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  • 99
    Thermo Fisher his tag magnetic beads
    Nanobody-coated beads agglutinate C. jejuni KC40 cells. The His-tagged nanobodies were coupled to magnetic <t>dynabeads,</t> leading to multimerization. A Nb84 coupled to dynabeads causes agglutination of KC40 cells. B As a negative control, dynabeads coated with anti- E. coli nanobodies were mixed with KC40 cells. No agglutination was observed in this case. C The C. jejuni KC40 bacteria and D the beads coated with Nb84. The results were observed by phase contrast microscopy, using a ×100 oil immersion objective.
    His Tag Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 106 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Thermo Fisher magnetic his tag dynabeads
    Nanobody-coated beads agglutinate C. jejuni KC40 cells. The His-tagged nanobodies were coupled to magnetic <t>dynabeads,</t> leading to multimerization. A Nb84 coupled to dynabeads causes agglutination of KC40 cells. B As a negative control, dynabeads coated with anti- E. coli nanobodies were mixed with KC40 cells. No agglutination was observed in this case. C The C. jejuni KC40 bacteria and D the beads coated with Nb84. The results were observed by phase contrast microscopy, using a ×100 oil immersion objective.
    Magnetic His Tag Dynabeads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/magnetic his tag dynabeads/product/Thermo Fisher
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    92
    Thermo Fisher magnetic dynabeads his tag isolation kit
    Nanobody-coated beads agglutinate C. jejuni KC40 cells. The His-tagged nanobodies were coupled to magnetic <t>dynabeads,</t> leading to multimerization. A Nb84 coupled to dynabeads causes agglutination of KC40 cells. B As a negative control, dynabeads coated with anti- E. coli nanobodies were mixed with KC40 cells. No agglutination was observed in this case. C The C. jejuni KC40 bacteria and D the beads coated with Nb84. The results were observed by phase contrast microscopy, using a ×100 oil immersion objective.
    Magnetic Dynabeads His Tag Isolation Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/magnetic dynabeads his tag isolation kit/product/Thermo Fisher
    Average 92 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
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    84
    Thermo Fisher dynabeads his tag isolation magnetic beads
    HULC interacts with the glycolytic enzyme PKM2. a Biotinylated HULC and antisense HULC were synthesized by in vitro transcription and incubated with HepG2 cell lysates, respectively. The RNA-protein complexes were isolated with streptavidin-conjugated beads. PKM2 in the pull down was examined by western blotting. Biotinylated antisense HULC was used as the control. b The cellular localizations of HULC and PKM2 were analyzed by RNA-FISH combined with immunofluorescence. Cell nuclei were stained with DAPI, and the scale bar was 20 μm. c Immunoprecipitation of PKM1 and PKM2. The left panel shows the immunoblots of PKM1 and PKM2 in the cell lysate and immunoprecipitates. The right panel shows the agarose gel electrophoresis images of the qRT-PCR products of HULC. LincRNA-p21 was examined as RNA control. d Binding of HULC to flag-tagged exon 9 (PKM1 specific) and exon 10 (PKM2 specific) as determined by the RIP assay. e His-tagged rPKM2 was first immobilized to <t>Dynabeads</t> ® His-tag isolation magnetic beads, and then incubated with in vitro transcribed HULC or antisense HULC. The RNA-protein complexes were isolated, and the levels of HULC were examined by qRT-PCR. Data represent the mean ± s.d. of triplicate independent experiments (*** P
    Dynabeads His Tag Isolation Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher magnetic beads
    HULC interacts with the glycolytic enzyme PKM2. a Biotinylated HULC and antisense HULC were synthesized by in vitro transcription and incubated with HepG2 cell lysates, respectively. The RNA-protein complexes were isolated with streptavidin-conjugated beads. PKM2 in the pull down was examined by western blotting. Biotinylated antisense HULC was used as the control. b The cellular localizations of HULC and PKM2 were analyzed by RNA-FISH combined with immunofluorescence. Cell nuclei were stained with DAPI, and the scale bar was 20 μm. c Immunoprecipitation of PKM1 and PKM2. The left panel shows the immunoblots of PKM1 and PKM2 in the cell lysate and immunoprecipitates. The right panel shows the agarose gel electrophoresis images of the qRT-PCR products of HULC. LincRNA-p21 was examined as RNA control. d Binding of HULC to flag-tagged exon 9 (PKM1 specific) and exon 10 (PKM2 specific) as determined by the RIP assay. e His-tagged rPKM2 was first immobilized to <t>Dynabeads</t> ® His-tag isolation magnetic beads, and then incubated with in vitro transcribed HULC or antisense HULC. The RNA-protein complexes were isolated, and the levels of HULC were examined by qRT-PCR. Data represent the mean ± s.d. of triplicate independent experiments (*** P
    Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 10068 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Thermo Fisher dynabeads magnetic beads
    HULC interacts with the glycolytic enzyme PKM2. a Biotinylated HULC and antisense HULC were synthesized by in vitro transcription and incubated with HepG2 cell lysates, respectively. The RNA-protein complexes were isolated with streptavidin-conjugated beads. PKM2 in the pull down was examined by western blotting. Biotinylated antisense HULC was used as the control. b The cellular localizations of HULC and PKM2 were analyzed by RNA-FISH combined with immunofluorescence. Cell nuclei were stained with DAPI, and the scale bar was 20 μm. c Immunoprecipitation of PKM1 and PKM2. The left panel shows the immunoblots of PKM1 and PKM2 in the cell lysate and immunoprecipitates. The right panel shows the agarose gel electrophoresis images of the qRT-PCR products of HULC. LincRNA-p21 was examined as RNA control. d Binding of HULC to flag-tagged exon 9 (PKM1 specific) and exon 10 (PKM2 specific) as determined by the RIP assay. e His-tagged rPKM2 was first immobilized to <t>Dynabeads</t> ® His-tag isolation magnetic beads, and then incubated with in vitro transcribed HULC or antisense HULC. The RNA-protein complexes were isolated, and the levels of HULC were examined by qRT-PCR. Data represent the mean ± s.d. of triplicate independent experiments (*** P
    Dynabeads Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 491 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Thermo Fisher cobalt derivatized magnetic beads
    HULC interacts with the glycolytic enzyme PKM2. a Biotinylated HULC and antisense HULC were synthesized by in vitro transcription and incubated with HepG2 cell lysates, respectively. The RNA-protein complexes were isolated with streptavidin-conjugated beads. PKM2 in the pull down was examined by western blotting. Biotinylated antisense HULC was used as the control. b The cellular localizations of HULC and PKM2 were analyzed by RNA-FISH combined with immunofluorescence. Cell nuclei were stained with DAPI, and the scale bar was 20 μm. c Immunoprecipitation of PKM1 and PKM2. The left panel shows the immunoblots of PKM1 and PKM2 in the cell lysate and immunoprecipitates. The right panel shows the agarose gel electrophoresis images of the qRT-PCR products of HULC. LincRNA-p21 was examined as RNA control. d Binding of HULC to flag-tagged exon 9 (PKM1 specific) and exon 10 (PKM2 specific) as determined by the RIP assay. e His-tagged rPKM2 was first immobilized to <t>Dynabeads</t> ® His-tag isolation magnetic beads, and then incubated with in vitro transcribed HULC or antisense HULC. The RNA-protein complexes were isolated, and the levels of HULC were examined by qRT-PCR. Data represent the mean ± s.d. of triplicate independent experiments (*** P
    Cobalt Derivatized Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Thermo Fisher cobalt dynabeads magnetic beads
    HULC interacts with the glycolytic enzyme PKM2. a Biotinylated HULC and antisense HULC were synthesized by in vitro transcription and incubated with HepG2 cell lysates, respectively. The RNA-protein complexes were isolated with streptavidin-conjugated beads. PKM2 in the pull down was examined by western blotting. Biotinylated antisense HULC was used as the control. b The cellular localizations of HULC and PKM2 were analyzed by RNA-FISH combined with immunofluorescence. Cell nuclei were stained with DAPI, and the scale bar was 20 μm. c Immunoprecipitation of PKM1 and PKM2. The left panel shows the immunoblots of PKM1 and PKM2 in the cell lysate and immunoprecipitates. The right panel shows the agarose gel electrophoresis images of the qRT-PCR products of HULC. LincRNA-p21 was examined as RNA control. d Binding of HULC to flag-tagged exon 9 (PKM1 specific) and exon 10 (PKM2 specific) as determined by the RIP assay. e His-tagged rPKM2 was first immobilized to <t>Dynabeads</t> ® His-tag isolation magnetic beads, and then incubated with in vitro transcribed HULC or antisense HULC. The RNA-protein complexes were isolated, and the levels of HULC were examined by qRT-PCR. Data represent the mean ± s.d. of triplicate independent experiments (*** P
    Cobalt Dynabeads Magnetic Beads, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Nanobody-coated beads agglutinate C. jejuni KC40 cells. The His-tagged nanobodies were coupled to magnetic dynabeads, leading to multimerization. A Nb84 coupled to dynabeads causes agglutination of KC40 cells. B As a negative control, dynabeads coated with anti- E. coli nanobodies were mixed with KC40 cells. No agglutination was observed in this case. C The C. jejuni KC40 bacteria and D the beads coated with Nb84. The results were observed by phase contrast microscopy, using a ×100 oil immersion objective.

