streptavidin conjugated agarose  (Millipore)


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    Structured Review

    Millipore streptavidin conjugated agarose
    Cell surface localization of unglycosylated gp130 in NECs treated with tunicamycin. To confirm the cell surface localization of unglycosylated gp130, cell surface proteins expressed in NECs treated with or without tunicamycin (2 μg/ml) for 8 h were biotinylated by treating the cells with sulfo-NHS-LC-biotin. After lysis, biotinylated cell surface proteins were pulled down with <t>streptavidin-conjugated</t> agarose and then analyzed by Western-blot using anti-gp130 antibody ( A ) or anti-LIFR antibody ( B ).
    Streptavidin Conjugated Agarose, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin conjugated agarose/product/Millipore
    Average 99 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    streptavidin conjugated agarose - by Bioz Stars, 2020-04
    99/100 stars

    Images

    1) Product Images from "N-Glycans modulate the activation of gp130 in mouse embryonic neural precursor cells"

    Article Title: N-Glycans modulate the activation of gp130 in mouse embryonic neural precursor cells

    Journal: Biochemical and biophysical research communications

    doi: 10.1016/j.bbrc.2009.05.132

    Cell surface localization of unglycosylated gp130 in NECs treated with tunicamycin. To confirm the cell surface localization of unglycosylated gp130, cell surface proteins expressed in NECs treated with or without tunicamycin (2 μg/ml) for 8 h were biotinylated by treating the cells with sulfo-NHS-LC-biotin. After lysis, biotinylated cell surface proteins were pulled down with streptavidin-conjugated agarose and then analyzed by Western-blot using anti-gp130 antibody ( A ) or anti-LIFR antibody ( B ).
    Figure Legend Snippet: Cell surface localization of unglycosylated gp130 in NECs treated with tunicamycin. To confirm the cell surface localization of unglycosylated gp130, cell surface proteins expressed in NECs treated with or without tunicamycin (2 μg/ml) for 8 h were biotinylated by treating the cells with sulfo-NHS-LC-biotin. After lysis, biotinylated cell surface proteins were pulled down with streptavidin-conjugated agarose and then analyzed by Western-blot using anti-gp130 antibody ( A ) or anti-LIFR antibody ( B ).

    Techniques Used: Lysis, Western Blot

    2) Product Images from "?-Opioid receptors stimulate GLUT1-mediated glucose uptake through Src- and IGF-1 receptor-dependent activation of PI3-kinase signalling in CHO cells"

    Article Title: ?-Opioid receptors stimulate GLUT1-mediated glucose uptake through Src- and IGF-1 receptor-dependent activation of PI3-kinase signalling in CHO cells

