminidase/product/New England Biolabs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    neuraminidase - by Bioz Stars, 2021-07
    94/100 stars

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    SDS Page:

    Article Title: Exome sequencing and in vitro studies identified podocalyxin as a candidate gene for focal and segmental glomerulosclerosis
    Article Snippet: Total and biotinylated PODXL were detected by Western blot analysis as above. .. Deglycosylation Cell lysates were either mock treated or treated with peptide N-glycosidase F, neuraminidase, or O-glycosidase and neuraminidase (PNGase F; O-Glycosidase & Neuraminidase Bundle; New England Biolabs) as per the manufacturer’s recommendations, followed by SDS-PAGE and Western blot analysis. .. Deglycosylation Cell lysates were either mock treated or treated with peptide N -glycosidase F, neuraminidase, or O-glycosidase and neuraminidase (PNGase F; O-Glycosidase & Neuraminidase Bundle; New England Biolabs) as per the manufacturer’s recommendations, followed by SDS-PAGE and Western blot analysis.

    Article Title: FXYD5 Is an Essential Mediator of the Inflammatory Response during Lung Injury
    Article Snippet: Immunoblots were quantified by densitometry using Image J 1.46r (National Institutes of Health, Bethesda, MD). .. Where indicated, surface biotinylated proteins were treated with O-glycosidase and Neuraminidase Bundle according to the manufacturer’s instructions (New England Biolabs, Inc.) prior to loading on SDS-PAGE as we previously described ( ). .. Interferon α (IFN-α, Biolegend) and TNF-α (Biolegend) were added to A549 cells for up to 24 and 2 h, respectively, as described for LPS treatment.

    Western Blot:

    Article Title: Exome sequencing and in vitro studies identified podocalyxin as a candidate gene for focal and segmental glomerulosclerosis
    Article Snippet: Total and biotinylated PODXL were detected by Western blot analysis as above. .. Deglycosylation Cell lysates were either mock treated or treated with peptide N-glycosidase F, neuraminidase, or O-glycosidase and neuraminidase (PNGase F; O-Glycosidase & Neuraminidase Bundle; New England Biolabs) as per the manufacturer’s recommendations, followed by SDS-PAGE and Western blot analysis. .. Deglycosylation Cell lysates were either mock treated or treated with peptide N -glycosidase F, neuraminidase, or O-glycosidase and neuraminidase (PNGase F; O-Glycosidase & Neuraminidase Bundle; New England Biolabs) as per the manufacturer’s recommendations, followed by SDS-PAGE and Western blot analysis.

    Incubation:

    Article Title: The half-life of the bone-derived hormone osteocalcin is regulated through O-glycosylation in mice, but not in humans
    Article Snippet: In-vitro de-glycosylation assay was performed on 10 μg of bone homogenate. .. Briefly, proteins were denatured in denaturing buffer (0.5% SDS, 40 mM DTT) at 95°C for 5 min and incubated with 80000 units of O-glycosidase and 100 units of neuraminidases for 4 hr at 37 °C following the NEB kit protocol (E0540S; NEB). .. Samples were resolved on 15% Tris-tricine SDS-PAGE gel and blotted using anti-Cterm OCN goat antibody.

    Article Title: Loss of N-Acetylgalactosaminyltransferase-4 Orchestrates Oncogenic MicroRNA-9 in Hepatocellular Carcinoma *
    Article Snippet: Then the membrane was incubated with biotinylated VVA (Vector Laboratories) at 10 μg/ml for 30 min at room temperature and detected by VECTASTAIN ABC reagents (Vector Laboratories). .. For lectin pull-down, neuraminidase (New England Biolabs, Ipswich, MA) was used to remove sialic acid, and cell lysates were incubated with agarose-bound VVA (Vector Laboratories) at 4 °C for 4 h followed by washing with lysis buffer three times. .. Immunoprecipitation was conducted with an immunoprecipitation kit (Roche Applied Science) according to the manufacturer's instructions.

