wheat germ agglutinin swga  (Vector Laboratories)


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    Vector Laboratories wheat germ agglutinin swga
    (A) Schematic outline of mass spectrometry sample preparation and analysis strategies. Cortical neurons at 12-15 DIV were treated with DMSO (vehicle control) or Thiamet-G overnight to capture dynamic O-GlcNAc modification. O-GlcNAc-modified proteins were enriched from crude mitochondrial fractions <t>using</t> <t>succinylated</t> wheat germ agglutinin <t>(sWGA)</t> beads. Label-free quantitative mass spectrometry (LC-MS/MS) data was further analyzed to select proteins with ;: 2 peptides (Filter 1) and to identify mitochondrial proteins based on MitoCarta 3.0 and Mitominer databases (Filter 2). (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated mitochondrial proteins. Annotated proteins (blue dots) represent p<0.05 (FC, fold change). (C) Pathway enrichment analysis, and (D) sub-mitochondrial localization of identified mitochondrial proteins. (E) Illustration of mitochondrial O-GlcNAcome, colored by MitoPathway assignments from MitoCarta3.0. n=3 biological replicates. See also , Table S1 and S2.
    Wheat Germ Agglutinin Swga, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    wheat germ agglutinin swga - by Bioz Stars, 2024-05
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    1) Product Images from "Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity"

    Article Title: Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity

    Journal: bioRxiv

    doi: 10.1101/2023.01.11.523512

    (A) Schematic outline of mass spectrometry sample preparation and analysis strategies. Cortical neurons at 12-15 DIV were treated with DMSO (vehicle control) or Thiamet-G overnight to capture dynamic O-GlcNAc modification. O-GlcNAc-modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Label-free quantitative mass spectrometry (LC-MS/MS) data was further analyzed to select proteins with ;: 2 peptides (Filter 1) and to identify mitochondrial proteins based on MitoCarta 3.0 and Mitominer databases (Filter 2). (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated mitochondrial proteins. Annotated proteins (blue dots) represent p<0.05 (FC, fold change). (C) Pathway enrichment analysis, and (D) sub-mitochondrial localization of identified mitochondrial proteins. (E) Illustration of mitochondrial O-GlcNAcome, colored by MitoPathway assignments from MitoCarta3.0. n=3 biological replicates. See also , Table S1 and S2.
    Figure Legend Snippet: (A) Schematic outline of mass spectrometry sample preparation and analysis strategies. Cortical neurons at 12-15 DIV were treated with DMSO (vehicle control) or Thiamet-G overnight to capture dynamic O-GlcNAc modification. O-GlcNAc-modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Label-free quantitative mass spectrometry (LC-MS/MS) data was further analyzed to select proteins with ;: 2 peptides (Filter 1) and to identify mitochondrial proteins based on MitoCarta 3.0 and Mitominer databases (Filter 2). (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated mitochondrial proteins. Annotated proteins (blue dots) represent p<0.05 (FC, fold change). (C) Pathway enrichment analysis, and (D) sub-mitochondrial localization of identified mitochondrial proteins. (E) Illustration of mitochondrial O-GlcNAcome, colored by MitoPathway assignments from MitoCarta3.0. n=3 biological replicates. See also , Table S1 and S2.

    Techniques Used: Mass Spectrometry, Sample Prep, Modification, Liquid Chromatography with Mass Spectroscopy

    (A) The total sWGA-bound protein O-GlcNAcylation level changes evaluated by SDS gel electrophoresis and probed with anti-O-GlcNAc antibodies (RL2). Crude mitochondrial fractions isolated from cortical neurons at 12-15 DIV, treated with DMSO (vehicle control) or Thiamet-G overnight to augment O-GlcNAc modification. O-GlcNAc modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Free GlcNAc used as a control to validate the specificity of sWGA binding. Mitochondrial fractions (input) were analyzed by SDS gel electrophoresis and probed with anti-ATP5β, anti-Slc25a4/5 and anti-Suclg1 antibodies. and anti-tubulin (loading control) antibodies. (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated proteins. Annotated proteins (red dots) represent p<0.05 (FC, fold change). (C) Venn diagram analysis of identified proteins using mitochondrial databases (MitoCarta3.0 and IMPI) and O-GlcNAcome catalogue. (D) Subcellular localization of identified proteins. (E) STRING protein-protein interaction analysis of mitochondrial proteins with nodes colored by FC Thiamet-G / Control.
    Figure Legend Snippet: (A) The total sWGA-bound protein O-GlcNAcylation level changes evaluated by SDS gel electrophoresis and probed with anti-O-GlcNAc antibodies (RL2). Crude mitochondrial fractions isolated from cortical neurons at 12-15 DIV, treated with DMSO (vehicle control) or Thiamet-G overnight to augment O-GlcNAc modification. O-GlcNAc modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Free GlcNAc used as a control to validate the specificity of sWGA binding. Mitochondrial fractions (input) were analyzed by SDS gel electrophoresis and probed with anti-ATP5β, anti-Slc25a4/5 and anti-Suclg1 antibodies. and anti-tubulin (loading control) antibodies. (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated proteins. Annotated proteins (red dots) represent p<0.05 (FC, fold change). (C) Venn diagram analysis of identified proteins using mitochondrial databases (MitoCarta3.0 and IMPI) and O-GlcNAcome catalogue. (D) Subcellular localization of identified proteins. (E) STRING protein-protein interaction analysis of mitochondrial proteins with nodes colored by FC Thiamet-G / Control.

    Techniques Used: SDS-Gel, Electrophoresis, Isolation, Modification, Binding Assay

    wheat germ agglutinin swga  (Vector Laboratories)


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    Vector Laboratories wheat germ agglutinin swga
    (A) Schematic outline of mass spectrometry sample preparation and analysis strategies. Cortical neurons at 12-15 DIV were treated with DMSO (vehicle control) or Thiamet-G overnight to capture dynamic O-GlcNAc modification. O-GlcNAc-modified proteins were enriched from crude mitochondrial fractions <t>using</t> <t>succinylated</t> wheat germ agglutinin <t>(sWGA)</t> beads. Label-free quantitative mass spectrometry (LC-MS/MS) data was further analyzed to select proteins with ;: 2 peptides (Filter 1) and to identify mitochondrial proteins based on MitoCarta 3.0 and Mitominer databases (Filter 2). (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated mitochondrial proteins. Annotated proteins (blue dots) represent p<0.05 (FC, fold change). (C) Pathway enrichment analysis, and (D) sub-mitochondrial localization of identified mitochondrial proteins. (E) Illustration of mitochondrial O-GlcNAcome, colored by MitoPathway assignments from MitoCarta3.0. n=3 biological replicates. See also , Table S1 and S2.
    Wheat Germ Agglutinin Swga, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/wheat germ agglutinin swga/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    wheat germ agglutinin swga - by Bioz Stars, 2024-05
    93/100 stars

    Images

    1) Product Images from "Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity"