    Journal: British Journal of Pharmacology

    doi: 10.1111/j.1476-5381.2011.01234.x

    SNC 80 increases maximal glucose transport rate without changing membrane GLUT1 expression. (A) Cells were incubated with either vehicle (control) or 100 nM SNC 80 for 15 min. Thereafter, [ 3 H]-2-deoxy-D-glucose uptake was determined in the presence of the indicated concentrations of unlabelled hexose. Values are mean ± SEM of three experiments. (B) Lineweaver-Burk plot of the data reported in (A). (C) Western blot analysis of GLUT1, GLUT3 and GLUT4 expression in CHO/DOR whole-cell extracts. GLUT3 and GLUT4 immunoreactivities in rat frontal cortex and soleus, respectively, are also shown. Each lane was loaded with 5 µg of cell or tissue protein. Data are representative of three similar experiments. (D) Cells (deprived of serum) were treated as in glucose uptake experiments and incubated for 15 min with either vehicle or 100 nM SNC 80. Cells were washed and incubated for 30 min at 4°C without or with 0.25 mg·mL −1 sulpho-NHS-LC-biotin. Cell extracts were incubated overnight with streptavidin-conjugated agarose beads and the samples were then centrifuged to obtain a supernatant (supern) and a pellet fraction. Following repeated washing, the biotinylated proteins were separated by SDS-PAGE and immunoblotted with antibodies against GLUT1, α1 subunit of Na + /K + ATPase (Na/K-ATPase) as plasma membrane marker protein, and actin as cytosolic marker protein. The density of GLUT1 immunoreactive bands was measured and normalized to the density of either the Na/K-ATPase or actin for plasma membrane and cytosolic samples respectively. Values are mean ± SEM of four experiments. (E) Western blot analysis of GLUT1 content in plasma membrane (p membr) and microsomal (micr) fractions of cells treated with either vehicle or SNC 80 (100 nM) for 15 min. Data are representative of three experiments. CHO, Chinese hamster ovary; CHO/DOR, CHO cells stably expressing the human δ-opioid receptor; SDS, sodium dodecyl sulphate; SDS-PAGE, SDS-polyacrylamide gel electrophoresis.
    Figure Legend Snippet: SNC 80 increases maximal glucose transport rate without changing membrane GLUT1 expression. (A) Cells were incubated with either vehicle (control) or 100 nM SNC 80 for 15 min. Thereafter, [ 3 H]-2-deoxy-D-glucose uptake was determined in the presence of the indicated concentrations of unlabelled hexose. Values are mean ± SEM of three experiments. (B) Lineweaver-Burk plot of the data reported in (A). (C) Western blot analysis of GLUT1, GLUT3 and GLUT4 expression in CHO/DOR whole-cell extracts. GLUT3 and GLUT4 immunoreactivities in rat frontal cortex and soleus, respectively, are also shown. Each lane was loaded with 5 µg of cell or tissue protein. Data are representative of three similar experiments. (D) Cells (deprived of serum) were treated as in glucose uptake experiments and incubated for 15 min with either vehicle or 100 nM SNC 80. Cells were washed and incubated for 30 min at 4°C without or with 0.25 mg·mL −1 sulpho-NHS-LC-biotin. Cell extracts were incubated overnight with streptavidin-conjugated agarose beads and the samples were then centrifuged to obtain a supernatant (supern) and a pellet fraction. Following repeated washing, the biotinylated proteins were separated by SDS-PAGE and immunoblotted with antibodies against GLUT1, α1 subunit of Na + /K + ATPase (Na/K-ATPase) as plasma membrane marker protein, and actin as cytosolic marker protein. The density of GLUT1 immunoreactive bands was measured and normalized to the density of either the Na/K-ATPase or actin for plasma membrane and cytosolic samples respectively. Values are mean ± SEM of four experiments. (E) Western blot analysis of GLUT1 content in plasma membrane (p membr) and microsomal (micr) fractions of cells treated with either vehicle or SNC 80 (100 nM) for 15 min. Data are representative of three experiments. CHO, Chinese hamster ovary; CHO/DOR, CHO cells stably expressing the human δ-opioid receptor; SDS, sodium dodecyl sulphate; SDS-PAGE, SDS-polyacrylamide gel electrophoresis.

    Techniques Used: Expressing, Incubation, Western Blot, SDS Page, Marker, Stable Transfection, Polyacrylamide Gel Electrophoresis

    3) Product Images from "N-Glycans modulate the activation of gp130 in mouse embryonic neural precursor cells"

    Article Title: N-Glycans modulate the activation of gp130 in mouse embryonic neural precursor cells

    Journal: Biochemical and biophysical research communications

    doi: 10.1016/j.bbrc.2009.05.132

    Cell surface localization of unglycosylated gp130 in NECs treated with tunicamycin. To confirm the cell surface localization of unglycosylated gp130, cell surface proteins expressed in NECs treated with or without tunicamycin (2 μg/ml) for 8 h were biotinylated by treating the cells with sulfo-NHS-LC-biotin. After lysis, biotinylated cell surface proteins were pulled down with streptavidin-conjugated agarose and then analyzed by Western-blot using anti-gp130 antibody ( A ) or anti-LIFR antibody ( B ).
    Figure Legend Snippet: Cell surface localization of unglycosylated gp130 in NECs treated with tunicamycin. To confirm the cell surface localization of unglycosylated gp130, cell surface proteins expressed in NECs treated with or without tunicamycin (2 μg/ml) for 8 h were biotinylated by treating the cells with sulfo-NHS-LC-biotin. After lysis, biotinylated cell surface proteins were pulled down with streptavidin-conjugated agarose and then analyzed by Western-blot using anti-gp130 antibody ( A ) or anti-LIFR antibody ( B ).

