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GE Healthcare polyvinylidene fluoride pvdf
Polyvinylidene Fluoride Pvdf, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/polyvinylidene fluoride pvdf/product/GE Healthcare
Average 92 stars, based on 15 article reviews
Price from $9.99 to $1999.99
polyvinylidene fluoride pvdf - by Bioz Stars, 2020-08
92/100 stars

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Electron Microscopy:

Article Title: Endothelial Transcytotic Machinery Involves Supramolecular Protein-Lipid Complexes
Article Snippet: .. The high performance thin-layer chromatography plates (HPTLC) were bought from EM Science (Gibbstown, NY); other reagents were obtained from the following sources: polyvinylidene difluoride (PVDF) and nitrocellulose membranes (Micron Separations, Westboro, MA); [α-32 P]GTP (Amersham, Arlington Heights, IL); Kodak film X-OMAT-AR (Eastman Kodak, Rochester, NY); all EM grade reagents (Electron Microscopy Science, Forth Washington, PA); m-maleimidobenzoil-N-hydroxisuccinimide ester and sulfo DST (disulfosuccinimidyl tartrate) ( Pierce , Rockford, IL); and lipid markers (Avanti Polar Lipids, Alabaster, AL). ..

Nucleic Acid Electrophoresis:

Article Title: Knockdown of High Mobility Group-Box 3 (HMGB3) Expression Inhibits Proliferation, Reduces Migration, and Affects Chemosensitivity in Gastric Cancer Cells
Article Snippet: .. Proteins were electrophoresed via 10% sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) and transferred onto polyvinylidene fluoride (PVDF) (GE Healthcare, UK). .. The PVDF membranes were blocked with 5% skimmed milk powder for two hours, and then incubated overnight with antibodies against HMGB3 (abcam, UK), BCL-2 (Boster, Wuhan, China), Bax (Boster, Wuhan, China), p53 (Bioss, Beijing, China), p21 (Bioss, Beijing, China), MMP2 (Proteintech, USA), MMP9 (Proteintech, USA), and β-actin (Proteintech, USA).

High Performance Thin Layer Chromatography:

Article Title: Endothelial Transcytotic Machinery Involves Supramolecular Protein-Lipid Complexes
Article Snippet: .. The high performance thin-layer chromatography plates (HPTLC) were bought from EM Science (Gibbstown, NY); other reagents were obtained from the following sources: polyvinylidene difluoride (PVDF) and nitrocellulose membranes (Micron Separations, Westboro, MA); [α-32 P]GTP (Amersham, Arlington Heights, IL); Kodak film X-OMAT-AR (Eastman Kodak, Rochester, NY); all EM grade reagents (Electron Microscopy Science, Forth Washington, PA); m-maleimidobenzoil-N-hydroxisuccinimide ester and sulfo DST (disulfosuccinimidyl tartrate) ( Pierce , Rockford, IL); and lipid markers (Avanti Polar Lipids, Alabaster, AL). ..

other:

Article Title: Syringe-push membrane absorption as a simple rapid method of urine preparation for clinical proteomics
Article Snippet: Three commonly available membranes including nitrocellulose (Bio-Rad Laboratories Inc., Hercules, CA), polyvinylidene difluoride (PVDF) and Whatman no.1 filter membrane (Whatman no.1) were selected for this study.

Migration:

Article Title: Identification of two human nuclear proteins that recognise the cytosine-rich strand of human telomeres in vitro
Article Snippet: .. After a 90 min migration at 15 V/cm the gel was electrotransferred to a polyvinylidene difluoride (PVDF) or nitrocellulose membrane (Amersham). ..

Polyacrylamide Gel Electrophoresis:

Article Title: Knockdown of High Mobility Group-Box 3 (HMGB3) Expression Inhibits Proliferation, Reduces Migration, and Affects Chemosensitivity in Gastric Cancer Cells
Article Snippet: .. Proteins were electrophoresed via 10% sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) and transferred onto polyvinylidene fluoride (PVDF) (GE Healthcare, UK). .. The PVDF membranes were blocked with 5% skimmed milk powder for two hours, and then incubated overnight with antibodies against HMGB3 (abcam, UK), BCL-2 (Boster, Wuhan, China), Bax (Boster, Wuhan, China), p53 (Bioss, Beijing, China), p21 (Bioss, Beijing, China), MMP2 (Proteintech, USA), MMP9 (Proteintech, USA), and β-actin (Proteintech, USA).