    Article Title: Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity

    Journal: bioRxiv

    doi: 10.1101/2023.01.11.523512

    (A) Schematic outline of mass spectrometry sample preparation and analysis strategies. Cortical neurons at 12-15 DIV were treated with DMSO (vehicle control) or Thiamet-G overnight to capture dynamic O-GlcNAc modification. O-GlcNAc-modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Label-free quantitative mass spectrometry (LC-MS/MS) data was further analyzed to select proteins with ;: 2 peptides (Filter 1) and to identify mitochondrial proteins based on MitoCarta 3.0 and Mitominer databases (Filter 2). (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated mitochondrial proteins. Annotated proteins (blue dots) represent p<0.05 (FC, fold change). (C) Pathway enrichment analysis, and (D) sub-mitochondrial localization of identified mitochondrial proteins. (E) Illustration of mitochondrial O-GlcNAcome, colored by MitoPathway assignments from MitoCarta3.0. n=3 biological replicates. See also , Table S1 and S2.
    Figure Legend Snippet: (A) Schematic outline of mass spectrometry sample preparation and analysis strategies. Cortical neurons at 12-15 DIV were treated with DMSO (vehicle control) or Thiamet-G overnight to capture dynamic O-GlcNAc modification. O-GlcNAc-modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Label-free quantitative mass spectrometry (LC-MS/MS) data was further analyzed to select proteins with ;: 2 peptides (Filter 1) and to identify mitochondrial proteins based on MitoCarta 3.0 and Mitominer databases (Filter 2). (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated mitochondrial proteins. Annotated proteins (blue dots) represent p<0.05 (FC, fold change). (C) Pathway enrichment analysis, and (D) sub-mitochondrial localization of identified mitochondrial proteins. (E) Illustration of mitochondrial O-GlcNAcome, colored by MitoPathway assignments from MitoCarta3.0. n=3 biological replicates. See also , Table S1 and S2.

    Techniques Used: Mass Spectrometry, Sample Prep, Modification, Liquid Chromatography with Mass Spectroscopy

    (A) The total sWGA-bound protein O-GlcNAcylation level changes evaluated by SDS gel electrophoresis and probed with anti-O-GlcNAc antibodies (RL2). Crude mitochondrial fractions isolated from cortical neurons at 12-15 DIV, treated with DMSO (vehicle control) or Thiamet-G overnight to augment O-GlcNAc modification. O-GlcNAc modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Free GlcNAc used as a control to validate the specificity of sWGA binding. Mitochondrial fractions (input) were analyzed by SDS gel electrophoresis and probed with anti-ATP5β, anti-Slc25a4/5 and anti-Suclg1 antibodies. and anti-tubulin (loading control) antibodies. (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated proteins. Annotated proteins (red dots) represent p<0.05 (FC, fold change). (C) Venn diagram analysis of identified proteins using mitochondrial databases (MitoCarta3.0 and IMPI) and O-GlcNAcome catalogue. (D) Subcellular localization of identified proteins. (E) STRING protein-protein interaction analysis of mitochondrial proteins with nodes colored by FC Thiamet-G / Control.
    Figure Legend Snippet: (A) The total sWGA-bound protein O-GlcNAcylation level changes evaluated by SDS gel electrophoresis and probed with anti-O-GlcNAc antibodies (RL2). Crude mitochondrial fractions isolated from cortical neurons at 12-15 DIV, treated with DMSO (vehicle control) or Thiamet-G overnight to augment O-GlcNAc modification. O-GlcNAc modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Free GlcNAc used as a control to validate the specificity of sWGA binding. Mitochondrial fractions (input) were analyzed by SDS gel electrophoresis and probed with anti-ATP5β, anti-Slc25a4/5 and anti-Suclg1 antibodies. and anti-tubulin (loading control) antibodies. (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated proteins. Annotated proteins (red dots) represent p<0.05 (FC, fold change). (C) Venn diagram analysis of identified proteins using mitochondrial databases (MitoCarta3.0 and IMPI) and O-GlcNAcome catalogue. (D) Subcellular localization of identified proteins. (E) STRING protein-protein interaction analysis of mitochondrial proteins with nodes colored by FC Thiamet-G / Control.

    Techniques Used: SDS-Gel, Electrophoresis, Isolation, Modification, Binding Assay

    wheat germ agglutinin wga agarose  (Vector Laboratories)


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    Vector Laboratories wheat germ agglutinin wga agarose
    Wheat Germ Agglutinin Wga Agarose, supplied by Vector Laboratories, 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/wheat germ agglutinin wga agarose/product/Vector Laboratories
    Average 94 stars, based on 1 article reviews
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    wga agarose  (Vector Laboratories)


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    Vector Laboratories wga agarose
    A) Western blot analysis of αDG core protein detection by rabbit aDGct supernatants. Monoclonal antibodies 5–2, 29–5, and 45–3 were tested on replicate Western blots of solubilized <t>murine</t> <t>skeletal</t> muscle. Lane 1 contains normal murine skeletal muscle (LC) and lane 2 contains skeletal muscle from a mouse with a tamoxifen-induced fukutin-deficient dystroglycanopathy (KO). Detection with antibody IIH6 shows glycosylated αDG for comparison. Molecular weight standards are indicated in kDa. B) Wheat germ agglutinin <t>(WGA)</t> purifications of LC and KO mouse brain and heart lysates were conducted and the elution fraction was analyzed by Western blot. Monoclonal antibody media supernatants 5–2, 29–5, and 45–3 were used to detect αDG core protein on replicate blots; detection with IIH6 was performed by reprobing stripped blots. Molecular weight standards are indicated in kDa.
    Wga Agarose, supplied by Vector Laboratories, 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/wga agarose/product/Vector Laboratories
    Average 94 stars, based on 1 article reviews
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    1) Product Images from "Development of Rabbit Monoclonal Antibodies for Detection of Alpha-Dystroglycan in Normal and Dystrophic Tissue"

    Article Title: Development of Rabbit Monoclonal Antibodies for Detection of Alpha-Dystroglycan in Normal and Dystrophic Tissue

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0097567

    A) Western blot analysis of αDG core protein detection by rabbit aDGct supernatants. Monoclonal antibodies 5–2, 29–5, and 45–3 were tested on replicate Western blots of solubilized murine skeletal muscle. Lane 1 contains normal murine skeletal muscle (LC) and lane 2 contains skeletal muscle from a mouse with a tamoxifen-induced fukutin-deficient dystroglycanopathy (KO). Detection with antibody IIH6 shows glycosylated αDG for comparison. Molecular weight standards are indicated in kDa. B) Wheat germ agglutinin (WGA) purifications of LC and KO mouse brain and heart lysates were conducted and the elution fraction was analyzed by Western blot. Monoclonal antibody media supernatants 5–2, 29–5, and 45–3 were used to detect αDG core protein on replicate blots; detection with IIH6 was performed by reprobing stripped blots. Molecular weight standards are indicated in kDa.
    Figure Legend Snippet: A) Western blot analysis of αDG core protein detection by rabbit aDGct supernatants. Monoclonal antibodies 5–2, 29–5, and 45–3 were tested on replicate Western blots of solubilized murine skeletal muscle. Lane 1 contains normal murine skeletal muscle (LC) and lane 2 contains skeletal muscle from a mouse with a tamoxifen-induced fukutin-deficient dystroglycanopathy (KO). Detection with antibody IIH6 shows glycosylated αDG for comparison. Molecular weight standards are indicated in kDa. B) Wheat germ agglutinin (WGA) purifications of LC and KO mouse brain and heart lysates were conducted and the elution fraction was analyzed by Western blot. Monoclonal antibody media supernatants 5–2, 29–5, and 45–3 were used to detect αDG core protein on replicate blots; detection with IIH6 was performed by reprobing stripped blots. Molecular weight standards are indicated in kDa.