    Techniques Used: Lysis, Western Blot

    4) Product Images from "NEDD9/Arf6-Dependent Endocytic Trafficking of Matrix Metalloproteinase 14: A Novel Mechanism for Blocking Mesenchymal Cell Invasion and Metastasis of Breast Cancer"

    Article Title: NEDD9/Arf6-Dependent Endocytic Trafficking of Matrix Metalloproteinase 14: A Novel Mechanism for Blocking Mesenchymal Cell Invasion and Metastasis of Breast Cancer

    Journal: Oncogene

    doi: 10.1038/onc.2014.297

    NEDD9 depletion does not affect internalization of MMP14 (a) Western blot (WB) analysis of immunoprecipitated (IP) biotinylated MMP14 from shCon-, shNEDD9 (N1, N2)-MDA-MB-231cells: no strip-0°C (lines 1-3), the rest incubated at 37°C for indicated times, striped with MESNA, lysed, IPed with streptavidin agarose and probed with anti-MMP14 antibody. (b) Quantification of WBs as in (a), three independent experiments, graphs are mean percent (%) of relative intensity units (RIU) to no strip conditions (100%) ±S.E.M; one-way ANOVA with Dunnett's post-hoc analysis *p= 0.0054, 0.0049, 0.0098, 0.0028 for 5, 15, 30 and 60 min respectively. (c) Representative confocal images of shCon-, shNEDD9 (N1, N2)-MDA-MB-231cells expressing PA-mCherry-MMP14 before photo-activation (pre-PA), after- (PA), and 5 min after PA in a defined area. Scale bar, 10μm; inserts are the enlarged areas of PA; BF-bright field image. (d) Quantification of relative fluorescence intensity units (RFU) of mCherry-MMP14 in cells as in (c) in perinuclear area (p); graph is mean RFU % of total RFU/cell ±S.E.M; 10 cells/per treatment (Con, N1, N2); F test performed for fitted lines, p is non-significant (ns) for shCon/shN1 or /N2. (e) Quantification of relative fluorescence intensity (RFU) of mCherry-MMP14 in cells as in (c) in PA area (black rectangle); graph is mean RFU (%) of max RFU/cell (100%) ±S.E.M; 10 cells/per treatment (Con, N1, N2), F test performed for fitted lines, p is (ns).
    Figure Legend Snippet: NEDD9 depletion does not affect internalization of MMP14 (a) Western blot (WB) analysis of immunoprecipitated (IP) biotinylated MMP14 from shCon-, shNEDD9 (N1, N2)-MDA-MB-231cells: no strip-0°C (lines 1-3), the rest incubated at 37°C for indicated times, striped with MESNA, lysed, IPed with streptavidin agarose and probed with anti-MMP14 antibody. (b) Quantification of WBs as in (a), three independent experiments, graphs are mean percent (%) of relative intensity units (RIU) to no strip conditions (100%) ±S.E.M; one-way ANOVA with Dunnett's post-hoc analysis *p= 0.0054, 0.0049, 0.0098, 0.0028 for 5, 15, 30 and 60 min respectively. (c) Representative confocal images of shCon-, shNEDD9 (N1, N2)-MDA-MB-231cells expressing PA-mCherry-MMP14 before photo-activation (pre-PA), after- (PA), and 5 min after PA in a defined area. Scale bar, 10μm; inserts are the enlarged areas of PA; BF-bright field image. (d) Quantification of relative fluorescence intensity units (RFU) of mCherry-MMP14 in cells as in (c) in perinuclear area (p); graph is mean RFU % of total RFU/cell ±S.E.M; 10 cells/per treatment (Con, N1, N2); F test performed for fitted lines, p is non-significant (ns) for shCon/shN1 or /N2. (e) Quantification of relative fluorescence intensity (RFU) of mCherry-MMP14 in cells as in (c) in PA area (black rectangle); graph is mean RFU (%) of max RFU/cell (100%) ±S.E.M; 10 cells/per treatment (Con, N1, N2), F test performed for fitted lines, p is (ns).

