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  • 93
    Integrated DNA Technologies electroporation enhancer
    Electroporation Enhancer, supplied by Integrated DNA Technologies, used in various techniques. Bioz Stars score: 93/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Lonza electroporation
    Electroporation, supplied by Lonza, used in various techniques. Bioz Stars score: 90/100, based on 1268 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher electroporation
    Electroporation, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 3712 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Bio-Rad electroporation
    EBNA3C competes with p21 for Pim-1 binding. A–B) 10 million HEK-293 cells were transfected with different combinations of Myc-tagged Pim-1, Flag-tagged p21, untagged-EBNA3C expression vectors as indicated by <t>electroporation.</t> A) IP was performed with anti-Myc antibody and IP complexes were resolved by 10% SDS-PAGE. Western blot was performed with indicated antibodies. B) Above mentioned transfected cells were treated with MG132 drug for 6 hrs and protein lysates were prepared by RIPA buffer. Western blot analysis was performed by indicated antibodies.
    Electroporation, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 14478 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Integrated DNA Technologies cas9 electroporation enhancer
    EBNA3C competes with p21 for Pim-1 binding. A–B) 10 million HEK-293 cells were transfected with different combinations of Myc-tagged Pim-1, Flag-tagged p21, untagged-EBNA3C expression vectors as indicated by <t>electroporation.</t> A) IP was performed with anti-Myc antibody and IP complexes were resolved by 10% SDS-PAGE. Western blot was performed with indicated antibodies. B) Above mentioned transfected cells were treated with MG132 drug for 6 hrs and protein lysates were prepared by RIPA buffer. Western blot analysis was performed by indicated antibodies.
    Cas9 Electroporation Enhancer, supplied by Integrated DNA Technologies, used in various techniques. Bioz Stars score: 96/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Lonza amaxa electroporation
    EBNA3C competes with p21 for Pim-1 binding. A–B) 10 million HEK-293 cells were transfected with different combinations of Myc-tagged Pim-1, Flag-tagged p21, untagged-EBNA3C expression vectors as indicated by <t>electroporation.</t> A) IP was performed with anti-Myc antibody and IP complexes were resolved by 10% SDS-PAGE. Western blot was performed with indicated antibodies. B) Above mentioned transfected cells were treated with MG132 drug for 6 hrs and protein lysates were prepared by RIPA buffer. Western blot analysis was performed by indicated antibodies.
    Amaxa Electroporation, supplied by Lonza, used in various techniques. Bioz Stars score: 91/100, based on 127 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Amaxa electroporation buffer
    Adrx Knockdown augmented TNFα-induced expression of ICAM-1 and VCAM-1, and monocyte adherence to HUVEC. ( a) HUVECs were transiently transfected with short interfering RNA targeting on Adrx (si-Adrx) or non-specific short interfering RNA (si-Control) by <t>electroporation</t> (Amaxa). Transfected cells were quiescent for 24 hours and then treated with or without TNFα for 8 hours. Expression of Adrx, ICAM-1 and VCAM-1 were detected using Western blot analysis. ( b) Band intensity was quantified by Gel-Pro Analyzer software and normalized protein levels of ICAM-1 and VCAM-1 are shown in Fig. 4b ; n = 3, *P
    Electroporation Buffer, supplied by Amaxa, used in various techniques. Bioz Stars score: 92/100, based on 140 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad electroporation buffer
    Assessment of EV and siRNA uptake following sonication To assess EV uptake, flow cytometry analysis of PKH67-labeled HEK293T-derived EVs and Cy3-labeled siRNA was conducted. PKH67+ and Cy3+ populations were gated from live cells, with the upper right quadrant indicative of cells containing both labeled EVs and labeled siRNA. The upper four panels show control conditions: cells incubated with unlabeled EVs alone (Unlabeled EVs), siRNA alone (siRNA), labeled EVs alone (EVs), or transfected with labeled siRNA (Transfected). The lower three panels represent cells incubated with EVs loaded with siRNA by different methods: passively by mixing (No Stimulation), sonication as described in Materials and Methods (Sonication), or <t>electroporation</t> as described in Materials and Methods (Electroporation).