    Lysis:

    Article Title: Loss of N-Acetylgalactosaminyltransferase-4 Orchestrates Oncogenic MicroRNA-9 in Hepatocellular Carcinoma *
    Article Snippet: Then the membrane was incubated with biotinylated VVA (Vector Laboratories) at 10 μg/ml for 30 min at room temperature and detected by VECTASTAIN ABC reagents (Vector Laboratories). .. For lectin pull-down, neuraminidase (New England Biolabs, Ipswich, MA) was used to remove sialic acid, and cell lysates were incubated with agarose-bound VVA (Vector Laboratories) at 4 °C for 4 h followed by washing with lysis buffer three times. .. Immunoprecipitation was conducted with an immunoprecipitation kit (Roche Applied Science) according to the manufacturer's instructions.

    Expressing:

    Article Title: Endoglycan plays a role in axon guidance by modulating cell adhesion
    Article Snippet: .. Both commissural and motoneurons were tested for adhesive strength after HEK cells expressing Endoglycan were treated with O-glycosidase (8’000 U/ml) or α2–3,6,8 Neuraminidase (5 U/ml; NEB Cat# E0540S, kit with both enzymes) for 2 hr before commissural neurons or motoneurons were added ( ; ). .. Growth cone blasting assay Commissural neurons were dissected from the most dorsal region of spinal cords of HH25/26 embryos that were unilaterally electroporated in ovo at HH17-18 with a plasmid encoding mRFP under the β-actin promotor (30 ng/μl) or co-electroporated with a plasmid encoding the open-reading frame of Endoglycan under the β-actin promotor (300 ng/μl).

    other:

    Article Title: Analysis of N- and O-Glycosylation of Lysosomal Glycoproteins
    Article Snippet: Enzymes: Peptide- N -Glycosidase F (PNGase F) from Flavobacterium meningosepticum (New England BioLabs), endoglycosidase H (Endo H) from Streptomyces plicatus (Glyco-Prozyme Inc.), Jack bean α-Mannosidase (Sigma-Aldrich) and O -glycosidase & Neuraminidase Bundle (New England BioLabs).

