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PerkinElmer polyvinylidene difluoride pvdf membrane
Polyvinylidene Difluoride Pvdf Membrane, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 94/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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polyvinylidene difluoride pvdf membrane - by Bioz Stars, 2020-12
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Centrifugation:

Article Title: GATA-3 regulates the homeostasis and activation of CD8+ T cells 1
Article Snippet: .. Cell lysate was separated from debris by centrifugation at 12,000 rpm for 10 min. Lysate was loaded onto 9% polyacrylamide gels and transferred onto PVDF membrane (Polyscreen; Perkin Elmer). .. Anti-ERK2 (C-14), anti-JNK (F-3), anti-p38α (C-20), anti-Lat (11B.12), and anti-Hsp90 were purchased from Santa Cruz Biotechnology, Santa Cruz, CA.

Electrophoresis:

Article Title: Neurogenin3 Cooperates with Foxa2 to Autoactivate Its Own Expression *
Article Snippet: .. 50 μg of whole cell extracts or immunoprecipitates were separated by PAGE-SDS electrophoresis, transferred to a Polyscreen PVDF membrane (Perkin Elmer, Waltham, MA) and incubated overnight at 4 °C with goat anti-mouse Foxa2 (1:1000, Santa Cruz Biotechnology), mouse anti-HA (1:1000, Sigma) or beta actin (1:1000, Sigma). .. Blots were visualized with ECL Reagent (Pierce Biotechnology) using a LAS4000 Lumi-Imager (Fuji Photo Film, Valhalla, NY).

Incubation:

Article Title: Neurogenin3 Cooperates with Foxa2 to Autoactivate Its Own Expression *
Article Snippet: .. 50 μg of whole cell extracts or immunoprecipitates were separated by PAGE-SDS electrophoresis, transferred to a Polyscreen PVDF membrane (Perkin Elmer, Waltham, MA) and incubated overnight at 4 °C with goat anti-mouse Foxa2 (1:1000, Santa Cruz Biotechnology), mouse anti-HA (1:1000, Sigma) or beta actin (1:1000, Sigma). .. Blots were visualized with ECL Reagent (Pierce Biotechnology) using a LAS4000 Lumi-Imager (Fuji Photo Film, Valhalla, NY).

Polyacrylamide Gel Electrophoresis:

Article Title: Neurogenin3 Cooperates with Foxa2 to Autoactivate Its Own Expression *
Article Snippet: .. 50 μg of whole cell extracts or immunoprecipitates were separated by PAGE-SDS electrophoresis, transferred to a Polyscreen PVDF membrane (Perkin Elmer, Waltham, MA) and incubated overnight at 4 °C with goat anti-mouse Foxa2 (1:1000, Santa Cruz Biotechnology), mouse anti-HA (1:1000, Sigma) or beta actin (1:1000, Sigma). .. Blots were visualized with ECL Reagent (Pierce Biotechnology) using a LAS4000 Lumi-Imager (Fuji Photo Film, Valhalla, NY).

Western Blot:

Article Title: Bisected, complex N-glycans and galectins in mouse mammary tumor progression and human breast cancer
Article Snippet: .. Proteins were transferred to a Polyscreen polyvinylidene difluoride (PVDF) membrane (PerkinElmer, Waltham, MA) in Tris-glycine buffer containing 5% methanol, and western blot analysis was conducted as described previously ( ). .. Briefly, membranes were blocked in blocking buffer Tris-buffered saline and Tween 20 (TBS-T) (25 mM Tris–HCl, 150 mM NaCl, 0.05% Tween 20, pH 7.5) with either 3% bovine serum albumin (BSA) (for signaling molecules) or 3% nonfat dry milk (for all other antibodies) for over 1 h, and then incubated with primary antibody diluted in 3% Cold Fish Gelatin, 1% BSA, 0.001% Thimerosal/TBS-T at room temperature for 1–3 h. After washing with TBS-T, membranes were incubated with HRP-conjugated secondary antibody diluted in the appropriate blocking buffer for 1 h. After washing with TBS-T, bands were visualized using an enhanced chemiluminescence (ECL) kit (Thermo Scientific) and exposed to film (Denville scientific, South Plainfield, NJ) and scanned or imaged with Fujifilm LAS-3000 (Valhalla, NY).