    Techniques Used: Western Blot, Immunoprecipitation, Multiple Displacement Amplification, Stripping Membranes, Incubation, Expressing, Activation Assay, Fluorescence

    5) Product Images from "Involvement of ?1-Integrin Up-regulation in Basic Fibroblast Growth Factor- and Epidermal Growth Factor-induced Proliferation of Mouse Neuroepithelial Cells *"

    Article Title: Involvement of ?1-Integrin Up-regulation in Basic Fibroblast Growth Factor- and Epidermal Growth Factor-induced Proliferation of Mouse Neuroepithelial Cells *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.114645

    bFGF- and EGF-induced up-regulation of β1-integrin in NECs. A , total cell lysates from NECs cultured in the presence or absence of 10 and 50 ng/ml of bFGF or EGF for 4 days were analyzed by Western blot with the anti-β1-integrin antibody and anti-β-actin antibody. β-Actin was detected as a loading control. B , the intensities of β1-integrin bands in A were quantified by Image J software ( n = 3). C , to confirm the cell surface localization of β1-integrin, NECs cultured in the presence of 10 and 50 ng/ml bFGF or EGF for 4 days were biotinylated by treating the cells with sulfo-NHS-LC-biotin. After lysis, biotinylated cell surface proteins were pulled down with streptavidin-conjugated agarose. The cell lysates ( Input ) and pull-down were analyzed by Western blot. D , the intensities of β1-integrin bands in ( C , Pulldown ) were quantified by Image J software ( n = 3).
    Figure Legend Snippet: bFGF- and EGF-induced up-regulation of β1-integrin in NECs. A , total cell lysates from NECs cultured in the presence or absence of 10 and 50 ng/ml of bFGF or EGF for 4 days were analyzed by Western blot with the anti-β1-integrin antibody and anti-β-actin antibody. β-Actin was detected as a loading control. B , the intensities of β1-integrin bands in A were quantified by Image J software ( n = 3). C , to confirm the cell surface localization of β1-integrin, NECs cultured in the presence of 10 and 50 ng/ml bFGF or EGF for 4 days were biotinylated by treating the cells with sulfo-NHS-LC-biotin. After lysis, biotinylated cell surface proteins were pulled down with streptavidin-conjugated agarose. The cell lysates ( Input ) and pull-down were analyzed by Western blot. D , the intensities of β1-integrin bands in ( C , Pulldown ) were quantified by Image J software ( n = 3).

    Techniques Used: Cell Culture, Western Blot, Software, Lysis

    Related Articles

    Amplification:

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Synthesized:

    Article Title: Specificity of ? and Non-? Isoforms of Arabidopsis 14-3-3 Proteins Towards the H+-ATPase and Other Targets
    Article Snippet: The bL15Vp peptide biotinyl-LKGLDIDTIQQNYTpV (Tp, phosphothreonine) was synthesized by Neosystem (Strasbourg, France). .. Streptavidin-agarose magnetic beads, glutathione-sepharose resin, the catalytic subunit of protein kinase A and thrombin were obtained from Sigma (St. Louis, MO, USA).

    Incubation:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: One sample was neither incubated nor reduced with cleavage buffer to determine the total amount of biotinylated proteins. .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions.

    Article Title: Conserved Intergenic Elements and DNA Methylation Cooperate to Regulate Transcription at the il17 Locus *
    Article Snippet: Oligonucleotide probes used for EMSA analysis were 5′ end-labeled with biotin and incubated (0.5 μ m ) with total cell lysate (400 μg) prepared from stimulated Th17 cells under the same ionic conditions used in EMSA reactions. .. Magnetic streptavidin-conjugated agarose beads (MagSelect, Sigma-Aldrich) were used to collect protein complexes bound to the DNA probes.

    Activity Assay:

    Article Title: DNA binding induces dissociation of the multimeric form of HIV-1 integrase: A time-resolved fluorescence anisotropy study
    Article Snippet: Paragraph title: IN and Activity Assay. ... After removal of thrombin by streptavidin-agarose magnetic beads (Novagen), a final dialysis was performed against buffer A containing 20% (vol/vol) glycerol.

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: The helicases containing fractions, identified by both DNA-dependent ATP hydrolysis and helicase activity assays, were pooled. .. Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI).

    Expressing:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: The expression of the protein was induced by adding isopropylthio-β- d -galactoside to 0.5 mM at low-log phase (OD600 = 0.6). .. Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI).