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    New England Biolabs o glycosidase and neuraminidase bundle
    OCN is <t>O-glycosylated</t> in vitro <t>and</t> in vivo on serine 8. ( A ) Western blot analysis on the secretion medium (SM) of HEK293 (WT) and HEK293 lacking COSMC ( C1GALT1C1 -/-) transfected with mouse OCN-V5. ( B ) Western blot analysis on the SM of CHO and CHO-ldlD cells transfected with mouse OCN-V5. CHO-ldlD cells were treated or not with 0.1 mM Galactose (Gal) and/or 1 mM N-acetylgalactosamine (GalNAc). ( C ) Effect of N-acetylgalactosaminyltransferase (GalNAc-Ts) inhibition on mouse OCN O-glycosylation in osteoblasts. Western blot analysis on the SM and cell extract (CE) of primary osteoblasts transfected with mouse OCN-V5 and treated or not with 2 mM of GalNAc-bn. ( D ) OCN deglycosylation assay. Bone extracts of C57BL/6J mice were treated or not with <t>O-glycosidase</t> and <t>neuraminidase</t> for 4 hr at 37°C and analyzed by western blot using anti-C-termimal OCN antibody (Cterm OCN). β-actin was used as a loading control. Rec OCN: Non-glycosylated OCN produced in bacteria. ( E ) Structure of mouse pre-pro-OCN and amino acid sequence of mature mouse OCN. The serine ( S ) and threonine ( S ) residues are in red. ( F ) Western blot analysis on the SM and cell extract (CE) of primary osteoblasts transfected with OCN-V5 containing or not the indicated mutations. In the 6XST→6XA mutant, all six serine and threonine residues from OCN were mutated to alanine. ( G ) Western blot analysis on the SM and cell extract (CE) of primary osteoblasts transfected with OCN-V5 containing or not the indicated mutations. ( H ) Annotated HCD MS/MS spectrum of a modified form of OCN (HexNAc-Hex-NANA + 3 Gla + S-S) pulled down from the bone homogenate of C57BL/6J mice. The precursor m/z value is 1180.95003 (M+5H) +5 and mass accuracy with the annotated OCN modified form is 4.6 ppm. In C , F and G , GFP co-expressed from OCN-V5 expression vector, was used as a loading control. Original western blot image from Figure 1A . Original western blot image from Figure 1B . Original western blot image from Figure 1C . Original western blot image from Figure 1D . Original western blot image from Figure 1F . Original western blot image from Figure 1G . Raw proteomic data from Figure 1H .
    O Glycosidase And Neuraminidase Bundle, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/o glycosidase and neuraminidase bundle/product/New England Biolabs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    o glycosidase and neuraminidase bundle - by Bioz Stars, 2021-07
    94/100 stars
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    OCN is O-glycosylated in vitro and in vivo on serine 8. ( A ) Western blot analysis on the secretion medium (SM) of HEK293 (WT) and HEK293 lacking COSMC ( C1GALT1C1 -/-) transfected with mouse OCN-V5. ( B ) Western blot analysis on the SM of CHO and CHO-ldlD cells transfected with mouse OCN-V5. CHO-ldlD cells were treated or not with 0.1 mM Galactose (Gal) and/or 1 mM N-acetylgalactosamine (GalNAc). ( C ) Effect of N-acetylgalactosaminyltransferase (GalNAc-Ts) inhibition on mouse OCN O-glycosylation in osteoblasts. Western blot analysis on the SM and cell extract (CE) of primary osteoblasts transfected with mouse OCN-V5 and treated or not with 2 mM of GalNAc-bn. ( D ) OCN deglycosylation assay. Bone extracts of C57BL/6J mice were treated or not with O-glycosidase and neuraminidase for 4 hr at 37°C and analyzed by western blot using anti-C-termimal OCN antibody (Cterm OCN). β-actin was used as a loading control. Rec OCN: Non-glycosylated OCN produced in bacteria. ( E ) Structure of mouse pre-pro-OCN and amino acid sequence of mature mouse OCN. The serine ( S ) and threonine ( S ) residues are in red. ( F ) Western blot analysis on the SM and cell extract (CE) of primary osteoblasts transfected with OCN-V5 containing or not the indicated mutations. In the 6XST→6XA mutant, all six serine and threonine residues from OCN were mutated to alanine. ( G ) Western blot analysis on the SM and cell extract (CE) of primary osteoblasts transfected with OCN-V5 containing or not the indicated mutations. ( H ) Annotated HCD MS/MS spectrum of a modified form of OCN (HexNAc-Hex-NANA + 3 Gla + S-S) pulled down from the bone homogenate of C57BL/6J mice. The precursor m/z value is 1180.95003 (M+5H) +5 and mass accuracy with the annotated OCN modified form is 4.6 ppm. In C , F and G , GFP co-expressed from OCN-V5 expression vector, was used as a loading control. Original western blot image from Figure 1A . Original western blot image from Figure 1B . Original western blot image from Figure 1C . Original western blot image from Figure 1D . Original western blot image from Figure 1F . Original western blot image from Figure 1G . Raw proteomic data from Figure 1H .

    Journal: eLife

    Article Title: The half-life of the bone-derived hormone osteocalcin is regulated through O-glycosylation in mice, but not in humans