SDS Page:

Article Title: Angiotensin II directly regulates intestinal epithelial NHE3 in Caco2BBE cells
Article Snippet: .. Total cellular protein (35 μg) or IP samples were separated on 7.5% SDS-PAGE and immediately transferred to PVDF membranes (Polyscreen, Perkin Elmer Life Sciences, Boston, MA) in 1× Towbin's buffer (25 mM Tris, 192 mM glycine, pH 8.8 with 15% vol/vol methanol). ..

Article Title: Mutation G827R in Matriptase Causing Autosomal Recessive Ichthyosis with Hypotrichosis Yields an Inactive Protease *
Article Snippet: .. Proteins were then separated by SDS-PAGE on 12% polyacrylamide gels and transferred to Polyscreen polyvinylidene difluoride membranes (PerkinElmer Life Sciences). .. Matriptase was detected using polyclonal rabbit anti-human matriptase antibody (Bethyl Laboratories, Montgomery, TX) and horseradish peroxidase-coupled donkey anti-rabbit antibody (GE Healthcare).

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  • 94
    PerkinElmer pvdf membrane
    KMTs interact with their substrate. SETDB1 interacts with ING2. (A) FLAG-purified ING2 complex from a stably expressing cell line was probed for the presence of SETDB1. The SETDB1 antibody detected the presence of the endogenous enzyme only in the ING2 complex, but not in the control lane. (B) HEK-293T cells were transfected with an empty vector or 2 independent clones of HA-SETDB1 in the absence or presence of FLAG-ING2. The cells were lysed and proteins immunoprecipitated using FLAG-M2 agarose. The samples were separated by <t>SDS-PAGE,</t> transferred to <t>PVDF</t> and analysed with either α-HA or α-FLAG M2-HRP antibodies. (C) ING2 is methylated in vitro by SETDB1. Recombinant SETDB1 purified from insect cells was incubated alone or with either GST or GST-ING2 in the presence of 3 H-SA M. Autoradiography of the experiment (left) and Coomassie staining of the gel (right). The arrow indicates GST-ING2. The two stars (**) indicate SETDB1 and its auto-methylated forms. (D) HP1α is methylated in vitro by SUV39H1. Autoradiography of an enzymatic reaction using bacterially expressed recombinant SUV39H1 and HP1α. In the first lane, only the KMT is present. In the second lane, GST was used as a negative control for SUV39H1 methylation. In the last lane, both SUV39H1 and HP1α were incubated. The arrow indicates HP1α.
    Pvdf Membrane, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 94/100, based on 218 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pvdf membrane/product/PerkinElmer
    Average 94 stars, based on 218 article reviews
    Price from $9.99 to $1999.99
    pvdf membrane - by Bioz Stars, 2020-12
    94/100 stars
      Buy from Supplier

    92
    PerkinElmer pvdf co hfp membrane
    ( a ) Comparative investigation on the absorbed levels of liquid electrolyte into (1) commercially available polypropylene (PP) separator and as-electrospun cross-linked <t>PVDF-</t> co <t>-HFP</t> separators with the two different thicknesses of (2) 40 μm and (3) 100 μm for 10 s, ( b ) a photo image representing a structural robust and stretchable PVDF- co -HFP GPE encapsulating 1 M LiPF 6 in EC: DMC, and ( c ) electrochemical impedance spectra (EIS) results of the PVDF- co -HFP GPE used in the stainless steel (SS)/GPE/SS cell.
    Pvdf Co Hfp Membrane, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pvdf co hfp membrane/product/PerkinElmer
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    pvdf co hfp membrane - by Bioz Stars, 2020-12
    92/100 stars
      Buy from Supplier

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    KMTs interact with their substrate. SETDB1 interacts with ING2. (A) FLAG-purified ING2 complex from a stably expressing cell line was probed for the presence of SETDB1. The SETDB1 antibody detected the presence of the endogenous enzyme only in the ING2 complex, but not in the control lane. (B) HEK-293T cells were transfected with an empty vector or 2 independent clones of HA-SETDB1 in the absence or presence of FLAG-ING2. The cells were lysed and proteins immunoprecipitated using FLAG-M2 agarose. The samples were separated by SDS-PAGE, transferred to PVDF and analysed with either α-HA or α-FLAG M2-HRP antibodies. (C) ING2 is methylated in vitro by SETDB1. Recombinant SETDB1 purified from insect cells was incubated alone or with either GST or GST-ING2 in the presence of 3 H-SA M. Autoradiography of the experiment (left) and Coomassie staining of the gel (right). The arrow indicates GST-ING2. The two stars (**) indicate SETDB1 and its auto-methylated forms. (D) HP1α is methylated in vitro by SUV39H1. Autoradiography of an enzymatic reaction using bacterially expressed recombinant SUV39H1 and HP1α. In the first lane, only the KMT is present. In the second lane, GST was used as a negative control for SUV39H1 methylation. In the last lane, both SUV39H1 and HP1α were incubated. The arrow indicates HP1α.