    Techniques Used: Western Blot, Molecular Weight

    A) Immunoblotting of healthy (N) and BMD-affected (A) pig skeletal muscle homogenates was conducted with monoclonal antibodies 5–2, 29–5, and 45–3. IIH6 detection of glycosylated αDG (reprobe) is shown. Molecular weight standards are indicated in kDa. B) Quantification of signal intensity of αDG detection by Western blot. αDG bands were analyzed; the signal intensity for each sample was normalized to the average αDG expression of all controls on the same blot. The resulting relative αDG expression is plotted for each individual control and BMD-affected sample (with group mean and SEM). C) Immunoblotting of WGA-enriched protein eluted from 500 µg of skeletal muscle lysate from normal and BMD-affected pigs using monoclonal antibody media supernatants 5–2, 29–5, 45–3, and IIH6 on replicate blots. Four hundred micrograms of skeletal muscle lysate (mSkM) from a normal mouse was run along with the pig WGA elutions for comparison. D) Diaphragm muscle from healthy (normal) and BMD-affected pigs (BMD-affected) were stained with 45–3 and IIH6. 20X objective; 100 µm scale bar. E) Quantification of pig αDG in normal and BMD-affected muscle by immunofluorescence. The total number of αDG positive pixels summed from 4 representative images was normalized to the average of all normal images per antibody for each control and BMD-affected sample. Asterisks indicate statistical significance between normal and affected pairs; * P = 0.01–0.05, ** P = 0.001–0.01, *** P = 0.0001–0.001, **** P = <0.0001.
    Figure Legend Snippet: A) Immunoblotting of healthy (N) and BMD-affected (A) pig skeletal muscle homogenates was conducted with monoclonal antibodies 5–2, 29–5, and 45–3. IIH6 detection of glycosylated αDG (reprobe) is shown. Molecular weight standards are indicated in kDa. B) Quantification of signal intensity of αDG detection by Western blot. αDG bands were analyzed; the signal intensity for each sample was normalized to the average αDG expression of all controls on the same blot. The resulting relative αDG expression is plotted for each individual control and BMD-affected sample (with group mean and SEM). C) Immunoblotting of WGA-enriched protein eluted from 500 µg of skeletal muscle lysate from normal and BMD-affected pigs using monoclonal antibody media supernatants 5–2, 29–5, 45–3, and IIH6 on replicate blots. Four hundred micrograms of skeletal muscle lysate (mSkM) from a normal mouse was run along with the pig WGA elutions for comparison. D) Diaphragm muscle from healthy (normal) and BMD-affected pigs (BMD-affected) were stained with 45–3 and IIH6. 20X objective; 100 µm scale bar. E) Quantification of pig αDG in normal and BMD-affected muscle by immunofluorescence. The total number of αDG positive pixels summed from 4 representative images was normalized to the average of all normal images per antibody for each control and BMD-affected sample. Asterisks indicate statistical significance between normal and affected pairs; * P = 0.01–0.05, ** P = 0.001–0.01, *** P = 0.0001–0.001, **** P = <0.0001.

    Techniques Used: Western Blot, Molecular Weight, Expressing, Staining, Immunofluorescence

    agarose bound wheat germ agglutinin kit wga  (Vector Laboratories)


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    Vector Laboratories agarose bound wheat germ agglutinin kit wga
    (A–B) HEK293 cells were transfected with control or ULK1 plasmid for 48 h; (C–D) HUVECs were transfected with control or ULK1 siRNA for 48 h, then treated with NONOate (50 µM) for 4 h. The western blots are representative of three independent experiments. *represents p <0.05 vs control ( n = 3); NS, not significant vs si-ULK1 alone. OGT, O-GlcNAc transferase; <t>WGA,</t> wheat <t>germ</t> <t>agglutinin;</t> Si, siRNA.
    Agarose Bound Wheat Germ Agglutinin Kit Wga, supplied by Vector Laboratories, 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/agarose bound wheat germ agglutinin kit wga/product/Vector Laboratories
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    agarose bound wheat germ agglutinin kit wga - by Bioz Stars, 2024-05
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    Images

    1) Product Images from "Upregulation of Unc-51-Like Kinase 1 by Nitric Oxide Stabilizes SIRT1, Independent of Autophagy"

    Article Title: Upregulation of Unc-51-Like Kinase 1 by Nitric Oxide Stabilizes SIRT1, Independent of Autophagy

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0116165

    (A–B) HEK293 cells were transfected with control or ULK1 plasmid for 48 h; (C–D) HUVECs were transfected with control or ULK1 siRNA for 48 h, then treated with NONOate (50 µM) for 4 h. The western blots are representative of three independent experiments. *represents p <0.05 vs control ( n = 3); NS, not significant vs si-ULK1 alone. OGT, O-GlcNAc transferase; WGA, wheat germ agglutinin; Si, siRNA.
    Figure Legend Snippet: (A–B) HEK293 cells were transfected with control or ULK1 plasmid for 48 h; (C–D) HUVECs were transfected with control or ULK1 siRNA for 48 h, then treated with NONOate (50 µM) for 4 h. The western blots are representative of three independent experiments. *represents p <0.05 vs control ( n = 3); NS, not significant vs si-ULK1 alone. OGT, O-GlcNAc transferase; WGA, wheat germ agglutinin; Si, siRNA.

    Techniques Used: Transfection, Plasmid Preparation, Western Blot

    wga conjugated agarose beads  (Vector Laboratories)


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    Vector Laboratories wga conjugated agarose beads
    Wga Conjugated Agarose Beads, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    agarose bound wheat germ agglutinin kit wga  (Vector Laboratories)


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    Vector Laboratories agarose bound wheat germ agglutinin kit wga
    (A) HUVEC respectively treated with A23187, Bradykinin, and SNP presented increased O-GlcNAc modification of Rpt2 without altering total Rpt2 protein levels. (B) Overexpression of eNOS but not GFP upregulated Rpt2 O-GlcNAcylation without changing the levels of total Rpt2 protein. Rpt2 O-GlcNAcylation was detected with the <t>WGA</t> protocol. (C) Confirming Rpt2-GlcNAcylation by repeating experiments in (A) but using an O-GlcNAc antibody (CD110.6) to pull down <t>O-GlcNAcylated</t> <t>proteins.</t> (D) Confirming the effect of NO on Rpt2-GlcNAcylation by repeating experiments in (C) but with DETA-NONOate. The shown blots were representative of at least 3 independent experiments with similar results. * represent p<0.05 vs control (n = 3), otherwise, not significant. Ad-, Adenoviral overexpression; Ctrl, control; SNP, sodium nitroprusside; WGA, wheat germ agglutinin; GFP, green fluorescent protein; eNOS, endothelial nitric oxide synthase.
    Agarose Bound Wheat Germ Agglutinin Kit Wga, supplied by Vector Laboratories, 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/agarose bound wheat germ agglutinin kit wga/product/Vector Laboratories
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    agarose bound wheat germ agglutinin kit wga - by Bioz Stars, 2024-05
    94/100 stars

    Images

    1) Product Images from "Identification of Nitric Oxide as an Endogenous Inhibitor of 26S Proteasomes in Vascular Endothelial Cells"

    Article Title: Identification of Nitric Oxide as an Endogenous Inhibitor of 26S Proteasomes in Vascular Endothelial Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0098486