Western Blot:

Article Title: Silymarin Accelerates Liver Regeneration after Partial Hepatectomy
Article Snippet: .. Western Blot Analysis Liver extracts (20 μ g) were run on by 12% SDS-PAGE gel for 90 min, at 100 V, and then transferred to polyvinylidene difluoride (PVDF) (Hybond-C Extra Supported, 0.45 μ m; Amersham, Piscataway, NJ, USA) membranes. .. Membranes were blocked in 5% nonfat milk (diluted in Tris-buffered saline and 0.1% Tween 20) for 30 min and probed with the appropriate primary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) against HGF, TGFα , TGFβ 1, cyclin D1, pRb, cyclin E, E2F, cyclin A, and cyclin A at 4°C overnight and then incubated with HRP-conjugated secondary antibody (Promega, Madison, WI, USA).

SDS Page:

Article Title: Silymarin Accelerates Liver Regeneration after Partial Hepatectomy
Article Snippet: .. Western Blot Analysis Liver extracts (20 μ g) were run on by 12% SDS-PAGE gel for 90 min, at 100 V, and then transferred to polyvinylidene difluoride (PVDF) (Hybond-C Extra Supported, 0.45 μ m; Amersham, Piscataway, NJ, USA) membranes. .. Membranes were blocked in 5% nonfat milk (diluted in Tris-buffered saline and 0.1% Tween 20) for 30 min and probed with the appropriate primary antibody (Santa Cruz Biotechnology, Santa Cruz, CA, USA) against HGF, TGFα , TGFβ 1, cyclin D1, pRb, cyclin E, E2F, cyclin A, and cyclin A at 4°C overnight and then incubated with HRP-conjugated secondary antibody (Promega, Madison, WI, USA).

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    GE Healthcare pvdf membranes
    Time course of Klotho-mediated phosphorylation of endogenous 14-3-3ζ (Ser-58) effect on 14-3-3ζ monomer levels in HEK 293 cells. (A) Plot describing time-dependent 14-3-3ζ phosphorylation mediated by Klotho was demonstrated by adding 200 pM of the recombinant protein to the cultured cells at the indicated times. Peak phosphorylation times (i.e. 30–45 min) are within the range where the <t>Trx/ASK1</t> complex protection against oxidative stress occurred ( Fig 1 ). Data are reported as ± SEM. (B) Plot of 14-3-3ζ monomer level in HEK 293 cells treated with either secreted Klotho or buffer control for 40 min. Shown beside plot is a native Western blot of the samples as described in Materials and Methods. The 14-3-3ζ antibody recognizes a predominant ~30 k Da protein band representing the expected size of the monomer. Replicate samples were separated under SDS-PAGE, electroblotted onto <t>PVDF</t> membrane and probed with same antibody to account for lysate levels of total 14-3-3ζ. Digitized values of the WB of monomer levels are shown in S3 Table .
    Pvdf Membranes, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 2482 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pvdf membranes/product/GE Healthcare
    Average 92 stars, based on 2482 article reviews
    Price from $9.99 to $1999.99
    pvdf membranes - by Bioz Stars, 2020-08
    92/100 stars
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    Time course of Klotho-mediated phosphorylation of endogenous 14-3-3ζ (Ser-58) effect on 14-3-3ζ monomer levels in HEK 293 cells. (A) Plot describing time-dependent 14-3-3ζ phosphorylation mediated by Klotho was demonstrated by adding 200 pM of the recombinant protein to the cultured cells at the indicated times. Peak phosphorylation times (i.e. 30–45 min) are within the range where the Trx/ASK1 complex protection against oxidative stress occurred ( Fig 1 ). Data are reported as ± SEM. (B) Plot of 14-3-3ζ monomer level in HEK 293 cells treated with either secreted Klotho or buffer control for 40 min. Shown beside plot is a native Western blot of the samples as described in Materials and Methods. The 14-3-3ζ antibody recognizes a predominant ~30 k Da protein band representing the expected size of the monomer. Replicate samples were separated under SDS-PAGE, electroblotted onto PVDF membrane and probed with same antibody to account for lysate levels of total 14-3-3ζ. Digitized values of the WB of monomer levels are shown in S3 Table .