    doi: 10.7554/eLife.61174

    Figure Lengend Snippet: OCN is O-glycosylated in vitro and in vivo on serine 8. ( A ) Western blot analysis on the secretion medium (SM) of HEK293 (WT) and HEK293 lacking COSMC ( C1GALT1C1 -/-) transfected with mouse OCN-V5. ( B ) Western blot analysis on the SM of CHO and CHO-ldlD cells transfected with mouse OCN-V5. CHO-ldlD cells were treated or not with 0.1 mM Galactose (Gal) and/or 1 mM N-acetylgalactosamine (GalNAc). ( C ) Effect of N-acetylgalactosaminyltransferase (GalNAc-Ts) inhibition on mouse OCN O-glycosylation in osteoblasts. Western blot analysis on the SM and cell extract (CE) of primary osteoblasts transfected with mouse OCN-V5 and treated or not with 2 mM of GalNAc-bn. ( D ) OCN deglycosylation assay. Bone extracts of C57BL/6J mice were treated or not with O-glycosidase and neuraminidase for 4 hr at 37°C and analyzed by western blot using anti-C-termimal OCN antibody (Cterm OCN). β-actin was used as a loading control. Rec OCN: Non-glycosylated OCN produced in bacteria. ( E ) Structure of mouse pre-pro-OCN and amino acid sequence of mature mouse OCN. The serine ( S ) and threonine ( S ) residues are in red. ( F ) Western blot analysis on the SM and cell extract (CE) of primary osteoblasts transfected with OCN-V5 containing or not the indicated mutations. In the 6XST→6XA mutant, all six serine and threonine residues from OCN were mutated to alanine. ( G ) Western blot analysis on the SM and cell extract (CE) of primary osteoblasts transfected with OCN-V5 containing or not the indicated mutations. ( H ) Annotated HCD MS/MS spectrum of a modified form of OCN (HexNAc-Hex-NANA + 3 Gla + S-S) pulled down from the bone homogenate of C57BL/6J mice. The precursor m/z value is 1180.95003 (M+5H) +5 and mass accuracy with the annotated OCN modified form is 4.6 ppm. In C , F and G , GFP co-expressed from OCN-V5 expression vector, was used as a loading control. Original western blot image from Figure 1A . Original western blot image from Figure 1B . Original western blot image from Figure 1C . Original western blot image from Figure 1D . Original western blot image from Figure 1F . Original western blot image from Figure 1G . Raw proteomic data from Figure 1H .

    Article Snippet: Briefly, proteins were denatured in denaturing buffer (0.5% SDS, 40 mM DTT) at 95°C for 5 min and incubated with 80000 units of O-glycosidase and 100 units of neuraminidases for 4 hr at 37 °C following the NEB kit protocol (E0540S; NEB).

    Techniques: In Vitro, In Vivo, Western Blot, Transfection, Inhibition, Mouse Assay, Produced, Sequencing, Mutagenesis, Tandem Mass Spectroscopy, Modification, Expressing, Plasmid Preparation

    OCN is O-glycosylated in vitro and in vivo on serine 8. (A) Western blot analysis on the secretion media (SM) of HEK293 (WT) and HEK293 lacking COSMC (COSMC-/-) transfected with mouse OCN-V5. (B) Western blot analysis on the secretion media (SM) of CHO and CHO-ldlD cells transfected with mouse OCN-V5. CHO-ldlD cells were treated or not with 0.1 mM Galactose (Gal) and/or 1 mM N-acetylgalactosamine (GalNAc). (C) Effect of N-acetylgalactosaminyltransferase (GalNAc-Ts) inhibition on mouse OCN O-glycosylation in osteoblasts. Western blot analysis on the secretion media (SM) and cell extract (CE) of primary osteoblasts transfected with mouse OCN-V5 and treated or not with 2 mM of GalNAc-bn. (D) OCN deglycosylation assay. Bone extract of C57BL/6J mice were treated or not with O-glycosidase and neuraminidase for 4 hours at 37°C and analyzed by Western blot using anti-C-termimal OCN antibody (Cterm OCN). β-actin was used as a loading control. Rec OCN: Non-glycosylated OCN produced in bacteria. (E) Structure of mouse pre-pro-OCN and amino acid sequence of mature mouse OCN. The serine (S) and threonine (S) residues are in red. (F) Western blot analysis on the secretion media (SM) and cell extract (CE) of primary osteoblasts transfected with OCN-V5 containing or not the indicated mutations. In the 6XST→6XA mutant, all six serine and threonine residues from OCN were mutated to alanine. (G) Western blot analysis on the secretion media (SM) and cell extract (CE) of primary osteoblasts transfected with OCN-V5 containing or not the indicated mutations. (H) Annotated HCD MS/MS spectrum of a modified form of OCN (HexNAc-Hex-NANA + 3 Gla + S-S) pulled down from the bone homogenate of C57BL/6J mice. The precursor m/z value is 1180.95003 (M+5H) +5 and mass accuracy with the annotated OCN modified form is 4.6 ppm. In C, F and G , GFP co-expressed from OCN-V5 expression vector, was used as a loading control.