    Journal: Epigenetics

    Article Title: Trimethylation of histone H3 lysine 4 impairs methylation of histone H3 lysine 9

    doi: 10.4161/epi.5.8.13278

    Figure Lengend Snippet: KMTs interact with their substrate. SETDB1 interacts with ING2. (A) FLAG-purified ING2 complex from a stably expressing cell line was probed for the presence of SETDB1. The SETDB1 antibody detected the presence of the endogenous enzyme only in the ING2 complex, but not in the control lane. (B) HEK-293T cells were transfected with an empty vector or 2 independent clones of HA-SETDB1 in the absence or presence of FLAG-ING2. The cells were lysed and proteins immunoprecipitated using FLAG-M2 agarose. The samples were separated by SDS-PAGE, transferred to PVDF and analysed with either α-HA or α-FLAG M2-HRP antibodies. (C) ING2 is methylated in vitro by SETDB1. Recombinant SETDB1 purified from insect cells was incubated alone or with either GST or GST-ING2 in the presence of 3 H-SA M. Autoradiography of the experiment (left) and Coomassie staining of the gel (right). The arrow indicates GST-ING2. The two stars (**) indicate SETDB1 and its auto-methylated forms. (D) HP1α is methylated in vitro by SUV39H1. Autoradiography of an enzymatic reaction using bacterially expressed recombinant SUV39H1 and HP1α. In the first lane, only the KMT is present. In the second lane, GST was used as a negative control for SUV39H1 methylation. In the last lane, both SUV39H1 and HP1α were incubated. The arrow indicates HP1α.

    Article Snippet: Then, the samples separated by SDS-PAGE, transferred to PVDF membrane, which were then dried and sprayed with En3Hance (Perkin Elmer) prior to autoradiography.

    Techniques: Purification, Stable Transfection, Expressing, Transfection, Plasmid Preparation, Clone Assay, Immunoprecipitation, SDS Page, Methylation, In Vitro, Recombinant, Incubation, Autoradiography, Staining, Negative Control

    Determination of transporter protein expression in human liver lysates. (A) GFP‐fusion proteins of each of the five transporters that were studied were prepared in HEK293FT cells, as described in Materials and Methods. SDS‐PAGE of aliquots of each of the HEK293FT lysates was performed, transferred to PVDF membrane, and subjected to western blot using GFP antibody. In this representative experiment of three that were performed, the amount (µg) of cell lysate protein applied to the gel was adjusted to provide similar intensities for each of the GFP‐transporter fusion proteins, as indicated. Relative expression of GFP‐OATPs was obtained by densitometry, and the means ± SD of the three experiments are indicated in the figure. (B) In these representative western blots, lysates of liver samples from 3 patients as well as appropriate calibrated HEK293FT lysates containing approximately equal amounts of GFP‐transporter fusion proteins were subjected to SDS‐PAGE followed by western blots, using specific transporter antibodies as indicated.

    Journal: Hepatology Communications

    Article Title: Interindividual Diversity in Expression of Organic Anion Uptake Transporters in Normal and Cirrhotic Human Liver

    doi: 10.1002/hep4.1489

    Figure Lengend Snippet: Determination of transporter protein expression in human liver lysates. (A) GFP‐fusion proteins of each of the five transporters that were studied were prepared in HEK293FT cells, as described in Materials and Methods. SDS‐PAGE of aliquots of each of the HEK293FT lysates was performed, transferred to PVDF membrane, and subjected to western blot using GFP antibody. In this representative experiment of three that were performed, the amount (µg) of cell lysate protein applied to the gel was adjusted to provide similar intensities for each of the GFP‐transporter fusion proteins, as indicated. Relative expression of GFP‐OATPs was obtained by densitometry, and the means ± SD of the three experiments are indicated in the figure. (B) In these representative western blots, lysates of liver samples from 3 patients as well as appropriate calibrated HEK293FT lysates containing approximately equal amounts of GFP‐transporter fusion proteins were subjected to SDS‐PAGE followed by western blots, using specific transporter antibodies as indicated.