    Journal: PLoS ONE

    Article Title: Klotho Regulates 14-3-3ζ Monomerization and Binding to the ASK1 Signaling Complex in Response to Oxidative Stress

    doi: 10.1371/journal.pone.0141968

    Figure Lengend Snippet: Time course of Klotho-mediated phosphorylation of endogenous 14-3-3ζ (Ser-58) effect on 14-3-3ζ monomer levels in HEK 293 cells. (A) Plot describing time-dependent 14-3-3ζ phosphorylation mediated by Klotho was demonstrated by adding 200 pM of the recombinant protein to the cultured cells at the indicated times. Peak phosphorylation times (i.e. 30–45 min) are within the range where the Trx/ASK1 complex protection against oxidative stress occurred ( Fig 1 ). Data are reported as ± SEM. (B) Plot of 14-3-3ζ monomer level in HEK 293 cells treated with either secreted Klotho or buffer control for 40 min. Shown beside plot is a native Western blot of the samples as described in Materials and Methods. The 14-3-3ζ antibody recognizes a predominant ~30 k Da protein band representing the expected size of the monomer. Replicate samples were separated under SDS-PAGE, electroblotted onto PVDF membrane and probed with same antibody to account for lysate levels of total 14-3-3ζ. Digitized values of the WB of monomer levels are shown in S3 Table .

    Article Snippet: Resolved proteins were Western transferred onto PVDF membranes and probed with Trx, ASK1, or 14-3-3ζ antibodies as described above.

    Techniques: Recombinant, Cell Culture, Western Blot, SDS Page

    Gel filtration analysis of the interaction between Photofrin and recombinant procaspase-3-D 3 A. Recombinant procaspase-3-D 3 A alone (1 mg), Photofrin alone (18.13 μ g) or recombinant procaspase-3-D 3 A (1 mg) plus Photofrin (18.13 μ g) (molar ratio 1 : 1) were applied to Superose 12 columns for gel filtration analysis, as described. ( a ) Each fraction was subjected to optical density measurement (280 nm) for procaspase-3-D 3 A proteins and fluorescence measurement (excitation 400 nm and emission 630 nm) for Photofrin. ( b ) Fractions were also directly spotted onto a PVDF membrane, and procaspase-3-D 3 A and Photofrin signals were detected by immunoblotting and fluorescence scanning (Typhoon 9400), respectively. ( c ) Procaspase-3-D 3 A, bovine serum albumin (BSA), ovalbumin, casein (10 μ g of each protein) or Photofrin (5 μ g) were spotted onto a PVDF membrane. The membrane was incubated with Photofrin-containing solution (100 μ g in 10 ml distilled water) at room temperature in the dark for 3 h, washed thrice for 10 min with distilled water and thrice for 10 min with TTBS buffer (20 mM Tris-HCl, pH 7.4, 0.5 M NaCl, and 0.05% Tween 20). The washed membrane was air-dried and then scanned by a Typhoon 9400 fluorescence scanner

    Journal: Cell Death & Disease

    Article Title: Photofrin binds to procaspase-3 and mediates photodynamic treatment-triggered methionine oxidation and inactivation of procaspase-3

    doi: 10.1038/cddis.2012.85

    Figure Lengend Snippet: Gel filtration analysis of the interaction between Photofrin and recombinant procaspase-3-D 3 A. Recombinant procaspase-3-D 3 A alone (1 mg), Photofrin alone (18.13 μ g) or recombinant procaspase-3-D 3 A (1 mg) plus Photofrin (18.13 μ g) (molar ratio 1 : 1) were applied to Superose 12 columns for gel filtration analysis, as described. ( a ) Each fraction was subjected to optical density measurement (280 nm) for procaspase-3-D 3 A proteins and fluorescence measurement (excitation 400 nm and emission 630 nm) for Photofrin. ( b ) Fractions were also directly spotted onto a PVDF membrane, and procaspase-3-D 3 A and Photofrin signals were detected by immunoblotting and fluorescence scanning (Typhoon 9400), respectively. ( c ) Procaspase-3-D 3 A, bovine serum albumin (BSA), ovalbumin, casein (10 μ g of each protein) or Photofrin (5 μ g) were spotted onto a PVDF membrane. The membrane was incubated with Photofrin-containing solution (100 μ g in 10 ml distilled water) at room temperature in the dark for 3 h, washed thrice for 10 min with distilled water and thrice for 10 min with TTBS buffer (20 mM Tris-HCl, pH 7.4, 0.5 M NaCl, and 0.05% Tween 20). The washed membrane was air-dried and then scanned by a Typhoon 9400 fluorescence scanner

    Article Snippet: Fractions were also directly spotted onto PVDF membranes, and procaspase-3-D3 A and Photofrin signals were detected by immunoblotting and fluorescence scanning (Typhoon 9400; GE Healthcare), respectively.