    (A) HUVEC respectively treated with A23187, Bradykinin, and SNP presented increased O-GlcNAc modification of Rpt2 without altering total Rpt2 protein levels. (B) Overexpression of eNOS but not GFP upregulated Rpt2 O-GlcNAcylation without changing the levels of total Rpt2 protein. Rpt2 O-GlcNAcylation was detected with the WGA protocol. (C) Confirming Rpt2-GlcNAcylation by repeating experiments in (A) but using an O-GlcNAc antibody (CD110.6) to pull down O-GlcNAcylated proteins. (D) Confirming the effect of NO on Rpt2-GlcNAcylation by repeating experiments in (C) but with DETA-NONOate. The shown blots were representative of at least 3 independent experiments with similar results. * represent p<0.05 vs control (n = 3), otherwise, not significant. Ad-, Adenoviral overexpression; Ctrl, control; SNP, sodium nitroprusside; WGA, wheat germ agglutinin; GFP, green fluorescent protein; eNOS, endothelial nitric oxide synthase.
    Figure Legend Snippet: (A) HUVEC respectively treated with A23187, Bradykinin, and SNP presented increased O-GlcNAc modification of Rpt2 without altering total Rpt2 protein levels. (B) Overexpression of eNOS but not GFP upregulated Rpt2 O-GlcNAcylation without changing the levels of total Rpt2 protein. Rpt2 O-GlcNAcylation was detected with the WGA protocol. (C) Confirming Rpt2-GlcNAcylation by repeating experiments in (A) but using an O-GlcNAc antibody (CD110.6) to pull down O-GlcNAcylated proteins. (D) Confirming the effect of NO on Rpt2-GlcNAcylation by repeating experiments in (C) but with DETA-NONOate. The shown blots were representative of at least 3 independent experiments with similar results. * represent p<0.05 vs control (n = 3), otherwise, not significant. Ad-, Adenoviral overexpression; Ctrl, control; SNP, sodium nitroprusside; WGA, wheat germ agglutinin; GFP, green fluorescent protein; eNOS, endothelial nitric oxide synthase.

    Techniques Used: Modification, Over Expression

    OGT siRNA knockdown abolished the proteasome reporter protein accumulation and Rpt2 O-GlcNAcylation induced by (A) SNP; (B) Bradykinin; and (C) A23187. Rpt2 O-GlcNAcylation was detected with the WGA protocol. The shown blots were representative of at least 3 independent experiments with similar results. OGT knockdown by siRNA restored 26S proteasome activity in cell treated with (D) SNP; (E) Bradykinin; and (F) A23187. 26S proteasome activity was quantified by measuring chymotrypsin-like activity in the cell lysates. * represent p<0.05 vs control (n = 3). An overlaid portion (less exposure) of each whole blot indicating Ub-GFP is presented. Ctrl, control (scrambled) siRNA; NS, not significant (v.s. control); OGT, O-GlcNAc transferase; SNP, sodium nitroprusside; Ub-GFP, ubiquitin-green fluorescent protein; WGA, wheat germ agglutinin.
    Figure Legend Snippet: OGT siRNA knockdown abolished the proteasome reporter protein accumulation and Rpt2 O-GlcNAcylation induced by (A) SNP; (B) Bradykinin; and (C) A23187. Rpt2 O-GlcNAcylation was detected with the WGA protocol. The shown blots were representative of at least 3 independent experiments with similar results. OGT knockdown by siRNA restored 26S proteasome activity in cell treated with (D) SNP; (E) Bradykinin; and (F) A23187. 26S proteasome activity was quantified by measuring chymotrypsin-like activity in the cell lysates. * represent p<0.05 vs control (n = 3). An overlaid portion (less exposure) of each whole blot indicating Ub-GFP is presented. Ctrl, control (scrambled) siRNA; NS, not significant (v.s. control); OGT, O-GlcNAc transferase; SNP, sodium nitroprusside; Ub-GFP, ubiquitin-green fluorescent protein; WGA, wheat germ agglutinin.

    Techniques Used: Activity Assay

    The Ub G76V -GFP-transfected HUVEC were treated with vehicle (medium) and glucosamine (5 mM) for indicated time up to 4h and followed by (A) quantifications of poly-Ub-GFP protein levels with an anti-GFP antibody and O-GlcNAc modification of Rpt2 with an anti-Rpt2 antibody (on WGA pull-down) in Western blot; (B) Western blotting of global O-GlcNAc modified proteins with an anti-O-GlcNAc antibody; (C) proteasomal chymotrypsin-like activity assay. (D) Overexpression of OGT not GFP increased both Rpt2 O-GlcNAcylation and the levels of reporter protein. (E) Chymotrypsin-like activity in GFP- and OGT-overexpressing cells. The blots shown were representative of 3 independent experiments with similar results. * represents p<0.05 vs the control (n = 3). An overlaid portion (less exposure) of each whole blot indicating Ub-GFP is presented. Ub-GFP, ubiquitin-green fluorescent protein; OGT, O-GlcNAc transferase; UDP-GlcNAc, Uridine diphosphate-GlcNAc; WGA, wheat germ agglutinin.
    Figure Legend Snippet: The Ub G76V -GFP-transfected HUVEC were treated with vehicle (medium) and glucosamine (5 mM) for indicated time up to 4h and followed by (A) quantifications of poly-Ub-GFP protein levels with an anti-GFP antibody and O-GlcNAc modification of Rpt2 with an anti-Rpt2 antibody (on WGA pull-down) in Western blot; (B) Western blotting of global O-GlcNAc modified proteins with an anti-O-GlcNAc antibody; (C) proteasomal chymotrypsin-like activity assay. (D) Overexpression of OGT not GFP increased both Rpt2 O-GlcNAcylation and the levels of reporter protein. (E) Chymotrypsin-like activity in GFP- and OGT-overexpressing cells. The blots shown were representative of 3 independent experiments with similar results. * represents p<0.05 vs the control (n = 3). An overlaid portion (less exposure) of each whole blot indicating Ub-GFP is presented. Ub-GFP, ubiquitin-green fluorescent protein; OGT, O-GlcNAc transferase; UDP-GlcNAc, Uridine diphosphate-GlcNAc; WGA, wheat germ agglutinin.

    Techniques Used: Transfection, Modification, Western Blot, Activity Assay, Over Expression

    (A) Ub G76V -GFP-expressing HUVEC were transfected either with control or OGA siRNA and cell lysates were subjected to Western blot to detect reporter protein levels and Rpt2 O-GlcNAcylation. (B) chymotrypsin-like activity in siRNA treated cells. (C) Adenoviral overexpression of OGA, not GFP, decreased both the levels of reporter protein and Rpt2 O-GlcNAcylation. (D) chymotrypsin-like activity in adenovirus infected cells. The blots shown were representative of 3 independent experiments with similar results. * represents p<0.05 vs the control (n = 3). An overlaid portion (less exposure) of each whole blot indicating Ub-GFP is presented. Ctrl, control (scrambled) siRNA; OGA, O-GlcNAcase; OGT, O-GlcNAc transferase; Ub-GFP, ubiquitin-green fluorescent protein; WGA, wheat germ agglutinin.
    Figure Legend Snippet: (A) Ub G76V -GFP-expressing HUVEC were transfected either with control or OGA siRNA and cell lysates were subjected to Western blot to detect reporter protein levels and Rpt2 O-GlcNAcylation. (B) chymotrypsin-like activity in siRNA treated cells. (C) Adenoviral overexpression of OGA, not GFP, decreased both the levels of reporter protein and Rpt2 O-GlcNAcylation. (D) chymotrypsin-like activity in adenovirus infected cells. The blots shown were representative of 3 independent experiments with similar results. * represents p<0.05 vs the control (n = 3). An overlaid portion (less exposure) of each whole blot indicating Ub-GFP is presented. Ctrl, control (scrambled) siRNA; OGA, O-GlcNAcase; OGT, O-GlcNAc transferase; Ub-GFP, ubiquitin-green fluorescent protein; WGA, wheat germ agglutinin.