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: Verification of biotinylated-SSO incorporation λ-Red expression was induced in cultures of DY380/pmKan cells (in 50 ml LB medium in 250 ml Erlenmeyer flasks, grown to OD600 0.3) by shifting them from incubation at 32°C to a shaking water bath at 42°C for 15 min, before chilling them in iced-water. .. After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ).

    Transferring:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions. .. The presence of RSV F proteins was detected by transferring the gel to a polyvinylidene difluoride (PVDF) membrane and subsequent incubation with RSV F-specific MAb.

    Infection:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: Surface proteins of the infected cells were biotinylated using EZ-link Sulfo-NHS-SS-biotin (Thermo Fisher Scientific) at 4°C. .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions.

    Endocytosis Assay:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: Paragraph title: Spontaneous endocytosis assay. ... After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions.

    DNA Sequencing:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. The mutation was created using the QuikChange kit for Site-Directed Mutagenesis from Stratagene and confirmed by DNA sequencing (MWG Biotech).

    Polymerase Chain Reaction:

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Binding Assay:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: The lysate was centrifuged and applied to the column charged with histidine binding resin (Novagen). .. Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI).

    Magnetic Beads:

    Article Title: Specificity of ? and Non-? Isoforms of Arabidopsis 14-3-3 Proteins Towards the H+-ATPase and Other Targets
    Article Snippet: .. Streptavidin-agarose magnetic beads, glutathione-sepharose resin, the catalytic subunit of protein kinase A and thrombin were obtained from Sigma (St. Louis, MO, USA). .. Restriction enzymes were obtained from Roche Diagnostics (Mannheim, Germany).

    Article Title: DNA binding induces dissociation of the multimeric form of HIV-1 integrase: A time-resolved fluorescence anisotropy study
    Article Snippet: .. After removal of thrombin by streptavidin-agarose magnetic beads (Novagen), a final dialysis was performed against buffer A containing 20% (vol/vol) glycerol. .. TFA parameters were obtained from the two polarized fluorescence decays Ivv(t) and Ivh(t) by using a time-correlated, single-photon counting technique.

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: .. Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. RecQ helicase was further purified by FPLC size-exclusion chromatography using a Superdex 200 column (Pharmacia).

    Mutagenesis:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. The mutation was created using the QuikChange kit for Site-Directed Mutagenesis from Stratagene and confirmed by DNA sequencing (MWG Biotech).

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Isolation:

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: .. After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Size-exclusion Chromatography:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. RecQ helicase was further purified by FPLC size-exclusion chromatography using a Superdex 200 column (Pharmacia).

    Purification:

    Article Title: DNA binding induces dissociation of the multimeric form of HIV-1 integrase: A time-resolved fluorescence anisotropy study
    Article Snippet: The purification was based on a batch procedure by using Ni-NTA agarose beads (Amersham Pharmacia). .. After removal of thrombin by streptavidin-agarose magnetic beads (Novagen), a final dialysis was performed against buffer A containing 20% (vol/vol) glycerol.

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. RecQ helicase was further purified by FPLC size-exclusion chromatography using a Superdex 200 column (Pharmacia).

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: .. After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Fast Protein Liquid Chromatography:

    Article Title: Simultaneously monitoring DNA binding and helicase-catalyzed DNA unwinding by fluorescence polarization
    Article Snippet: Removal of biotinylated thrombin was accomplished using streptavidin–agarose magnetic beads (Novagen, Madison, WI). .. RecQ helicase was further purified by FPLC size-exclusion chromatography using a Superdex 200 column (Pharmacia).

    SDS Page:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions. .. The presence of RSV F proteins was detected by transferring the gel to a polyvinylidene difluoride (PVDF) membrane and subsequent incubation with RSV F-specific MAb.

    Plasmid Preparation:

    Article Title: The involvement of replication in single stranded oligonucleotide-mediated gene repair
    Article Snippet: .. After isolation of the plasmid DNA, biotinylated DNA was captured on streptavidin-conjugated magnetic agarose beads (Novagen), and was purified as described by Edwards et al . ( ). .. The identity of the biotinylated pmKan plasmid was confirmed by PCR amplification of a 496 bp-region of the kan gene which contained the site of the original point mutation using primer 1 and primer 2.

    Radio Immunoprecipitation:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions. .. The presence of RSV F proteins was detected by transferring the gel to a polyvinylidene difluoride (PVDF) membrane and subsequent incubation with RSV F-specific MAb.