    Journal: Veterinary Research

    Article Title: Nanobodies targeting conserved epitopes on the major outer membrane protein of Campylobacter as potential tools for control of Campylobacter colonization

    doi: 10.1186/s13567-017-0491-9

    Figure Lengend Snippet: Nanobody-coated beads agglutinate C. jejuni KC40 cells. The His-tagged nanobodies were coupled to magnetic dynabeads, leading to multimerization. A Nb84 coupled to dynabeads causes agglutination of KC40 cells. B As a negative control, dynabeads coated with anti- E. coli nanobodies were mixed with KC40 cells. No agglutination was observed in this case. C The C. jejuni KC40 bacteria and D the beads coated with Nb84. The results were observed by phase contrast microscopy, using a ×100 oil immersion objective.

    Article Snippet: Multimerization of nanobodies Selected nanobodies were coupled to Co2+ -coated magnetic Dynabeads (Dynabeads® His-Tag Isolation and Pulldown, Thermo Fisher Scientific) to make them multivalent, using the buffers described in the manual.

    Techniques: Agglutination, Negative Control, Microscopy

    Binding of p190RhoGAP to GST-tagged p120 catenin deletion mutants. A , GST-tagged full-length p120 catenin 1A (GST-p120 1A) and related deletion mutants were cotransfected in HEK 293T cells together with His-tagged p190RhoGAP. B , interacting complexes were pulled down with His-tagged Dynabeads, and p120 catenin domains bound to p190RhoGAP were detected by Western blot with anti-GST and anti-p120-catenin antibodies. The bottom panel shows the protein content of recombinant p120-catenin and its deletion mutants in total whole cell lysates ( WCL ). Asterisks indicate the bands corresponding to p120–1A-catenin constructs expressed. MW , molecular weight.

    Journal: The Journal of Biological Chemistry

    Article Title: Interaction of p190RhoGAP with C-terminal Domain of p120-catenin Modulates Endothelial Cytoskeleton and Permeability *

    doi: 10.1074/jbc.M112.432757

    Figure Lengend Snippet: Binding of p190RhoGAP to GST-tagged p120 catenin deletion mutants. A , GST-tagged full-length p120 catenin 1A (GST-p120 1A) and related deletion mutants were cotransfected in HEK 293T cells together with His-tagged p190RhoGAP. B , interacting complexes were pulled down with His-tagged Dynabeads, and p120 catenin domains bound to p190RhoGAP were detected by Western blot with anti-GST and anti-p120-catenin antibodies. The bottom panel shows the protein content of recombinant p120-catenin and its deletion mutants in total whole cell lysates ( WCL ). Asterisks indicate the bands corresponding to p120–1A-catenin constructs expressed. MW , molecular weight.

    Article Snippet: Clarified lysates were then incubated with either glutathione magnetic beads (Thermo Scientific) or His-Tag Dynabeads (Invitrogen) overnight at 4 °C and washed three to four times with TBS-Nonidet P-40 lysis buffer, and the complexes were analyzed by Western blotting using the appropriate antibodies.

    Techniques: Binding Assay, Western Blot, Recombinant, Construct, Molecular Weight

    Identification of the C-terminal polypeptide sequence in p120-catenin responsible for recruitment of p190RhoGAP. GST-tagged full-length p120-catenin 1A (GST-p120 1A), related deletion mutants as well as truncated mutants of p120-catenin created by site specific mutagenesis ( A ) were cotransfected in HEK 293T cells together with His-tagged p190RhoGAP. Interacting complexes were pulled down with His-tagged Dynabeads ( B ), and their content was analyzed by Western blotting using antibodies to the His tag, GST tag, p120-catenin, or p190RhoGAP as indicated. Asterisks in B indicate the bands corresponding to p120-catenin constructs expressed. The bottom panel depicts the protein content of recombinant GST-tagged p120-catenin and its deletion mutants in whole cell lysates ( WCL ).