    Techniques Used: Expressing, Transfection, Western Blot, Activity Assay, Over Expression, Infection

    Adenoviral overexpression of OGA abolished Rpt2 O-GlcNAcylation induced by (A) SNP; (B) Bradykinin; (C) A23187; and (D) overexpression of eNOS. Rpt2 O-GlcNAcylation was detected with the WGA protocol. The shown blots were representative of at least 3 independent experiments with similar results. Ad-, Adenoviral overexpression; eNOS, endothelial nitric oxide synthase; NS, not significant (v.s. control); OGA, O-GlcNAcase; SNP, sodium nitroprusside; WGA, wheat germ agglutinin.
    Figure Legend Snippet: Adenoviral overexpression of OGA abolished Rpt2 O-GlcNAcylation induced by (A) SNP; (B) Bradykinin; (C) A23187; and (D) overexpression of eNOS. Rpt2 O-GlcNAcylation was detected with the WGA protocol. The shown blots were representative of at least 3 independent experiments with similar results. Ad-, Adenoviral overexpression; eNOS, endothelial nitric oxide synthase; NS, not significant (v.s. control); OGA, O-GlcNAcase; SNP, sodium nitroprusside; WGA, wheat germ agglutinin.

    Techniques Used: Over Expression

    (A) Genotyping of wild type (C57BL/6J) mice, Ub G76V -GFP (eNSO wild type) mice, and Ub G76V -GFP mice lacking eNOS by PCR analysis. (B) Gender (male) and age (12 weeks) matched wild type mice, Ub G76V -GFP/eNOS +/+ mice, and Ub G76V -GFP/eNOS −/− mice (n = 5/group) were used. The 26S proteasome reporter protein poly-Ub-GFP was stained with a rabbit-derived anti-GFP antibody through Western blot. The eNOS protein of the aortic tissues was detectable in eNOS +/+ but not eNOS −/− mice. (C) Aortic tissues of the eNOS −/− vs WT mice exhibited a decrease in Rpt2 O-GlcNAcylation, without changing the protein levels total Rpt2 and β7. (D) The 26S proteasome activity (chymotrypsin-like activity) was significantly higher in eNOS −/− vs WT mouse aortic tissues. (E) Proposed mechanisms of 26S proteasome regulation by eNOS-derived NO in vascular endothelial cells. In vascular endothelial cells, the eNOS-derived NO, which has been known to be expressed constitutively at low basal levels, maintains basal functionality of the 26S proteasome. This was achieved through an OGT-dependent O-GlcNAc modification of proteasome, likely on Rpt2, a key subunit of the proteasome regulatory complex recognized for this type of modification and associated with 26S proteasome function. The supporting evidence was obtained through either genetic or pharmacologic approaches both in 26S proteasome reporter cell and mouse models. eNOS, endothelial nitric oxide synthase; OGT, O-GlcNAc transferase; SNP, sodium nitroprusside; WGA, wheat germ agglutinin; WT, wild type.
    Figure Legend Snippet: (A) Genotyping of wild type (C57BL/6J) mice, Ub G76V -GFP (eNSO wild type) mice, and Ub G76V -GFP mice lacking eNOS by PCR analysis. (B) Gender (male) and age (12 weeks) matched wild type mice, Ub G76V -GFP/eNOS +/+ mice, and Ub G76V -GFP/eNOS −/− mice (n = 5/group) were used. The 26S proteasome reporter protein poly-Ub-GFP was stained with a rabbit-derived anti-GFP antibody through Western blot. The eNOS protein of the aortic tissues was detectable in eNOS +/+ but not eNOS −/− mice. (C) Aortic tissues of the eNOS −/− vs WT mice exhibited a decrease in Rpt2 O-GlcNAcylation, without changing the protein levels total Rpt2 and β7. (D) The 26S proteasome activity (chymotrypsin-like activity) was significantly higher in eNOS −/− vs WT mouse aortic tissues. (E) Proposed mechanisms of 26S proteasome regulation by eNOS-derived NO in vascular endothelial cells. In vascular endothelial cells, the eNOS-derived NO, which has been known to be expressed constitutively at low basal levels, maintains basal functionality of the 26S proteasome. This was achieved through an OGT-dependent O-GlcNAc modification of proteasome, likely on Rpt2, a key subunit of the proteasome regulatory complex recognized for this type of modification and associated with 26S proteasome function. The supporting evidence was obtained through either genetic or pharmacologic approaches both in 26S proteasome reporter cell and mouse models. eNOS, endothelial nitric oxide synthase; OGT, O-GlcNAc transferase; SNP, sodium nitroprusside; WGA, wheat germ agglutinin; WT, wild type.

    Techniques Used: Staining, Derivative Assay, Western Blot, Activity Assay, Modification

    agarose bound wheat germ agglutinin  (Vector Laboratories)


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    Vector Laboratories agarose bound wheat germ agglutinin
    Agarose Bound Wheat Germ Agglutinin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    agarose bound wheat germ agglutinin  (Vector Laboratories)


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    Vector Laboratories agarose bound wheat germ agglutinin
    Agarose Bound Wheat Germ Agglutinin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    wheat germ agglutinin wga agarose  (Vector Laboratories)


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    Vector Laboratories wheat germ agglutinin wga agarose
    Wheat Germ Agglutinin Wga Agarose, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    wga beads  (Vector Laboratories)


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    Vector Laboratories wga beads
    Selective inhibition of PDGFRβ inhibits growth of LLC and B16/PDGF-BB tumors with paracrine PDGF-BB signaling. ( A , B ) Dose-response analysis of treatment with 1-NaPP1 (15, 30 and 45 mg/kg/day) ( A ) or imatinib (75, 150 and 250 mg/kg/day) ( B ) of mice with Lewis lung carcinoma cells grown subcutaneously. ( C , D ) Effect of 1-NaPP1 (30 mg/kg/day) and imatinib (150 mg/kg/day) on growth of LLC ( C ) and B16/PDGF-BB tumors ( D ) in ASKA mice for 10 days (n= as stated in the figure). *** p<0.001. ( E ) LLC tumor lysates from mice treated with vehicle, 1-NaPP1 (30 mg/kg) or imatinib (150 mg/kg) were prepared and incubated overnight with <t>WGA-beads.</t> Retained proteins were analyzed by immunoblotting (IB) using a pY857 PDGFRβ antibody. Representative immunoblots out of two independent experiments are shown.
    Wga Beads, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Specific targeting of PDGFRβ in the stroma inhibits growth and angiogenesis in tumors with high PDGF-BB expression"

    Article Title: Specific targeting of PDGFRβ in the stroma inhibits growth and angiogenesis in tumors with high PDGF-BB expression