    Techniques: Filtration, Recombinant, Fluorescence, Incubation

    Galectin-1 (Gal-1)-induced phosphorylation of c-Jun N-terminal kinase 1 (JNK1) and JNK2 ( a ) and JNK activation with c-Jun(1-169)-GST ( b ), and c-Jun(1-89)-GST ( c ) as kinase substrates. Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with protein kinase C-θ (PKCθ) inhibitor and PKCδ inhibitor rottlerin for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, as well as with the ATP-competitive inhibitor for JNK SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) myricetin for 30 min as indicated. Control cells were incubated in medium alone. Cells were then stimulated with gal-1 without and in the presence of lactose or asialofetuin as indicated in panels a , b , and c . ( a ) For immunoblot analysis cell extract proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Blots were analyzed with a phospho-JNK (Thr183/Tyr185) monoclonal antibody (mAb). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. ( b ) After termination of the kinase reactions with 3 × SDS sample buffer, samples were electrophoretically separated and blotted on PVDF membranes. The [ 32 P]-labeled substrate c-Jun(1-169)-GST was recorded by autoradiography. To control loading, we separated 50 μ g cell extract protein/lane and blotted it on PVDF membranes. Membranes were probed with a JNK1 polyclonal antibody (pAb). ( c ) After termination of the kinase reactions, samples were separated and blotted on Hybond ECL membranes. Blots were analyzed for substrate phosphorylation with a phospho-c-Jun (Ser63) pAb. The bands were luminographically visualized on X-ray films using ECL Plus reagents. Shown are representative blots from three independent experiments

    Journal: Cell Death & Disease

    Article Title: Role of the JNK/c-Jun/AP-1 signaling pathway in galectin-1-induced T-cell death

    doi: 10.1038/cddis.2010.1

    Figure Lengend Snippet: Galectin-1 (Gal-1)-induced phosphorylation of c-Jun N-terminal kinase 1 (JNK1) and JNK2 ( a ) and JNK activation with c-Jun(1-169)-GST ( b ), and c-Jun(1-89)-GST ( c ) as kinase substrates. Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with protein kinase C-θ (PKCθ) inhibitor and PKCδ inhibitor rottlerin for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, as well as with the ATP-competitive inhibitor for JNK SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) myricetin for 30 min as indicated. Control cells were incubated in medium alone. Cells were then stimulated with gal-1 without and in the presence of lactose or asialofetuin as indicated in panels a , b , and c . ( a ) For immunoblot analysis cell extract proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Blots were analyzed with a phospho-JNK (Thr183/Tyr185) monoclonal antibody (mAb). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. ( b ) After termination of the kinase reactions with 3 × SDS sample buffer, samples were electrophoretically separated and blotted on PVDF membranes. The [ 32 P]-labeled substrate c-Jun(1-169)-GST was recorded by autoradiography. To control loading, we separated 50 μ g cell extract protein/lane and blotted it on PVDF membranes. Membranes were probed with a JNK1 polyclonal antibody (pAb). ( c ) After termination of the kinase reactions, samples were separated and blotted on Hybond ECL membranes. Blots were analyzed for substrate phosphorylation with a phospho-c-Jun (Ser63) pAb. The bands were luminographically visualized on X-ray films using ECL Plus reagents. Shown are representative blots from three independent experiments

    Article Snippet: Fetal calf serum (FCS), kanamycin, RPMI 1640 medium were from Gibco BRL (Eggenstein, Germany), enhanced chemiluminescence (ECL) detection reagents, Hybond ECL nitrocellulose membranes, protein G agarose, PVDF membranes, and [γ -32 P]ATP were from GE Healthcare Europe (Freiburg, Germany).