    Article Snippet: Western Blot Analysis Western blot was performed as described. ( ) In brief, tissue lysates (30 µg protein) were subjected to sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) under reducing conditions (100 mM dithiothreitol) and transferred to a polyvinylidene difluoride (PVDF) membrane (Perkin Elmer, Boston, MA).

    Techniques: Expressing, SDS Page, Western Blot

    Inhibitory effects of xenoestrogens panel on a broad set of arginine methyltransferases A ) In vitro . GST of PRMT1, PRMT3 and PRMT6 were incubated with GST-Npl3 and GST-GAR as substrates. GST-CARM1 was incubated with GST-PABP1 and purified calf thymus histone H3 as substrates. GST-SET7/9 was incubated with purified calf thymus histone H3 as substrate. Substrates (0.5 µg) were incubated with recombinant enzymes (0.2 µg) in the presence of 0.5 µM [ 3 H] AdoMet and the indicated xenoestrogen (5 µg) for 90 min at 30°C in the final volume of 30 µl of PBS. Reactions were separated by SDS-PAGE, transferred to a PVDF membrane, sprayed with Enhance™ (NEN) and exposed to film overnight (top panel). A control reaction was performed in the presence of DMSO (the xenoestrogens solvent) at 3.3% v/v. B ) The table shows the inhibitory ability of each xenoestrogen on the indicated enzymes. The number beside each xenoestrogen represents its lane in the fluorograph above. Strong (•••) weak (•) inhibition.

    Journal: Chembiochem

    Article Title: Xenoestrogens Regulate the Activity of Arginine Methyltransferases

    doi: 10.1002/cbic.201000522

    Figure Lengend Snippet: Inhibitory effects of xenoestrogens panel on a broad set of arginine methyltransferases A ) In vitro . GST of PRMT1, PRMT3 and PRMT6 were incubated with GST-Npl3 and GST-GAR as substrates. GST-CARM1 was incubated with GST-PABP1 and purified calf thymus histone H3 as substrates. GST-SET7/9 was incubated with purified calf thymus histone H3 as substrate. Substrates (0.5 µg) were incubated with recombinant enzymes (0.2 µg) in the presence of 0.5 µM [ 3 H] AdoMet and the indicated xenoestrogen (5 µg) for 90 min at 30°C in the final volume of 30 µl of PBS. Reactions were separated by SDS-PAGE, transferred to a PVDF membrane, sprayed with Enhance™ (NEN) and exposed to film overnight (top panel). A control reaction was performed in the presence of DMSO (the xenoestrogens solvent) at 3.3% v/v. B ) The table shows the inhibitory ability of each xenoestrogen on the indicated enzymes. The number beside each xenoestrogen represents its lane in the fluorograph above. Strong (•••) weak (•) inhibition.

    Article Snippet: The reaction was incubated at 30°C for 90 min and then separated by SDS/PAGE, transferred to a PVDF membrane, sprayed with Enhance™ (PerkinElmer Life Sciences), and exposed to film overnight for fluorograph.

    Techniques: In Vitro, Incubation, Purification, Recombinant, SDS Page, Inhibition

    Xenoestrogens are selective PRMT inhibitors In vitro methylation reactions were performed with recombinant GST fused arginine methyltransferases and a set of different substrates, in the presence of indicated xenoestrogens. GST-CARM1 was incubated with GSTPABP, GST-SMB, GST-CA150 and calf thymus histone H3 as substrate, respectively. GST-PRMT1 was incubated with GST-NPL3 and histone H4 as substrates. GST-PRMT3 was incubated with GST-NPL3 and GST-rpS2 as substrates. GST-PRMT6 was incubated with GST-NPL3 and histone H3 as substrates. Myc-tag PRMT5 purified from CARM1 null cells was incubated with MBP and histone H4 as substrates. Substrates (0.5 µg) were incubated with recombinant enzymes (0.2 µg) in the presence of 0.5 µM [3H] AdoMet and the indicated xenoestrogens (200 µM) for 90 min at 30°C in the final volume of 30 µl of PBS. Reactions were separated by SDS-PAGE, transferred to a PVDF membrane, sprayed with Enhance™ (NEN) and exposed to film overnight. The fluorographs are shown in the left panel, and the scintillation counts (dpm) of methylation levels are depicted in the right panel. A control reaction was performed in the presence of DMSO (the xenoestrogens solvent) at 3.3% v/v.