    Journal: Theranostics

    doi: 10.7150/thno.37851

    Selective inhibition of PDGFRβ inhibits growth of LLC and B16/PDGF-BB tumors with paracrine PDGF-BB signaling. ( A , B ) Dose-response analysis of treatment with 1-NaPP1 (15, 30 and 45 mg/kg/day) ( A ) or imatinib (75, 150 and 250 mg/kg/day) ( B ) of mice with Lewis lung carcinoma cells grown subcutaneously. ( C , D ) Effect of 1-NaPP1 (30 mg/kg/day) and imatinib (150 mg/kg/day) on growth of LLC ( C ) and B16/PDGF-BB tumors ( D ) in ASKA mice for 10 days (n= as stated in the figure). *** p<0.001. ( E ) LLC tumor lysates from mice treated with vehicle, 1-NaPP1 (30 mg/kg) or imatinib (150 mg/kg) were prepared and incubated overnight with WGA-beads. Retained proteins were analyzed by immunoblotting (IB) using a pY857 PDGFRβ antibody. Representative immunoblots out of two independent experiments are shown.
    Figure Legend Snippet: Selective inhibition of PDGFRβ inhibits growth of LLC and B16/PDGF-BB tumors with paracrine PDGF-BB signaling. ( A , B ) Dose-response analysis of treatment with 1-NaPP1 (15, 30 and 45 mg/kg/day) ( A ) or imatinib (75, 150 and 250 mg/kg/day) ( B ) of mice with Lewis lung carcinoma cells grown subcutaneously. ( C , D ) Effect of 1-NaPP1 (30 mg/kg/day) and imatinib (150 mg/kg/day) on growth of LLC ( C ) and B16/PDGF-BB tumors ( D ) in ASKA mice for 10 days (n= as stated in the figure). *** p<0.001. ( E ) LLC tumor lysates from mice treated with vehicle, 1-NaPP1 (30 mg/kg) or imatinib (150 mg/kg) were prepared and incubated overnight with WGA-beads. Retained proteins were analyzed by immunoblotting (IB) using a pY857 PDGFRβ antibody. Representative immunoblots out of two independent experiments are shown.

    Techniques Used: Inhibition, Incubation, Western Blot

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    Vector Laboratories wheat germ agglutinin swga
    (A) Schematic outline of mass spectrometry sample preparation and analysis strategies. Cortical neurons at 12-15 DIV were treated with DMSO (vehicle control) or Thiamet-G overnight to capture dynamic O-GlcNAc modification. O-GlcNAc-modified proteins were enriched from crude mitochondrial fractions <t>using</t> <t>succinylated</t> wheat germ agglutinin <t>(sWGA)</t> beads. Label-free quantitative mass spectrometry (LC-MS/MS) data was further analyzed to select proteins with ;: 2 peptides (Filter 1) and to identify mitochondrial proteins based on MitoCarta 3.0 and Mitominer databases (Filter 2). (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated mitochondrial proteins. Annotated proteins (blue dots) represent p<0.05 (FC, fold change). (C) Pathway enrichment analysis, and (D) sub-mitochondrial localization of identified mitochondrial proteins. (E) Illustration of mitochondrial O-GlcNAcome, colored by MitoPathway assignments from MitoCarta3.0. n=3 biological replicates. See also , Table S1 and S2.
    Wheat Germ Agglutinin Swga, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories wheat germ agglutinin wga agarose
    (A) Schematic outline of mass spectrometry sample preparation and analysis strategies. Cortical neurons at 12-15 DIV were treated with DMSO (vehicle control) or Thiamet-G overnight to capture dynamic O-GlcNAc modification. O-GlcNAc-modified proteins were enriched from crude mitochondrial fractions <t>using</t> <t>succinylated</t> wheat germ agglutinin <t>(sWGA)</t> beads. Label-free quantitative mass spectrometry (LC-MS/MS) data was further analyzed to select proteins with ;: 2 peptides (Filter 1) and to identify mitochondrial proteins based on MitoCarta 3.0 and Mitominer databases (Filter 2). (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated mitochondrial proteins. Annotated proteins (blue dots) represent p<0.05 (FC, fold change). (C) Pathway enrichment analysis, and (D) sub-mitochondrial localization of identified mitochondrial proteins. (E) Illustration of mitochondrial O-GlcNAcome, colored by MitoPathway assignments from MitoCarta3.0. n=3 biological replicates. See also , Table S1 and S2.
    Wheat Germ Agglutinin Wga Agarose, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories wga agarose
    A) Western blot analysis of αDG core protein detection by rabbit aDGct supernatants. Monoclonal antibodies 5–2, 29–5, and 45–3 were tested on replicate Western blots of solubilized <t>murine</t> <t>skeletal</t> muscle. Lane 1 contains normal murine skeletal muscle (LC) and lane 2 contains skeletal muscle from a mouse with a tamoxifen-induced fukutin-deficient dystroglycanopathy (KO). Detection with antibody IIH6 shows glycosylated αDG for comparison. Molecular weight standards are indicated in kDa. B) Wheat germ agglutinin <t>(WGA)</t> purifications of LC and KO mouse brain and heart lysates were conducted and the elution fraction was analyzed by Western blot. Monoclonal antibody media supernatants 5–2, 29–5, and 45–3 were used to detect αDG core protein on replicate blots; detection with IIH6 was performed by reprobing stripped blots. Molecular weight standards are indicated in kDa.
    Wga Agarose, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Vector Laboratories agarose bound wheat germ agglutinin kit wga
    (A–B) HEK293 cells were transfected with control or ULK1 plasmid for 48 h; (C–D) HUVECs were transfected with control or ULK1 siRNA for 48 h, then treated with NONOate (50 µM) for 4 h. The western blots are representative of three independent experiments. *represents p <0.05 vs control ( n = 3); NS, not significant vs si-ULK1 alone. OGT, O-GlcNAc transferase; <t>WGA,</t> wheat <t>germ</t> <t>agglutinin;</t> Si, siRNA.
    Agarose Bound Wheat Germ Agglutinin Kit Wga, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories wga conjugated agarose beads
    (A–B) HEK293 cells were transfected with control or ULK1 plasmid for 48 h; (C–D) HUVECs were transfected with control or ULK1 siRNA for 48 h, then treated with NONOate (50 µM) for 4 h. The western blots are representative of three independent experiments. *represents p <0.05 vs control ( n = 3); NS, not significant vs si-ULK1 alone. OGT, O-GlcNAc transferase; <t>WGA,</t> wheat <t>germ</t> <t>agglutinin;</t> Si, siRNA.
    Wga Conjugated Agarose Beads, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories agarose bound wheat germ agglutinin
    (A–B) HEK293 cells were transfected with control or ULK1 plasmid for 48 h; (C–D) HUVECs were transfected with control or ULK1 siRNA for 48 h, then treated with NONOate (50 µM) for 4 h. The western blots are representative of three independent experiments. *represents p <0.05 vs control ( n = 3); NS, not significant vs si-ULK1 alone. OGT, O-GlcNAc transferase; <t>WGA,</t> wheat <t>germ</t> <t>agglutinin;</t> Si, siRNA.
    Agarose Bound Wheat Germ Agglutinin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories wga beads
    Selective inhibition of PDGFRβ inhibits growth of LLC and B16/PDGF-BB tumors with paracrine PDGF-BB signaling. ( A , B ) Dose-response analysis of treatment with 1-NaPP1 (15, 30 and 45 mg/kg/day) ( A ) or imatinib (75, 150 and 250 mg/kg/day) ( B ) of mice with Lewis lung carcinoma cells grown subcutaneously. ( C , D ) Effect of 1-NaPP1 (30 mg/kg/day) and imatinib (150 mg/kg/day) on growth of LLC ( C ) and B16/PDGF-BB tumors ( D ) in ASKA mice for 10 days (n= as stated in the figure). *** p<0.001. ( E ) LLC tumor lysates from mice treated with vehicle, 1-NaPP1 (30 mg/kg) or imatinib (150 mg/kg) were prepared and incubated overnight with <t>WGA-beads.</t> Retained proteins were analyzed by immunoblotting (IB) using a pY857 PDGFRβ antibody. Representative immunoblots out of two independent experiments are shown.
    Wga Beads, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    (A) Schematic outline of mass spectrometry sample preparation and analysis strategies. Cortical neurons at 12-15 DIV were treated with DMSO (vehicle control) or Thiamet-G overnight to capture dynamic O-GlcNAc modification. O-GlcNAc-modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Label-free quantitative mass spectrometry (LC-MS/MS) data was further analyzed to select proteins with ;: 2 peptides (Filter 1) and to identify mitochondrial proteins based on MitoCarta 3.0 and Mitominer databases (Filter 2). (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated mitochondrial proteins. Annotated proteins (blue dots) represent p<0.05 (FC, fold change). (C) Pathway enrichment analysis, and (D) sub-mitochondrial localization of identified mitochondrial proteins. (E) Illustration of mitochondrial O-GlcNAcome, colored by MitoPathway assignments from MitoCarta3.0. n=3 biological replicates. See also , Table S1 and S2.