    Electroporation Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 714 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Eppendorf AG electroporation buffer
    Growth curves of genetically modified T cells . Patient PBMCs were transfected with the scFvFc:ζ plasmid by <t>electroporation</t> after stimulation with OKT3. For patients A, B, and D, populations of G418-resistant T cells were generated by limiting
    Electroporation Buffer, supplied by Eppendorf AG, used in various techniques. Bioz Stars score: 92/100, based on 157 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Teknova electroporation buffer
    Growth curves of genetically modified T cells . Patient PBMCs were transfected with the scFvFc:ζ plasmid by <t>electroporation</t> after stimulation with OKT3. For patients A, B, and D, populations of G418-resistant T cells were generated by limiting
    Electroporation Buffer, supplied by Teknova, used in various techniques. Bioz Stars score: 90/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher electroporation buffer
    GFP and VEGF gene expression of electroporated BMMSCs. Green fluorescence represents the successful <t>electroporation</t> of plasmid into BMMSCs. Electroporated cells after 48 h ( a and b ). G418 selection after 20 days ( d and e ) ( bright vision
    Electroporation Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 321 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Harvard Bioscience electroporation chamber
    Robo/Dll1 Signaling Regulates the Balance between Direct Neurogenesis and IPC Abundance in Chick Dorsal Pallium (A–D) Analysis of chick dorsal pallium at 6 days post-ovoposition (dpo), showing many neurons in the VZ (solid arrowheads) in the medial part (mDP; B) and basal mitoses (open arrowheads) in the lateral (lDP; C; n = 3 embryos; t tests). (E–H) ISH in chick DP at 6 dpo, and quantifications of intensity (au, arbitrary units). High magnifications show chkRobo1 (E’ and E”) and chkDll1 (G’ and G”) in the indicated regions. Panel shown in (G) is a tiled image. (I) qPCR analysis in the VZ of the regions and species indicated. Values are ratio Robo1 to Gapdh (n = 12–15 replicates; paired or independent samples t tests). (J–O) Experimental design to manipulate in ovo Robo and Dll1 in mDP and lDP, representative examples and quantifications of neurons in the VZ (Tbr1+) and basal mitoses (PH3, open arrowheads; n = 3-5 embryos per group; t tests in L and Q; one-way ANOVA followed by t tests in M and O). Red shadowing and asterisks in (L) and (O) indicate values within group corresponding to GFP− cells. (P and Q) Expression of Tbr2 in basal PH3+ mitoses (solid arrowhead, Tbr2+; open arrowhead, Tbr2−) upon <t>electroporation</t> of dnR1/2+Dll1 in mDP (as in J and K), and quantification (n = 4–5 embryos; t tests). (R–U) Analysis of neuronal clones (GFP+RFP+Tuj1+) upon overexpression of dnR1/2+Dll1+Gfp, representative examples and quantification (n = 52 clones Gfp, 59 clones dnR1/2+Dll1+Gfp, 3–7 embryos; t test or χ2-test). Values are mean + SEM; ∗ p
    Electroporation Chamber, supplied by Harvard Bioscience, used in various techniques. Bioz Stars score: 93/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher electroporation chamber
    Robo/Dll1 Signaling Regulates the Balance between Direct Neurogenesis and IPC Abundance in Chick Dorsal Pallium (A–D) Analysis of chick dorsal pallium at 6 days post-ovoposition (dpo), showing many neurons in the VZ (solid arrowheads) in the medial part (mDP; B) and basal mitoses (open arrowheads) in the lateral (lDP; C; n = 3 embryos; t tests). (E–H) ISH in chick DP at 6 dpo, and quantifications of intensity (au, arbitrary units). High magnifications show chkRobo1 (E’ and E”) and chkDll1 (G’ and G”) in the indicated regions. Panel shown in (G) is a tiled image. (I) qPCR analysis in the VZ of the regions and species indicated. Values are ratio Robo1 to Gapdh (n = 12–15 replicates; paired or independent samples t tests). (J–O) Experimental design to manipulate in ovo Robo and Dll1 in mDP and lDP, representative examples and quantifications of neurons in the VZ (Tbr1+) and basal mitoses (PH3, open arrowheads; n = 3-5 embryos per group; t tests in L and Q; one-way ANOVA followed by t tests in M and O). Red shadowing and asterisks in (L) and (O) indicate values within group corresponding to GFP− cells. (P and Q) Expression of Tbr2 in basal PH3+ mitoses (solid arrowhead, Tbr2+; open arrowhead, Tbr2−) upon <t>electroporation</t> of dnR1/2+Dll1 in mDP (as in J and K), and quantification (n = 4–5 embryos; t tests). (R–U) Analysis of neuronal clones (GFP+RFP+Tuj1+) upon overexpression of dnR1/2+Dll1+Gfp, representative examples and quantification (n = 52 clones Gfp, 59 clones dnR1/2+Dll1+Gfp, 3–7 embryos; t test or χ2-test). Values are mean + SEM; ∗ p
    Electroporation Chamber, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Avantor electroporation cuvette
    ( a and b ) The normalized fluorescence ( NF ) of intracellular Fluorescein-Dextran as a result of double-pulse <t>electroporation.</t> ( Symbols ) Experimental data; ( curves ) least-square fitting. For all cases, the first pulse was always E 1 = 100,000 V/m and t 1 = 0.001s. To see this figure in color, go online.