    Journal: Chembiochem

    Article Title: Xenoestrogens Regulate the Activity of Arginine Methyltransferases

    doi: 10.1002/cbic.201000522

    Figure Lengend Snippet: Xenoestrogens are selective PRMT inhibitors In vitro methylation reactions were performed with recombinant GST fused arginine methyltransferases and a set of different substrates, in the presence of indicated xenoestrogens. GST-CARM1 was incubated with GSTPABP, GST-SMB, GST-CA150 and calf thymus histone H3 as substrate, respectively. GST-PRMT1 was incubated with GST-NPL3 and histone H4 as substrates. GST-PRMT3 was incubated with GST-NPL3 and GST-rpS2 as substrates. GST-PRMT6 was incubated with GST-NPL3 and histone H3 as substrates. Myc-tag PRMT5 purified from CARM1 null cells was incubated with MBP and histone H4 as substrates. Substrates (0.5 µg) were incubated with recombinant enzymes (0.2 µg) in the presence of 0.5 µM [3H] AdoMet and the indicated xenoestrogens (200 µM) for 90 min at 30°C in the final volume of 30 µl of PBS. Reactions were separated by SDS-PAGE, transferred to a PVDF membrane, sprayed with Enhance™ (NEN) and exposed to film overnight. The fluorographs are shown in the left panel, and the scintillation counts (dpm) of methylation levels are depicted in the right panel. A control reaction was performed in the presence of DMSO (the xenoestrogens solvent) at 3.3% v/v.

    Article Snippet: The reaction was incubated at 30°C for 90 min and then separated by SDS/PAGE, transferred to a PVDF membrane, sprayed with Enhance™ (PerkinElmer Life Sciences), and exposed to film overnight for fluorograph.

    Techniques: In Vitro, Methylation, Recombinant, Incubation, Purification, SDS Page

    Inhibitory effects of chalcones on a set of methyltransferases A ) The structural relationship between AMI-18 and chalcones is depicted. B ) In vitro methylation reactions were performed with recombinant enzymes on different substrates (enzyme/substrate). Substrates (0.5 µg) were incubated with recombinant enzymes (0.2 µg) in the presence of 0.5 µM [ 3 H] AdoMet and the indicated xenoestrogen (5 µg) for 90 min at 30°C in the final volume of 30 µl of PBS. Reactions were separated by SDS-PAGE, transferred to a PVDF membrane, sprayed with Enhance™ (NEN) and exposed to film overnight. A control reaction was performed in the presence of DMSO (the xenoestrogens solvent) at 3.3% v/v. PRMT1, PRMT3 and CARM1 are arginine methyltransferases. SET7/9 is a lysine methyltransferase. NPL3, PABP1 and histone H3 are the enzyme substrates.

    Journal: Chembiochem

    Article Title: Xenoestrogens Regulate the Activity of Arginine Methyltransferases

    doi: 10.1002/cbic.201000522

    Figure Lengend Snippet: Inhibitory effects of chalcones on a set of methyltransferases A ) The structural relationship between AMI-18 and chalcones is depicted. B ) In vitro methylation reactions were performed with recombinant enzymes on different substrates (enzyme/substrate). Substrates (0.5 µg) were incubated with recombinant enzymes (0.2 µg) in the presence of 0.5 µM [ 3 H] AdoMet and the indicated xenoestrogen (5 µg) for 90 min at 30°C in the final volume of 30 µl of PBS. Reactions were separated by SDS-PAGE, transferred to a PVDF membrane, sprayed with Enhance™ (NEN) and exposed to film overnight. A control reaction was performed in the presence of DMSO (the xenoestrogens solvent) at 3.3% v/v. PRMT1, PRMT3 and CARM1 are arginine methyltransferases. SET7/9 is a lysine methyltransferase. NPL3, PABP1 and histone H3 are the enzyme substrates.

    Article Snippet: The reaction was incubated at 30°C for 90 min and then separated by SDS/PAGE, transferred to a PVDF membrane, sprayed with Enhance™ (PerkinElmer Life Sciences), and exposed to film overnight for fluorograph.

    Techniques: In Vitro, Methylation, Recombinant, Incubation, SDS Page

    ( a ) Comparative investigation on the absorbed levels of liquid electrolyte into (1) commercially available polypropylene (PP) separator and as-electrospun cross-linked PVDF- co -HFP separators with the two different thicknesses of (2) 40 μm and (3) 100 μm for 10 s, ( b ) a photo image representing a structural robust and stretchable PVDF- co -HFP GPE encapsulating 1 M LiPF 6 in EC: DMC, and ( c ) electrochemical impedance spectra (EIS) results of the PVDF- co -HFP GPE used in the stainless steel (SS)/GPE/SS cell.