    Techniques: Activation Assay, Incubation, Polyacrylamide Gel Electrophoresis, SDS Page, Expressing, Labeling, Autoradiography

    QseF is phosphorylated in vivo at Asp56 in the receiver domain and at an additional site in the C-terminus. A . Schematic representation of C-terminally Strep-tagged QseF and the various truncations used for metabolic labeling and StrepTactin pull-down. QseF comprises an N-terminal receiver domain, a σ 54 interaction domain and C-terminal helix-turn-helix (H-T-H) DNA-binding domain. Location of the conserved D56 phosphorylation site in the receiver domain is indicated by a black dot. B . StrepTactin pull-down assay of truncated QseF variants following metabolic [ 32 P] labeling. Strain Z196 (Δ qseF ) was employed, which harbored the following plasmids encoding the Strep-tagged QseF variants given in parentheses, respectively: pYG278 (FL = full-length QseF), pYG278-D56A (FL-D56A = full-length QseF with D56A exchange), pYG279 (NTD), pYG279-D56A (NTD-D56A) and pYG280 (CTD). Induction of synthesis of recombinant proteins following addition of IPTG was checked by separation of total protein extracts by SDS-PAGE and subsequent Coomassie blue staining (left panel). Cells were labelled with [ 32 P] and Strep-tagged proteins were isolated by pull-down and subsequently analyzed by Western Blotting using an antibody directed against the Strep-tag (middle panel) and by autoradiography (right panel). C . Western blot addressing the nature of the phosphorylation of the QseF-CTD. Three μg each of the purified Strep-tagged proteins indicated in the figure were separated by 15% SDS-PAGE and analyzed by Coomassie blue staining (top) and Western blotting (middle and bottom) using a phospho-threonine specific antibody. In the bottom panel the PVDF membrane was treated with 10 units alkaline phosphatase in FastAP buffer (ThermoFisher Scientific) for 60 minutes at 37°C before the α-phospho-threonine antibody was applied.

    Journal: PLoS Genetics

    Article Title: Interaction of lipoprotein QseG with sensor kinase QseE in the periplasm controls the phosphorylation state of the two-component system QseE/QseF in Escherichia coli

    doi: 10.1371/journal.pgen.1007547

    Figure Lengend Snippet: QseF is phosphorylated in vivo at Asp56 in the receiver domain and at an additional site in the C-terminus. A . Schematic representation of C-terminally Strep-tagged QseF and the various truncations used for metabolic labeling and StrepTactin pull-down. QseF comprises an N-terminal receiver domain, a σ 54 interaction domain and C-terminal helix-turn-helix (H-T-H) DNA-binding domain. Location of the conserved D56 phosphorylation site in the receiver domain is indicated by a black dot. B . StrepTactin pull-down assay of truncated QseF variants following metabolic [ 32 P] labeling. Strain Z196 (Δ qseF ) was employed, which harbored the following plasmids encoding the Strep-tagged QseF variants given in parentheses, respectively: pYG278 (FL = full-length QseF), pYG278-D56A (FL-D56A = full-length QseF with D56A exchange), pYG279 (NTD), pYG279-D56A (NTD-D56A) and pYG280 (CTD). Induction of synthesis of recombinant proteins following addition of IPTG was checked by separation of total protein extracts by SDS-PAGE and subsequent Coomassie blue staining (left panel). Cells were labelled with [ 32 P] and Strep-tagged proteins were isolated by pull-down and subsequently analyzed by Western Blotting using an antibody directed against the Strep-tag (middle panel) and by autoradiography (right panel). C . Western blot addressing the nature of the phosphorylation of the QseF-CTD. Three μg each of the purified Strep-tagged proteins indicated in the figure were separated by 15% SDS-PAGE and analyzed by Coomassie blue staining (top) and Western blotting (middle and bottom) using a phospho-threonine specific antibody. In the bottom panel the PVDF membrane was treated with 10 units alkaline phosphatase in FastAP buffer (ThermoFisher Scientific) for 60 minutes at 37°C before the α-phospho-threonine antibody was applied.

    Article Snippet: Proteins were separated on 12.5–15% SDS PAA gels and blotted onto a polyvinylidene difluoride (PVDF) membrane (GE Healthcare) by semi-dry blotting for 60–120 min at 2.0 mA/cm2 .

    Techniques: In Vivo, Labeling, Binding Assay, Pull Down Assay, Recombinant, SDS Page, Staining, Isolation, Western Blot, Strep-tag, Autoradiography, Purification