    Immunoprecipitation:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions. .. The presence of RSV F proteins was detected by transferring the gel to a polyvinylidene difluoride (PVDF) membrane and subsequent incubation with RSV F-specific MAb.

    Lysis:

    Article Title: Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein
    Article Snippet: .. After lysis of the cells with radioimmunoprecipitation assay (RIPA) lysis buffer (Millipore), biotinylated proteins were immunoprecipitated using Streptavidin Mag Sepharose (Sigma) and then SDS-PAGE under nonreducing conditions. .. The presence of RSV F proteins was detected by transferring the gel to a polyvinylidene difluoride (PVDF) membrane and subsequent incubation with RSV F-specific MAb.

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    Millipore streptavidin conjugated agarose
    Cell surface localization of unglycosylated gp130 in NECs treated with tunicamycin. To confirm the cell surface localization of unglycosylated gp130, cell surface proteins expressed in NECs treated with or without tunicamycin (2 μg/ml) for 8 h were biotinylated by treating the cells with sulfo-NHS-LC-biotin. After lysis, biotinylated cell surface proteins were pulled down with <t>streptavidin-conjugated</t> agarose and then analyzed by Western-blot using anti-gp130 antibody ( A ) or anti-LIFR antibody ( B ).
    Streptavidin Conjugated Agarose, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin conjugated agarose/product/Millipore
    Average 92 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    streptavidin conjugated agarose - by Bioz Stars, 2020-04
    92/100 stars
      Buy from Supplier

    92
    Millipore streptavidin conjugated agarose beads
    CARM1 is in association with Sox2. (A) Co-immunoprecipitation of Sox2 with CARM1. Whole cell extracts (WCEs) of MCF7 cells transfected with (+) or without (-) FLAG-CARM1 or GFP-Sox2, were subjected to immunoprecipitation with anti-FLAG antibody and blotted with antibodies against GFP or FLAG. (B) Co-precipitation of endogenous CARM1 with Sox2 by DNA pull-down. Biotin-labeled probes covering Sox2-binding sites in fgf4 and utf1 respectively were incubated with WCEs of P19 cells and <t>streptavidin-conjugated</t> agarose beads. The proteins precipitated with beads were denatured and resolved in SDS-PAGE and detected by immunoblotting with antibodies against Sox2 or CARM1. NC: negative control, no probe added. (C) Schematic drawing of the wild type and truncated CARM1 fragments. (D) GST pull-down assays to detect the interaction of Sox2 with CARM1 derivates. GST or GST-Sox2 was first incubated with WCEs of HEK293T cells ectopically expressing FLAG-CARM1 derivates. The GST pull-down products were immunoblotted with anti-FLAG antibody. Input: WCE control. (E) Schematic drawing of the wild type and truncated Sox2 fragments. (F) The interaction of Sox2 derivates with CARM1 in GST pull-down assays. GST or GST-Sox2 derivates were first incubated with whole cell extracts (WCEs) of HEK293T cells ectopically expressing FLAG-CARM1. The GST pull-down products were immunoblotted with anti-FLAG antibody.
    Streptavidin Conjugated Agarose Beads, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/streptavidin conjugated agarose beads/product/Millipore
    Average 92 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    streptavidin conjugated agarose beads - by Bioz Stars, 2020-04
    92/100 stars
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    Cell surface localization of unglycosylated gp130 in NECs treated with tunicamycin. To confirm the cell surface localization of unglycosylated gp130, cell surface proteins expressed in NECs treated with or without tunicamycin (2 μg/ml) for 8 h were biotinylated by treating the cells with sulfo-NHS-LC-biotin. After lysis, biotinylated cell surface proteins were pulled down with streptavidin-conjugated agarose and then analyzed by Western-blot using anti-gp130 antibody ( A ) or anti-LIFR antibody ( B ).

    Journal: Biochemical and biophysical research communications

    Article Title: N-Glycans modulate the activation of gp130 in mouse embryonic neural precursor cells

    doi: 10.1016/j.bbrc.2009.05.132

    Figure Lengend Snippet: Cell surface localization of unglycosylated gp130 in NECs treated with tunicamycin. To confirm the cell surface localization of unglycosylated gp130, cell surface proteins expressed in NECs treated with or without tunicamycin (2 μg/ml) for 8 h were biotinylated by treating the cells with sulfo-NHS-LC-biotin. After lysis, biotinylated cell surface proteins were pulled down with streptavidin-conjugated agarose and then analyzed by Western-blot using anti-gp130 antibody ( A ) or anti-LIFR antibody ( B ).

    Article Snippet: Biotinylated cell surface proteins in the lysates were pulled down by gentle agitation in the presence of streptavidin-conjugated agarose (EMD Biosciences) at 4°C overnight, washed three times with the lysis buffer, denatured in Laemmli sample buffer by boiling and subjected to Western-blot analysis using an anti-gp130 antibody or an anti-LIFR antibody.

    Techniques: Lysis, Western Blot

    NEDD9 depletion does not affect internalization of MMP14 (a) Western blot (WB) analysis of immunoprecipitated (IP) biotinylated MMP14 from shCon-, shNEDD9 (N1, N2)-MDA-MB-231cells: no strip-0°C (lines 1-3), the rest incubated at 37°C for indicated times, striped with MESNA, lysed, IPed with streptavidin agarose and probed with anti-MMP14 antibody. (b) Quantification of WBs as in (a), three independent experiments, graphs are mean percent (%) of relative intensity units (RIU) to no strip conditions (100%) ±S.E.M; one-way ANOVA with Dunnett's post-hoc analysis *p= 0.0054, 0.0049, 0.0098, 0.0028 for 5, 15, 30 and 60 min respectively. (c) Representative confocal images of shCon-, shNEDD9 (N1, N2)-MDA-MB-231cells expressing PA-mCherry-MMP14 before photo-activation (pre-PA), after- (PA), and 5 min after PA in a defined area. Scale bar, 10μm; inserts are the enlarged areas of PA; BF-bright field image. (d) Quantification of relative fluorescence intensity units (RFU) of mCherry-MMP14 in cells as in (c) in perinuclear area (p); graph is mean RFU % of total RFU/cell ±S.E.M; 10 cells/per treatment (Con, N1, N2); F test performed for fitted lines, p is non-significant (ns) for shCon/shN1 or /N2. (e) Quantification of relative fluorescence intensity (RFU) of mCherry-MMP14 in cells as in (c) in PA area (black rectangle); graph is mean RFU (%) of max RFU/cell (100%) ±S.E.M; 10 cells/per treatment (Con, N1, N2), F test performed for fitted lines, p is (ns).

    Journal: Oncogene

    Article Title: NEDD9/Arf6-Dependent Endocytic Trafficking of Matrix Metalloproteinase 14: A Novel Mechanism for Blocking Mesenchymal Cell Invasion and Metastasis of Breast Cancer

    doi: 10.1038/onc.2014.297

    Figure Lengend Snippet: NEDD9 depletion does not affect internalization of MMP14 (a) Western blot (WB) analysis of immunoprecipitated (IP) biotinylated MMP14 from shCon-, shNEDD9 (N1, N2)-MDA-MB-231cells: no strip-0°C (lines 1-3), the rest incubated at 37°C for indicated times, striped with MESNA, lysed, IPed with streptavidin agarose and probed with anti-MMP14 antibody. (b) Quantification of WBs as in (a), three independent experiments, graphs are mean percent (%) of relative intensity units (RIU) to no strip conditions (100%) ±S.E.M; one-way ANOVA with Dunnett's post-hoc analysis *p= 0.0054, 0.0049, 0.0098, 0.0028 for 5, 15, 30 and 60 min respectively. (c) Representative confocal images of shCon-, shNEDD9 (N1, N2)-MDA-MB-231cells expressing PA-mCherry-MMP14 before photo-activation (pre-PA), after- (PA), and 5 min after PA in a defined area. Scale bar, 10μm; inserts are the enlarged areas of PA; BF-bright field image. (d) Quantification of relative fluorescence intensity units (RFU) of mCherry-MMP14 in cells as in (c) in perinuclear area (p); graph is mean RFU % of total RFU/cell ±S.E.M; 10 cells/per treatment (Con, N1, N2); F test performed for fitted lines, p is non-significant (ns) for shCon/shN1 or /N2. (e) Quantification of relative fluorescence intensity (RFU) of mCherry-MMP14 in cells as in (c) in PA area (black rectangle); graph is mean RFU (%) of max RFU/cell (100%) ±S.E.M; 10 cells/per treatment (Con, N1, N2), F test performed for fitted lines, p is (ns).

    Article Snippet: Cells were homogenized in PTY buffer , and biotinylated molecules were pulled down with streptavidin-conjugated agarose (Millipore) and used for western blotting.

    Techniques: Western Blot, Immunoprecipitation, Multiple Displacement Amplification, Stripping Membranes, Incubation, Expressing, Activation Assay, Fluorescence

    CARM1 is in association with Sox2. (A) Co-immunoprecipitation of Sox2 with CARM1. Whole cell extracts (WCEs) of MCF7 cells transfected with (+) or without (-) FLAG-CARM1 or GFP-Sox2, were subjected to immunoprecipitation with anti-FLAG antibody and blotted with antibodies against GFP or FLAG. (B) Co-precipitation of endogenous CARM1 with Sox2 by DNA pull-down. Biotin-labeled probes covering Sox2-binding sites in fgf4 and utf1 respectively were incubated with WCEs of P19 cells and streptavidin-conjugated agarose beads. The proteins precipitated with beads were denatured and resolved in SDS-PAGE and detected by immunoblotting with antibodies against Sox2 or CARM1. NC: negative control, no probe added. (C) Schematic drawing of the wild type and truncated CARM1 fragments. (D) GST pull-down assays to detect the interaction of Sox2 with CARM1 derivates. GST or GST-Sox2 was first incubated with WCEs of HEK293T cells ectopically expressing FLAG-CARM1 derivates. The GST pull-down products were immunoblotted with anti-FLAG antibody. Input: WCE control. (E) Schematic drawing of the wild type and truncated Sox2 fragments. (F) The interaction of Sox2 derivates with CARM1 in GST pull-down assays. GST or GST-Sox2 derivates were first incubated with whole cell extracts (WCEs) of HEK293T cells ectopically expressing FLAG-CARM1. The GST pull-down products were immunoblotted with anti-FLAG antibody.

    Journal: PLoS ONE

    Article Title: CARM1 Mediates Modulation of Sox2

    doi: 10.1371/journal.pone.0027026

    Figure Lengend Snippet: CARM1 is in association with Sox2. (A) Co-immunoprecipitation of Sox2 with CARM1. Whole cell extracts (WCEs) of MCF7 cells transfected with (+) or without (-) FLAG-CARM1 or GFP-Sox2, were subjected to immunoprecipitation with anti-FLAG antibody and blotted with antibodies against GFP or FLAG. (B) Co-precipitation of endogenous CARM1 with Sox2 by DNA pull-down. Biotin-labeled probes covering Sox2-binding sites in fgf4 and utf1 respectively were incubated with WCEs of P19 cells and streptavidin-conjugated agarose beads. The proteins precipitated with beads were denatured and resolved in SDS-PAGE and detected by immunoblotting with antibodies against Sox2 or CARM1. NC: negative control, no probe added. (C) Schematic drawing of the wild type and truncated CARM1 fragments. (D) GST pull-down assays to detect the interaction of Sox2 with CARM1 derivates. GST or GST-Sox2 was first incubated with WCEs of HEK293T cells ectopically expressing FLAG-CARM1 derivates. The GST pull-down products were immunoblotted with anti-FLAG antibody. Input: WCE control. (E) Schematic drawing of the wild type and truncated Sox2 fragments. (F) The interaction of Sox2 derivates with CARM1 in GST pull-down assays. GST or GST-Sox2 derivates were first incubated with whole cell extracts (WCEs) of HEK293T cells ectopically expressing FLAG-CARM1. The GST pull-down products were immunoblotted with anti-FLAG antibody.

    Article Snippet: In brief, 50 nmol 5′-end biotin-labeled oligo-DNA probes covering the Sox2-binding sites in fgf4 or utf1 were incubated with 1 mg whole cell extracts of P19 cells and streptavidin-conjugated agarose beads (Millipore) overnight at 4°C.

    Techniques: Immunoprecipitation, Transfection, Labeling, Binding Assay, Incubation, SDS Page, Negative Control, Expressing