    Journal: bioRxiv

    Article Title: The half-life of the bone-derived hormone osteocalcin is regulated through O-glycosylation in mice, but not in humans

    doi: 10.1101/2020.07.16.206656

    Figure Lengend Snippet: OCN is O-glycosylated in vitro and in vivo on serine 8. (A) Western blot analysis on the secretion media (SM) of HEK293 (WT) and HEK293 lacking COSMC (COSMC-/-) transfected with mouse OCN-V5. (B) Western blot analysis on the secretion media (SM) of CHO and CHO-ldlD cells transfected with mouse OCN-V5. CHO-ldlD cells were treated or not with 0.1 mM Galactose (Gal) and/or 1 mM N-acetylgalactosamine (GalNAc). (C) Effect of N-acetylgalactosaminyltransferase (GalNAc-Ts) inhibition on mouse OCN O-glycosylation in osteoblasts. Western blot analysis on the secretion media (SM) and cell extract (CE) of primary osteoblasts transfected with mouse OCN-V5 and treated or not with 2 mM of GalNAc-bn. (D) OCN deglycosylation assay. Bone extract of C57BL/6J mice were treated or not with O-glycosidase and neuraminidase for 4 hours at 37°C and analyzed by Western blot using anti-C-termimal OCN antibody (Cterm OCN). β-actin was used as a loading control. Rec OCN: Non-glycosylated OCN produced in bacteria. (E) Structure of mouse pre-pro-OCN and amino acid sequence of mature mouse OCN. The serine (S) and threonine (S) residues are in red. (F) Western blot analysis on the secretion media (SM) and cell extract (CE) of primary osteoblasts transfected with OCN-V5 containing or not the indicated mutations. In the 6XST→6XA mutant, all six serine and threonine residues from OCN were mutated to alanine. (G) Western blot analysis on the secretion media (SM) and cell extract (CE) of primary osteoblasts transfected with OCN-V5 containing or not the indicated mutations. (H) Annotated HCD MS/MS spectrum of a modified form of OCN (HexNAc-Hex-NANA + 3 Gla + S-S) pulled down from the bone homogenate of C57BL/6J mice. The precursor m/z value is 1180.95003 (M+5H) +5 and mass accuracy with the annotated OCN modified form is 4.6 ppm. In C, F and G , GFP co-expressed from OCN-V5 expression vector, was used as a loading control.

    Article Snippet: Briefly, proteins were denatured in denaturing buffer (0.5% SDS, 40 mM DTT) at 95°C for 5 min and incubated with 80000 units of O-glycosidase and 100 units of neuraminidases for 4 hours at 37°C following the NEB kit protocol (E0540S; NEB).

    Techniques: In Vitro, In Vivo, Western Blot, Transfection, Inhibition, Mouse Assay, Produced, Sequencing, Mutagenesis, Tandem Mass Spectroscopy, Modification, Expressing, Plasmid Preparation

    OCN O-glycosylation by N-acetylgalactosaminyltransferase (GalNAc-Ts) is independent of its processing and γ-carboxylation. (A) Galnts expression in pre-osteoblasts (undifferentiated) and osteoblasts (differentiated) by quantitative PCR. Results are represented as copy number of Galnts normalized to Actb. (B) Western blot analysis of OCN in the secretion media (SM) of HEK293 cells deficient for specific GalNAc-Ts. OCN-V5 was transfected in parental, COSMC-/- (ΔCOSMC), or GALNTs deficient (Δ) HEK293 cells and analysed by Western blot using anti-V5 antibody. (C) Western blot analysis on the secretion media (SM) of osteoblasts transfected with mouse OCN-V5 and treated or not with 2 mM of GalNAc-bn, 50 μM warfarin or 50 μM Dec-RVKR-CMK (RVKR) (upper panel), and percentage of carboxylated OCN (Gla OCN) over total OCN measured by ELISA (lower panel). (D) Western blot analysis on the secretion media (SM) of osteoblasts transfected with mouse OCN-V5 containing or not the S8A mutation and treated with 50 μM Dec-RVKR-CMK (RVKR) (upper panel), and percentage of carboxylated OCN (Gla OCN) over total OCN measured by ELISA (lower panel). (E) Western blot analysis on the secretion media (SM) of osteoblasts transfected with mouse OCN-V5 containing or not the S8A mutation and treated with 50 μM warfarin (upper panel), and percentage of carboxylated OCN over total OCN measured by ELISA (lower panel). (F) Western blot analysis of OCN deglycosylation assay on bone extracts from Furin fl/fl and Furin Osb-/- mice. Bone extracts were treated or not with O-glycosidase and neuraminidase for 4 hours at 37°C and analyzed by Western blot using anti-C-termimal OCN antibody (Cterm OCN). ** p

    Journal: bioRxiv

    Article Title: The half-life of the bone-derived hormone osteocalcin is regulated through O-glycosylation in mice, but not in humans

    doi: 10.1101/2020.07.16.206656

    Figure Lengend Snippet: OCN O-glycosylation by N-acetylgalactosaminyltransferase (GalNAc-Ts) is independent of its processing and γ-carboxylation. (A) Galnts expression in pre-osteoblasts (undifferentiated) and osteoblasts (differentiated) by quantitative PCR. Results are represented as copy number of Galnts normalized to Actb. (B) Western blot analysis of OCN in the secretion media (SM) of HEK293 cells deficient for specific GalNAc-Ts. OCN-V5 was transfected in parental, COSMC-/- (ΔCOSMC), or GALNTs deficient (Δ) HEK293 cells and analysed by Western blot using anti-V5 antibody. (C) Western blot analysis on the secretion media (SM) of osteoblasts transfected with mouse OCN-V5 and treated or not with 2 mM of GalNAc-bn, 50 μM warfarin or 50 μM Dec-RVKR-CMK (RVKR) (upper panel), and percentage of carboxylated OCN (Gla OCN) over total OCN measured by ELISA (lower panel). (D) Western blot analysis on the secretion media (SM) of osteoblasts transfected with mouse OCN-V5 containing or not the S8A mutation and treated with 50 μM Dec-RVKR-CMK (RVKR) (upper panel), and percentage of carboxylated OCN (Gla OCN) over total OCN measured by ELISA (lower panel). (E) Western blot analysis on the secretion media (SM) of osteoblasts transfected with mouse OCN-V5 containing or not the S8A mutation and treated with 50 μM warfarin (upper panel), and percentage of carboxylated OCN over total OCN measured by ELISA (lower panel). (F) Western blot analysis of OCN deglycosylation assay on bone extracts from Furin fl/fl and Furin Osb-/- mice. Bone extracts were treated or not with O-glycosidase and neuraminidase for 4 hours at 37°C and analyzed by Western blot using anti-C-termimal OCN antibody (Cterm OCN). ** p

    Article Snippet: Briefly, proteins were denatured in denaturing buffer (0.5% SDS, 40 mM DTT) at 95°C for 5 min and incubated with 80000 units of O-glycosidase and 100 units of neuraminidases for 4 hours at 37°C following the NEB kit protocol (E0540S; NEB).

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Western Blot, Transfection, Enzyme-linked Immunosorbent Assay, Mutagenesis, Mouse Assay