    Journal: The Journal of Biological Chemistry

    Article Title: Interaction of p190RhoGAP with C-terminal Domain of p120-catenin Modulates Endothelial Cytoskeleton and Permeability *

    doi: 10.1074/jbc.M112.432757

    Figure Lengend Snippet: Identification of the C-terminal polypeptide sequence in p120-catenin responsible for recruitment of p190RhoGAP. GST-tagged full-length p120-catenin 1A (GST-p120 1A), related deletion mutants as well as truncated mutants of p120-catenin created by site specific mutagenesis ( A ) were cotransfected in HEK 293T cells together with His-tagged p190RhoGAP. Interacting complexes were pulled down with His-tagged Dynabeads ( B ), and their content was analyzed by Western blotting using antibodies to the His tag, GST tag, p120-catenin, or p190RhoGAP as indicated. Asterisks in B indicate the bands corresponding to p120-catenin constructs expressed. The bottom panel depicts the protein content of recombinant GST-tagged p120-catenin and its deletion mutants in whole cell lysates ( WCL ).

    Article Snippet: Clarified lysates were then incubated with either glutathione magnetic beads (Thermo Scientific) or His-Tag Dynabeads (Invitrogen) overnight at 4 °C and washed three to four times with TBS-Nonidet P-40 lysis buffer, and the complexes were analyzed by Western blotting using the appropriate antibodies.

    Techniques: Sequencing, Mutagenesis, Western Blot, Construct, Recombinant

    HULC interacts with the glycolytic enzyme PKM2. a Biotinylated HULC and antisense HULC were synthesized by in vitro transcription and incubated with HepG2 cell lysates, respectively. The RNA-protein complexes were isolated with streptavidin-conjugated beads. PKM2 in the pull down was examined by western blotting. Biotinylated antisense HULC was used as the control. b The cellular localizations of HULC and PKM2 were analyzed by RNA-FISH combined with immunofluorescence. Cell nuclei were stained with DAPI, and the scale bar was 20 μm. c Immunoprecipitation of PKM1 and PKM2. The left panel shows the immunoblots of PKM1 and PKM2 in the cell lysate and immunoprecipitates. The right panel shows the agarose gel electrophoresis images of the qRT-PCR products of HULC. LincRNA-p21 was examined as RNA control. d Binding of HULC to flag-tagged exon 9 (PKM1 specific) and exon 10 (PKM2 specific) as determined by the RIP assay. e His-tagged rPKM2 was first immobilized to Dynabeads ® His-tag isolation magnetic beads, and then incubated with in vitro transcribed HULC or antisense HULC. The RNA-protein complexes were isolated, and the levels of HULC were examined by qRT-PCR. Data represent the mean ± s.d. of triplicate independent experiments (*** P

    Journal: Nature Communications

    Article Title: Interactome analysis reveals that lncRNA HULC promotes aerobic glycolysis through LDHA and PKM2

    doi: 10.1038/s41467-020-16966-3

    Figure Lengend Snippet: HULC interacts with the glycolytic enzyme PKM2. a Biotinylated HULC and antisense HULC were synthesized by in vitro transcription and incubated with HepG2 cell lysates, respectively. The RNA-protein complexes were isolated with streptavidin-conjugated beads. PKM2 in the pull down was examined by western blotting. Biotinylated antisense HULC was used as the control. b The cellular localizations of HULC and PKM2 were analyzed by RNA-FISH combined with immunofluorescence. Cell nuclei were stained with DAPI, and the scale bar was 20 μm. c Immunoprecipitation of PKM1 and PKM2. The left panel shows the immunoblots of PKM1 and PKM2 in the cell lysate and immunoprecipitates. The right panel shows the agarose gel electrophoresis images of the qRT-PCR products of HULC. LincRNA-p21 was examined as RNA control. d Binding of HULC to flag-tagged exon 9 (PKM1 specific) and exon 10 (PKM2 specific) as determined by the RIP assay. e His-tagged rPKM2 was first immobilized to Dynabeads ® His-tag isolation magnetic beads, and then incubated with in vitro transcribed HULC or antisense HULC. The RNA-protein complexes were isolated, and the levels of HULC were examined by qRT-PCR. Data represent the mean ± s.d. of triplicate independent experiments (*** P