    Journal: Materials

    Article Title: Cross-Linked Poly(vinylidene fluoride-co-hexafluoropropene) (PVDF-co-HFP) Gel Polymer Electrolyte for Flexible Li-Ion Battery Integrated with Organic Light Emitting Diode (OLED)

    doi: 10.3390/ma11040543

    Figure Lengend Snippet: ( a ) Comparative investigation on the absorbed levels of liquid electrolyte into (1) commercially available polypropylene (PP) separator and as-electrospun cross-linked PVDF- co -HFP separators with the two different thicknesses of (2) 40 μm and (3) 100 μm for 10 s, ( b ) a photo image representing a structural robust and stretchable PVDF- co -HFP GPE encapsulating 1 M LiPF 6 in EC: DMC, and ( c ) electrochemical impedance spectra (EIS) results of the PVDF- co -HFP GPE used in the stainless steel (SS)/GPE/SS cell.

    Article Snippet: We performed dynamic mechanical analysis (DMA) of the PVDF- co -HFP membrane to measure its viscoelastic behavior using a dynamic mechanical analyzer (Pyris Diamond DMA; PerkinElmer, Waltham, MA, USA) at a frequency of 0.5 Hz and a ramp rate of 8 °C/min in the tension mode.

    Techniques: Impedance Spectroscopy

    A comparative study of the performance of LIB cells incorporated with the commercialized PP and the PVDF- co -HFP separators. ( a , b ) Galvanostatic charge and discharge profiles of the LIB full-cells with the two different separators at 0.5 C for 30 cycles, and ( c ) cycling performance of the LIB half-cells with the two different separators at 0.5 C for 100 cycles and their corresponding coulombic efficiencies.

    Journal: Materials

    Article Title: Cross-Linked Poly(vinylidene fluoride-co-hexafluoropropene) (PVDF-co-HFP) Gel Polymer Electrolyte for Flexible Li-Ion Battery Integrated with Organic Light Emitting Diode (OLED)

    doi: 10.3390/ma11040543

    Figure Lengend Snippet: A comparative study of the performance of LIB cells incorporated with the commercialized PP and the PVDF- co -HFP separators. ( a , b ) Galvanostatic charge and discharge profiles of the LIB full-cells with the two different separators at 0.5 C for 30 cycles, and ( c ) cycling performance of the LIB half-cells with the two different separators at 0.5 C for 100 cycles and their corresponding coulombic efficiencies.

    Article Snippet: We performed dynamic mechanical analysis (DMA) of the PVDF- co -HFP membrane to measure its viscoelastic behavior using a dynamic mechanical analyzer (Pyris Diamond DMA; PerkinElmer, Waltham, MA, USA) at a frequency of 0.5 Hz and a ramp rate of 8 °C/min in the tension mode.

    Techniques:

    ( a – d ) SEM images showing the morphological variation of as-electrospun PVDF- co -HFP fibers with the different concentrations of the PVDF- co -HFP copolymer dissolved in the co-solvent of NMP and acetone. Note that ( c ) represents the magnified SEM image of ( b ) to highlight the cross-linked area marked by the yellow circles.

    Journal: Materials

    Article Title: Cross-Linked Poly(vinylidene fluoride-co-hexafluoropropene) (PVDF-co-HFP) Gel Polymer Electrolyte for Flexible Li-Ion Battery Integrated with Organic Light Emitting Diode (OLED)

    doi: 10.3390/ma11040543

    Figure Lengend Snippet: ( a – d ) SEM images showing the morphological variation of as-electrospun PVDF- co -HFP fibers with the different concentrations of the PVDF- co -HFP copolymer dissolved in the co-solvent of NMP and acetone. Note that ( c ) represents the magnified SEM image of ( b ) to highlight the cross-linked area marked by the yellow circles.

    Article Snippet: We performed dynamic mechanical analysis (DMA) of the PVDF- co -HFP membrane to measure its viscoelastic behavior using a dynamic mechanical analyzer (Pyris Diamond DMA; PerkinElmer, Waltham, MA, USA) at a frequency of 0.5 Hz and a ramp rate of 8 °C/min in the tension mode.

    Techniques: