streptavidin agarose resin beads  (Millipore)


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    Structured Review

    Millipore streptavidin agarose resin beads
    Streptavidin Agarose Resin Beads, supplied by Millipore, 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/streptavidin agarose resin beads/product/Millipore
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    streptavidin agarose resin beads - by Bioz Stars, 2020-04
    93/100 stars

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    Related Articles

    Centrifugation:

    Article Title: PARI Regulates Stalled Replication Fork Processing To Maintain Genome Stability upon Replication Stress in Mice
    Article Snippet: .. After centrifugation, protease inhibitor cocktail (Roche) was added to the supernatant, incubated with streptavidin-agarose resin beads (Novagen), and washed with PBS, followed by a high-stringency wash with 1 M NaCl and 0.5% SDS in 25 mM Tris-HCl, pH 8.0, solution. .. Then, the beads were eluted with standard SDS-PAGE loading buffer for 25 min at 95°C.

    Protease Inhibitor:

    Article Title: PARI Regulates Stalled Replication Fork Processing To Maintain Genome Stability upon Replication Stress in Mice
    Article Snippet: .. After centrifugation, protease inhibitor cocktail (Roche) was added to the supernatant, incubated with streptavidin-agarose resin beads (Novagen), and washed with PBS, followed by a high-stringency wash with 1 M NaCl and 0.5% SDS in 25 mM Tris-HCl, pH 8.0, solution. .. Then, the beads were eluted with standard SDS-PAGE loading buffer for 25 min at 95°C.

    Transfection:

    Article Title: PARI Regulates Stalled Replication Fork Processing To Maintain Genome Stability upon Replication Stress in Mice
    Article Snippet: Briefly, 1 × 108 293T cells were transiently transfected with the pCAG-FLAG-PARI plasmid and pulse-labeled with 20 μM EdU (Thermo Scientific) for 30 min. .. After centrifugation, protease inhibitor cocktail (Roche) was added to the supernatant, incubated with streptavidin-agarose resin beads (Novagen), and washed with PBS, followed by a high-stringency wash with 1 M NaCl and 0.5% SDS in 25 mM Tris-HCl, pH 8.0, solution.

    Incubation:

    Article Title: PARI Regulates Stalled Replication Fork Processing To Maintain Genome Stability upon Replication Stress in Mice
    Article Snippet: .. After centrifugation, protease inhibitor cocktail (Roche) was added to the supernatant, incubated with streptavidin-agarose resin beads (Novagen), and washed with PBS, followed by a high-stringency wash with 1 M NaCl and 0.5% SDS in 25 mM Tris-HCl, pH 8.0, solution. .. Then, the beads were eluted with standard SDS-PAGE loading buffer for 25 min at 95°C.

    Western Blot:

    Article Title: PARI Regulates Stalled Replication Fork Processing To Maintain Genome Stability upon Replication Stress in Mice
    Article Snippet: After centrifugation, protease inhibitor cocktail (Roche) was added to the supernatant, incubated with streptavidin-agarose resin beads (Novagen), and washed with PBS, followed by a high-stringency wash with 1 M NaCl and 0.5% SDS in 25 mM Tris-HCl, pH 8.0, solution. .. SDS-PAGE and Western blotting were carried out according to standard procedures using anti-FLAG polyclonal antibody (1:2,000; Sigma-Aldrich) and anti-PCNA monoclonal antibody (1:1,000; PC10; Biolegend).

    Sonication:

    Article Title: PARI Regulates Stalled Replication Fork Processing To Maintain Genome Stability upon Replication Stress in Mice
    Article Snippet: The cells were lysed in 1% SDS, 50 mM Tris-HCl, pH 8.0, and sonicated with an ultrasonicator (S220; Covaris). .. After centrifugation, protease inhibitor cocktail (Roche) was added to the supernatant, incubated with streptavidin-agarose resin beads (Novagen), and washed with PBS, followed by a high-stringency wash with 1 M NaCl and 0.5% SDS in 25 mM Tris-HCl, pH 8.0, solution.

    SDS Page:

    Article Title: PARI Regulates Stalled Replication Fork Processing To Maintain Genome Stability upon Replication Stress in Mice
    Article Snippet: After centrifugation, protease inhibitor cocktail (Roche) was added to the supernatant, incubated with streptavidin-agarose resin beads (Novagen), and washed with PBS, followed by a high-stringency wash with 1 M NaCl and 0.5% SDS in 25 mM Tris-HCl, pH 8.0, solution. .. Then, the beads were eluted with standard SDS-PAGE loading buffer for 25 min at 95°C.

    Plasmid Preparation:

    Article Title: PARI Regulates Stalled Replication Fork Processing To Maintain Genome Stability upon Replication Stress in Mice
    Article Snippet: Briefly, 1 × 108 293T cells were transiently transfected with the pCAG-FLAG-PARI plasmid and pulse-labeled with 20 μM EdU (Thermo Scientific) for 30 min. .. After centrifugation, protease inhibitor cocktail (Roche) was added to the supernatant, incubated with streptavidin-agarose resin beads (Novagen), and washed with PBS, followed by a high-stringency wash with 1 M NaCl and 0.5% SDS in 25 mM Tris-HCl, pH 8.0, solution.

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    Millipore streptavidin agarose beads
    Proline-rich reading array screen and peptide pulldown. (A) Use of biotinylated eVP40 WT (MRRVILPTAPPEYMEAI[Lys-biotin]) peptide (50 μg) to screen a proline-rich reading array. The GST-WW domain fusion proteins are arrayed in duplicate and at different angles, as indicated in enlarged box C. Box C shows duplicate samples of all four WW domains from WWP1, WWP2, and ITCH as indicated. Additional positive interactions are indicated in the highlighted red boxes and ovals (A to H). The eVP40 mutant peptide (MRRVILPTAAAEAMEAI[Lys-biotin]) did not interact with any GST-WW domain fusion protein (data not shown). (B) Exogenously expressed FLAG-tagged WWP1-WT was pulled down with <t>streptavidin</t> beads bound to either eVP40 WT (WT) or PPXY mutant (mut) peptides and detected by Western blotting using anti-Flag antiserum (top). Expression controls for WWP1 and actin are shown (bottom).
    Streptavidin Agarose Beads, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 293 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin agarose beads/product/Millipore
    Average 97 stars, based on 293 article reviews
    Price from $9.99 to $1999.99
    streptavidin agarose beads - by Bioz Stars, 2020-04
    97/100 stars
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    Proline-rich reading array screen and peptide pulldown. (A) Use of biotinylated eVP40 WT (MRRVILPTAPPEYMEAI[Lys-biotin]) peptide (50 μg) to screen a proline-rich reading array. The GST-WW domain fusion proteins are arrayed in duplicate and at different angles, as indicated in enlarged box C. Box C shows duplicate samples of all four WW domains from WWP1, WWP2, and ITCH as indicated. Additional positive interactions are indicated in the highlighted red boxes and ovals (A to H). The eVP40 mutant peptide (MRRVILPTAAAEAMEAI[Lys-biotin]) did not interact with any GST-WW domain fusion protein (data not shown). (B) Exogenously expressed FLAG-tagged WWP1-WT was pulled down with streptavidin beads bound to either eVP40 WT (WT) or PPXY mutant (mut) peptides and detected by Western blotting using anti-Flag antiserum (top). Expression controls for WWP1 and actin are shown (bottom).

    Journal: Journal of Virology

    Article Title: Ubiquitin Ligase WWP1 Interacts with Ebola Virus VP40 To Regulate Egress

    doi: 10.1128/JVI.00812-17

    Figure Lengend Snippet: Proline-rich reading array screen and peptide pulldown. (A) Use of biotinylated eVP40 WT (MRRVILPTAPPEYMEAI[Lys-biotin]) peptide (50 μg) to screen a proline-rich reading array. The GST-WW domain fusion proteins are arrayed in duplicate and at different angles, as indicated in enlarged box C. Box C shows duplicate samples of all four WW domains from WWP1, WWP2, and ITCH as indicated. Additional positive interactions are indicated in the highlighted red boxes and ovals (A to H). The eVP40 mutant peptide (MRRVILPTAAAEAMEAI[Lys-biotin]) did not interact with any GST-WW domain fusion protein (data not shown). (B) Exogenously expressed FLAG-tagged WWP1-WT was pulled down with streptavidin beads bound to either eVP40 WT (WT) or PPXY mutant (mut) peptides and detected by Western blotting using anti-Flag antiserum (top). Expression controls for WWP1 and actin are shown (bottom).