    Journal: bioRxiv

    Article Title: Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity

    doi: 10.1101/2023.01.11.523512

    Figure Lengend Snippet: (A) Schematic outline of mass spectrometry sample preparation and analysis strategies. Cortical neurons at 12-15 DIV were treated with DMSO (vehicle control) or Thiamet-G overnight to capture dynamic O-GlcNAc modification. O-GlcNAc-modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Label-free quantitative mass spectrometry (LC-MS/MS) data was further analyzed to select proteins with ;: 2 peptides (Filter 1) and to identify mitochondrial proteins based on MitoCarta 3.0 and Mitominer databases (Filter 2). (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated mitochondrial proteins. Annotated proteins (blue dots) represent p<0.05 (FC, fold change). (C) Pathway enrichment analysis, and (D) sub-mitochondrial localization of identified mitochondrial proteins. (E) Illustration of mitochondrial O-GlcNAcome, colored by MitoPathway assignments from MitoCarta3.0. n=3 biological replicates. See also , Table S1 and S2.

    Article Snippet: 9 µg of succinylated Wheat Germ Agglutinin (sWGA)-bound agarose beads (Vector Laboratories, Burlingame, CA) and mitochondrial lysates were incubated for 12hr at 4 ºC for O-GlcNAcylated protein enrichment.

    Techniques: Mass Spectrometry, Sample Prep, Modification, Liquid Chromatography with Mass Spectroscopy

    (A) The total sWGA-bound protein O-GlcNAcylation level changes evaluated by SDS gel electrophoresis and probed with anti-O-GlcNAc antibodies (RL2). Crude mitochondrial fractions isolated from cortical neurons at 12-15 DIV, treated with DMSO (vehicle control) or Thiamet-G overnight to augment O-GlcNAc modification. O-GlcNAc modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Free GlcNAc used as a control to validate the specificity of sWGA binding. Mitochondrial fractions (input) were analyzed by SDS gel electrophoresis and probed with anti-ATP5β, anti-Slc25a4/5 and anti-Suclg1 antibodies. and anti-tubulin (loading control) antibodies. (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated proteins. Annotated proteins (red dots) represent p<0.05 (FC, fold change). (C) Venn diagram analysis of identified proteins using mitochondrial databases (MitoCarta3.0 and IMPI) and O-GlcNAcome catalogue. (D) Subcellular localization of identified proteins. (E) STRING protein-protein interaction analysis of mitochondrial proteins with nodes colored by FC Thiamet-G / Control.

    Journal: bioRxiv

    Article Title: Neuronal activity-driven O-GlcNAcylation promotes mitochondrial plasticity

    doi: 10.1101/2023.01.11.523512

    Figure Lengend Snippet: (A) The total sWGA-bound protein O-GlcNAcylation level changes evaluated by SDS gel electrophoresis and probed with anti-O-GlcNAc antibodies (RL2). Crude mitochondrial fractions isolated from cortical neurons at 12-15 DIV, treated with DMSO (vehicle control) or Thiamet-G overnight to augment O-GlcNAc modification. O-GlcNAc modified proteins were enriched from crude mitochondrial fractions using succinylated wheat germ agglutinin (sWGA) beads. Free GlcNAc used as a control to validate the specificity of sWGA binding. Mitochondrial fractions (input) were analyzed by SDS gel electrophoresis and probed with anti-ATP5β, anti-Slc25a4/5 and anti-Suclg1 antibodies. and anti-tubulin (loading control) antibodies. (B) Scatter plot analysis demonstrating the impact of Thiamet-G treatment on O-GlcNAcylated proteins. Annotated proteins (red dots) represent p<0.05 (FC, fold change). (C) Venn diagram analysis of identified proteins using mitochondrial databases (MitoCarta3.0 and IMPI) and O-GlcNAcome catalogue. (D) Subcellular localization of identified proteins. (E) STRING protein-protein interaction analysis of mitochondrial proteins with nodes colored by FC Thiamet-G / Control.

    Article Snippet: 9 µg of succinylated Wheat Germ Agglutinin (sWGA)-bound agarose beads (Vector Laboratories, Burlingame, CA) and mitochondrial lysates were incubated for 12hr at 4 ºC for O-GlcNAcylated protein enrichment.

    Techniques: SDS-Gel, Electrophoresis, Isolation, Modification, Binding Assay

    A) Western blot analysis of αDG core protein detection by rabbit aDGct supernatants. Monoclonal antibodies 5–2, 29–5, and 45–3 were tested on replicate Western blots of solubilized murine skeletal muscle. Lane 1 contains normal murine skeletal muscle (LC) and lane 2 contains skeletal muscle from a mouse with a tamoxifen-induced fukutin-deficient dystroglycanopathy (KO). Detection with antibody IIH6 shows glycosylated αDG for comparison. Molecular weight standards are indicated in kDa. B) Wheat germ agglutinin (WGA) purifications of LC and KO mouse brain and heart lysates were conducted and the elution fraction was analyzed by Western blot. Monoclonal antibody media supernatants 5–2, 29–5, and 45–3 were used to detect αDG core protein on replicate blots; detection with IIH6 was performed by reprobing stripped blots. Molecular weight standards are indicated in kDa.

    Journal: PLoS ONE

    Article Title: Development of Rabbit Monoclonal Antibodies for Detection of Alpha-Dystroglycan in Normal and Dystrophic Tissue

    doi: 10.1371/journal.pone.0097567

    Figure Lengend Snippet: A) Western blot analysis of αDG core protein detection by rabbit aDGct supernatants. Monoclonal antibodies 5–2, 29–5, and 45–3 were tested on replicate Western blots of solubilized murine skeletal muscle. Lane 1 contains normal murine skeletal muscle (LC) and lane 2 contains skeletal muscle from a mouse with a tamoxifen-induced fukutin-deficient dystroglycanopathy (KO). Detection with antibody IIH6 shows glycosylated αDG for comparison. Molecular weight standards are indicated in kDa. B) Wheat germ agglutinin (WGA) purifications of LC and KO mouse brain and heart lysates were conducted and the elution fraction was analyzed by Western blot. Monoclonal antibody media supernatants 5–2, 29–5, and 45–3 were used to detect αDG core protein on replicate blots; detection with IIH6 was performed by reprobing stripped blots. Molecular weight standards are indicated in kDa.

    Article Snippet: Mouse and pig solubilized supernatants and human skeletal muscle and heart lysates were incubated batch method with WGA-agarose (Vector Laboratories, Burlingame CA) overnight at 4°C using 500 µg (for all skeletal muscle and heart samples) or 1 mg (brains only) of starting sample per SDS-PAGE lane.

    Techniques: Western Blot, Molecular Weight

    A) Immunoblotting of healthy (N) and BMD-affected (A) pig skeletal muscle homogenates was conducted with monoclonal antibodies 5–2, 29–5, and 45–3. IIH6 detection of glycosylated αDG (reprobe) is shown. Molecular weight standards are indicated in kDa. B) Quantification of signal intensity of αDG detection by Western blot. αDG bands were analyzed; the signal intensity for each sample was normalized to the average αDG expression of all controls on the same blot. The resulting relative αDG expression is plotted for each individual control and BMD-affected sample (with group mean and SEM). C) Immunoblotting of WGA-enriched protein eluted from 500 µg of skeletal muscle lysate from normal and BMD-affected pigs using monoclonal antibody media supernatants 5–2, 29–5, 45–3, and IIH6 on replicate blots. Four hundred micrograms of skeletal muscle lysate (mSkM) from a normal mouse was run along with the pig WGA elutions for comparison. D) Diaphragm muscle from healthy (normal) and BMD-affected pigs (BMD-affected) were stained with 45–3 and IIH6. 20X objective; 100 µm scale bar. E) Quantification of pig αDG in normal and BMD-affected muscle by immunofluorescence. The total number of αDG positive pixels summed from 4 representative images was normalized to the average of all normal images per antibody for each control and BMD-affected sample. Asterisks indicate statistical significance between normal and affected pairs; * P = 0.01–0.05, ** P = 0.001–0.01, *** P = 0.0001–0.001, **** P = <0.0001.

    Journal: PLoS ONE

    Article Title: Development of Rabbit Monoclonal Antibodies for Detection of Alpha-Dystroglycan in Normal and Dystrophic Tissue

    doi: 10.1371/journal.pone.0097567

    Figure Lengend Snippet: A) Immunoblotting of healthy (N) and BMD-affected (A) pig skeletal muscle homogenates was conducted with monoclonal antibodies 5–2, 29–5, and 45–3. IIH6 detection of glycosylated αDG (reprobe) is shown. Molecular weight standards are indicated in kDa. B) Quantification of signal intensity of αDG detection by Western blot. αDG bands were analyzed; the signal intensity for each sample was normalized to the average αDG expression of all controls on the same blot. The resulting relative αDG expression is plotted for each individual control and BMD-affected sample (with group mean and SEM). C) Immunoblotting of WGA-enriched protein eluted from 500 µg of skeletal muscle lysate from normal and BMD-affected pigs using monoclonal antibody media supernatants 5–2, 29–5, 45–3, and IIH6 on replicate blots. Four hundred micrograms of skeletal muscle lysate (mSkM) from a normal mouse was run along with the pig WGA elutions for comparison. D) Diaphragm muscle from healthy (normal) and BMD-affected pigs (BMD-affected) were stained with 45–3 and IIH6. 20X objective; 100 µm scale bar. E) Quantification of pig αDG in normal and BMD-affected muscle by immunofluorescence. The total number of αDG positive pixels summed from 4 representative images was normalized to the average of all normal images per antibody for each control and BMD-affected sample. Asterisks indicate statistical significance between normal and affected pairs; * P = 0.01–0.05, ** P = 0.001–0.01, *** P = 0.0001–0.001, **** P = <0.0001.

    Article Snippet: Mouse and pig solubilized supernatants and human skeletal muscle and heart lysates were incubated batch method with WGA-agarose (Vector Laboratories, Burlingame CA) overnight at 4°C using 500 µg (for all skeletal muscle and heart samples) or 1 mg (brains only) of starting sample per SDS-PAGE lane.

    Techniques: Western Blot, Molecular Weight, Expressing, Staining, Immunofluorescence

    (A–B) HEK293 cells were transfected with control or ULK1 plasmid for 48 h; (C–D) HUVECs were transfected with control or ULK1 siRNA for 48 h, then treated with NONOate (50 µM) for 4 h. The western blots are representative of three independent experiments. *represents p <0.05 vs control ( n = 3); NS, not significant vs si-ULK1 alone. OGT, O-GlcNAc transferase; WGA, wheat germ agglutinin; Si, siRNA.

    Journal: PLoS ONE

    Article Title: Upregulation of Unc-51-Like Kinase 1 by Nitric Oxide Stabilizes SIRT1, Independent of Autophagy

    doi: 10.1371/journal.pone.0116165

    Figure Lengend Snippet: (A–B) HEK293 cells were transfected with control or ULK1 plasmid for 48 h; (C–D) HUVECs were transfected with control or ULK1 siRNA for 48 h, then treated with NONOate (50 µM) for 4 h. The western blots are representative of three independent experiments. *represents p <0.05 vs control ( n = 3); NS, not significant vs si-ULK1 alone. OGT, O-GlcNAc transferase; WGA, wheat germ agglutinin; Si, siRNA.

    Article Snippet: Agarose bound Wheat Germ Agglutinin Kit (WGA) was used to pull down proteins modified by O-linked GlcNAc according to instructions of the manufacturer, Vectorlabs (Burlingame, CA), and as described previously .

    Techniques: Transfection, Plasmid Preparation, Western Blot

    Selective inhibition of PDGFRβ inhibits growth of LLC and B16/PDGF-BB tumors with paracrine PDGF-BB signaling. ( A , B ) Dose-response analysis of treatment with 1-NaPP1 (15, 30 and 45 mg/kg/day) ( A ) or imatinib (75, 150 and 250 mg/kg/day) ( B ) of mice with Lewis lung carcinoma cells grown subcutaneously. ( C , D ) Effect of 1-NaPP1 (30 mg/kg/day) and imatinib (150 mg/kg/day) on growth of LLC ( C ) and B16/PDGF-BB tumors ( D ) in ASKA mice for 10 days (n= as stated in the figure). *** p<0.001. ( E ) LLC tumor lysates from mice treated with vehicle, 1-NaPP1 (30 mg/kg) or imatinib (150 mg/kg) were prepared and incubated overnight with WGA-beads. Retained proteins were analyzed by immunoblotting (IB) using a pY857 PDGFRβ antibody. Representative immunoblots out of two independent experiments are shown.

    Journal: Theranostics

    Article Title: Specific targeting of PDGFRβ in the stroma inhibits growth and angiogenesis in tumors with high PDGF-BB expression

    doi: 10.7150/thno.37851

    Figure Lengend Snippet: Selective inhibition of PDGFRβ inhibits growth of LLC and B16/PDGF-BB tumors with paracrine PDGF-BB signaling. ( A , B ) Dose-response analysis of treatment with 1-NaPP1 (15, 30 and 45 mg/kg/day) ( A ) or imatinib (75, 150 and 250 mg/kg/day) ( B ) of mice with Lewis lung carcinoma cells grown subcutaneously. ( C , D ) Effect of 1-NaPP1 (30 mg/kg/day) and imatinib (150 mg/kg/day) on growth of LLC ( C ) and B16/PDGF-BB tumors ( D ) in ASKA mice for 10 days (n= as stated in the figure). *** p<0.001. ( E ) LLC tumor lysates from mice treated with vehicle, 1-NaPP1 (30 mg/kg) or imatinib (150 mg/kg) were prepared and incubated overnight with WGA-beads. Retained proteins were analyzed by immunoblotting (IB) using a pY857 PDGFRβ antibody. Representative immunoblots out of two independent experiments are shown.

    Article Snippet: Incubation with agarose bound WGA beads (Vector Laboratories) was performed overnight, followed by three washing steps with lysis buffer.

    Techniques: Inhibition, Incubation, Western Blot