    Article Snippet: His-tag pull-down assay The His-tagged rPKM2 or rLDHA was incubated with Dynabeads® His-tag isolation magnetic beads (Invitrogen) in binding buffer (50 mM Na3 PO4 , 300 mM NaCl, 0.01% Tween-20, pH = 8.0) at 4 °C for 4 h. Unbound protein was removed, and the protein-coupled beads were incubated with in vitro transcribed HULC RNA for 2 h in a pull-down buffer (3.25 mM Na3 PO4, 70 mM NaCl, 0.01% Tween-20, pH = 7.4) at 4 °C; next, the beads were washed five times with binding buffer supplemented with a protease inhibitor cocktail and RNase inhibitor.

    Techniques: Synthesized, In Vitro, Incubation, Isolation, Western Blot, Fluorescence In Situ Hybridization, Immunofluorescence, Staining, Immunoprecipitation, Agarose Gel Electrophoresis, Quantitative RT-PCR, Binding Assay, Magnetic Beads

    HULC interacts with the glycolytic enzyme LDHA. a Validation of the interaction between LDHA and HULC. Immunoblots of LDHA in the cell lysates and immunoprecipitates of LDHA are shown in the left panel. Agarose gel electrophoresis images of HULC amplified by qRT-PCR are shown in the right panel. LincRNA-p21 was examined as the RNA control. b The cellular localizations of HULC and LDHA were analyzed by combining RNA-FISH and immunofluorescence. Cell nuclei were stained with DAPI, and the scale bar was 20 μm. c Biotinylated HULC was incubated with HepG2 cell lysate and then isolated by streptavidin-conjugated beads. LDHA and LDHB in the cell lysate and RNA pull-down were examined by western blotting. Biotinylated antisense HULC was used as the control. d His-tagged rLDHA or rLDHB was incubated with Dynabeads® His-tag isolation magnetic beads, respectively. Next, in vitro transcribed HULC or antisense HULC was incubated with the beads. Then, the RNA-protein complexes were isolated, and the levels of HULC were examined using qRT-PCR. Data represent the mean ± s.d. of triplicate independent experiments (*** P

    Journal: Nature Communications

    Article Title: Interactome analysis reveals that lncRNA HULC promotes aerobic glycolysis through LDHA and PKM2

    doi: 10.1038/s41467-020-16966-3

    Figure Lengend Snippet: HULC interacts with the glycolytic enzyme LDHA. a Validation of the interaction between LDHA and HULC. Immunoblots of LDHA in the cell lysates and immunoprecipitates of LDHA are shown in the left panel. Agarose gel electrophoresis images of HULC amplified by qRT-PCR are shown in the right panel. LincRNA-p21 was examined as the RNA control. b The cellular localizations of HULC and LDHA were analyzed by combining RNA-FISH and immunofluorescence. Cell nuclei were stained with DAPI, and the scale bar was 20 μm. c Biotinylated HULC was incubated with HepG2 cell lysate and then isolated by streptavidin-conjugated beads. LDHA and LDHB in the cell lysate and RNA pull-down were examined by western blotting. Biotinylated antisense HULC was used as the control. d His-tagged rLDHA or rLDHB was incubated with Dynabeads® His-tag isolation magnetic beads, respectively. Next, in vitro transcribed HULC or antisense HULC was incubated with the beads. Then, the RNA-protein complexes were isolated, and the levels of HULC were examined using qRT-PCR. Data represent the mean ± s.d. of triplicate independent experiments (*** P

    Article Snippet: His-tag pull-down assay The His-tagged rPKM2 or rLDHA was incubated with Dynabeads® His-tag isolation magnetic beads (Invitrogen) in binding buffer (50 mM Na3 PO4 , 300 mM NaCl, 0.01% Tween-20, pH = 8.0) at 4 °C for 4 h. Unbound protein was removed, and the protein-coupled beads were incubated with in vitro transcribed HULC RNA for 2 h in a pull-down buffer (3.25 mM Na3 PO4, 70 mM NaCl, 0.01% Tween-20, pH = 7.4) at 4 °C; next, the beads were washed five times with binding buffer supplemented with a protease inhibitor cocktail and RNase inhibitor.

    Techniques: Western Blot, Agarose Gel Electrophoresis, Amplification, Quantitative RT-PCR, Fluorescence In Situ Hybridization, Immunofluorescence, Staining, Incubation, Isolation, Magnetic Beads, In Vitro