    Article Snippet: Streptavidin agarose beads (Millipore) were prewashed once with 1× mild buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.1% NP-40, 5 mM EDTA, 5 mM EGTA, 15 mM MgCl2 ), and 15 μg of the WT or PPXY mutant eVP40 peptide was incubated with the prewashed streptavidin beads in 500 μl of 1× mild buffer for 1 h at 4°C with rocking.

    Techniques: Mutagenesis, Western Blot, Expressing

    The rate of cell surface expression/appearance/transport of BRI2 is reduced in the absence of N-glycosylation. Wild-type mycBRI2 or mycBRI2/N170A was expressed in HEK293 cells. The newly synthesized proteins were labeled with 35 S in radiolabeling medium for 2 h (pulse) at 16°C and then were incubated in non-radiolabeling medium for 0′, 20′, 40′ and 60′ (chase). ( A ) Cell surface proteins were labeled with biotin and precipitated with streptavidin beads. Precipitated cell surface proteins were eluted from the beads and immunoprecipitated with 9B11 antibody against the myc epitope before electrophoresis and autoradiography. ( B ) Immunoprecipitation of cell extracts with 9B11, electrophoresis and autoradiography were performed to verify the expression levels of BRI2.

    Journal: Glycobiology

    Article Title: Glycosylation of BRI2 on asparagine 170 is involved in its trafficking to the cell surface but not in its processing by furin or ADAM10

    doi: 10.1093/glycob/cwr097

    Figure Lengend Snippet: The rate of cell surface expression/appearance/transport of BRI2 is reduced in the absence of N-glycosylation. Wild-type mycBRI2 or mycBRI2/N170A was expressed in HEK293 cells. The newly synthesized proteins were labeled with 35 S in radiolabeling medium for 2 h (pulse) at 16°C and then were incubated in non-radiolabeling medium for 0′, 20′, 40′ and 60′ (chase). ( A ) Cell surface proteins were labeled with biotin and precipitated with streptavidin beads. Precipitated cell surface proteins were eluted from the beads and immunoprecipitated with 9B11 antibody against the myc epitope before electrophoresis and autoradiography. ( B ) Immunoprecipitation of cell extracts with 9B11, electrophoresis and autoradiography were performed to verify the expression levels of BRI2.

    Article Snippet: The cell extracts were centrifuged at 15,000 × g for 30 min and supernatants were incubated with 50 μL of streptavidin–agarose beads (Millipore) for 1 h at 4°C.

    Techniques: Expressing, Synthesized, Labeling, Radioactivity, Incubation, Immunoprecipitation, Electrophoresis, Autoradiography

    Inhibition of N-glycosylation of BRI2 inhibits its expression at the cell surface. Wild-type mycBRI2 or mycBRI2/N170A was expressed in HEK293 cells. Cell surface proteins were labeled with biotin (lanes 1 and 2) or were not labeled (lanes 3 and 4), as a control for biotinylation specificity. ( A ) Cell extracts were precipitated with streptavidin beads and analyzed with western blot against myc with 9B11 antibody. ( B ) Cell extracts were directly analyzed with western blot as a control for protein expression. The two immunoreactive bands of BRI2 proteins correspond to the furin-cleaved and the non-cleaved wild-type mycBRI2 or mycBRI2/N170A.

    Journal: Glycobiology

    Article Title: Glycosylation of BRI2 on asparagine 170 is involved in its trafficking to the cell surface but not in its processing by furin or ADAM10

    doi: 10.1093/glycob/cwr097

    Figure Lengend Snippet: Inhibition of N-glycosylation of BRI2 inhibits its expression at the cell surface. Wild-type mycBRI2 or mycBRI2/N170A was expressed in HEK293 cells. Cell surface proteins were labeled with biotin (lanes 1 and 2) or were not labeled (lanes 3 and 4), as a control for biotinylation specificity. ( A ) Cell extracts were precipitated with streptavidin beads and analyzed with western blot against myc with 9B11 antibody. ( B ) Cell extracts were directly analyzed with western blot as a control for protein expression. The two immunoreactive bands of BRI2 proteins correspond to the furin-cleaved and the non-cleaved wild-type mycBRI2 or mycBRI2/N170A.

    Article Snippet: The cell extracts were centrifuged at 15,000 × g for 30 min and supernatants were incubated with 50 μL of streptavidin–agarose beads (Millipore) for 1 h at 4°C.

    Techniques: Inhibition, Expressing, Labeling, Western Blot

    A19 phosphorylation. (A) Western blot analysis. BS-C-1 cells were infected with vFS-A11 and vFS-A19 in the presence of 100 μCi/ml 32 P i . After 18 h, the cells were lysed, and the soluble extract was bound to streptavidin-agarose beads. Bound proteins

    Journal: Journal of Virology

    Article Title: Vaccinia Virus A19 Protein Participates in the Transformation of Spherical Immature Particles to Barrel-Shaped Infectious Virions

    doi: 10.1128/JVI.01258-13

    Figure Lengend Snippet: A19 phosphorylation. (A) Western blot analysis. BS-C-1 cells were infected with vFS-A11 and vFS-A19 in the presence of 100 μCi/ml 32 P i . After 18 h, the cells were lysed, and the soluble extract was bound to streptavidin-agarose beads. Bound proteins

    Article Snippet: Soluble extracts obtained by low-speed centrifugation were allowed to bind to streptavidin-agarose beads (Millipore, Billerica, MA) for 3 h at 4°C.

    Techniques: Western Blot, Infection

    Expression and characterization of the A19 protein. (A) Schematic representation of the DNA construct used for generating recombinant vFS-A19. The FLAG- and streptavidin-binding peptide tag fused at the N terminus of the A19 ORF (FS) is indicated. The

    Journal: Journal of Virology

    Article Title: Vaccinia Virus A19 Protein Participates in the Transformation of Spherical Immature Particles to Barrel-Shaped Infectious Virions

    doi: 10.1128/JVI.01258-13

    Figure Lengend Snippet: Expression and characterization of the A19 protein. (A) Schematic representation of the DNA construct used for generating recombinant vFS-A19. The FLAG- and streptavidin-binding peptide tag fused at the N terminus of the A19 ORF (FS) is indicated. The

    Article Snippet: Soluble extracts obtained by low-speed centrifugation were allowed to bind to streptavidin-agarose beads (Millipore, Billerica, MA) for 3 h at 4°C.

    Techniques: Expressing, Construct, Recombinant, Binding Assay

    Analysis of viral PPxY-host WW-domain interactions between BAG3 and LFV-Z by peptide pull-down assays. ( A ) Flow chart of the peptide pull-down assay using LFV-Z peptides and cell lysates expressing BAG3-WT; ( B ) Schematic diagram of BAG3-WT, BAG3-ΔN, and BAG3-ΔC mutants with the various domains highlighted in color and amino acid positions indicated; ( C ) Western blot of peptide pull-down assay using streptavidin agarose beads conjugated with either the LFV-Z WT or LFV-Z PY mutant peptide. BAG3 proteins were detected using anti-c-myc antibody (top blot). Expression controls for BAG3 and actin are shown in the bottom blot. These results are from 1 of 2 independent experiments.

    Journal: Diseases

    Article Title: Host Protein BAG3 is a Negative Regulator of Lassa VLP Egress

    doi: 10.3390/diseases6030064

    Figure Lengend Snippet: Analysis of viral PPxY-host WW-domain interactions between BAG3 and LFV-Z by peptide pull-down assays. ( A ) Flow chart of the peptide pull-down assay using LFV-Z peptides and cell lysates expressing BAG3-WT; ( B ) Schematic diagram of BAG3-WT, BAG3-ΔN, and BAG3-ΔC mutants with the various domains highlighted in color and amino acid positions indicated; ( C ) Western blot of peptide pull-down assay using streptavidin agarose beads conjugated with either the LFV-Z WT or LFV-Z PY mutant peptide. BAG3 proteins were detected using anti-c-myc antibody (top blot). Expression controls for BAG3 and actin are shown in the bottom blot. These results are from 1 of 2 independent experiments.

    Article Snippet: Briefly, extracts from HEK293T cells expressing either BAG3-WT, BAG3-ΔN, or BAG3-ΔC ( B) were incubated with streptavidin agarose beads bound with either the LFV-Z-WT or LFV-Z-mutant peptides.

    Techniques: Flow Cytometry, Pull Down Assay, Expressing, Western Blot, Mutagenesis