    Electroporation Cuvette, supplied by Avantor, used in various techniques. Bioz Stars score: 93/100, based on 112 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad electroporation cuvette
    Electric field enhancement by CNT in <t>electroporation.</t> (a) Sketch of electroporation with CNT-free (left) and CNT associated cells (right). Table insert: theoretical electric field ( E ) enhancement over the applied field ( E 0 ) by a nanotube of 1 μ m long. d denotes the distance to nanotube tip. a 1 and a 2 are the aspect ratios (i.e. diameter/length) of nanotubes, and equal to 0.1 and 0.5 respectively. (b) Electroporation time constants versus the voltages. A series of time constants of the CNT associated Bal17 cells were obtained under various voltages. They were compared to the time constant of regular Bal17 cells at 230 V. (c) Improvement of EGFP transfection by CNT mediated electroporation in Bal17 cells. The gates of EGFP positive cells were adjusted based on the Neg Contl and Pos Contl . The mean values of EGFP levels (left axis) and the percentages (right axis) of gated viable cells are shown. Neg Contl : negative control, cells speared and electroporated without plasmid; Pos Contl : positive control, cells without spearing and electroporated at 230 V with EGFP plasmid; 180, 200 and 220 V: CNT associated cells and electroporated with EGFP plasmids at corresponding voltages.
    Electroporation Cuvette, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 2294 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Projects Ltd electroporation cuvette
    The effect of CD28 expression and segregated, stripe-shaped stimuli on tyrosine phosphorylation. The effect of receptor expression on signaling was studied using CD28-GFP transfected Jurkat ACC-282 T cells. After <t>electroporation,</t> cells were cultured for 48 h, serum starved for 6 h and then incubated on striped stimulatory surfaces for 10 minutes, fixed with 3% PFA and immunolabeled with αphosphotyrosine ( A ). The stimulatory surfaces were prepared using stamps coated with either 25 µg/ml αCD3 ( B D ); 25 µg/ml αCD28 ( C G ) or unspecific IgG2a only ( E F ). The stamped areas were subsequently overlaid with 5 µg/ml αCD28 ( B F ); 5 µg/ml αCD3 ( C E ) or unspecific IgG2a only ( D G ). B-G ) Top left panels: transmission image; top right panels: CD28-GFP; bottom left: αphosphotyrosine; bottom right panels: overlay of the stamped pattern (blue) and the αphosphotyrosine label (grayscale). In the CD28-GFP and overlay panels the contrast and brightness are adjusted proportionally for clarity. Scale bars 20 µm.
    Electroporation Cuvette, supplied by Cell Projects Ltd, used in various techniques. Bioz Stars score: 92/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Kaneka Corp electroporation cuvettes
    The effect of CD28 expression and segregated, stripe-shaped stimuli on tyrosine phosphorylation. The effect of receptor expression on signaling was studied using CD28-GFP transfected Jurkat ACC-282 T cells. After <t>electroporation,</t> cells were cultured for 48 h, serum starved for 6 h and then incubated on striped stimulatory surfaces for 10 minutes, fixed with 3% PFA and immunolabeled with αphosphotyrosine ( A ). The stimulatory surfaces were prepared using stamps coated with either 25 µg/ml αCD3 ( B D ); 25 µg/ml αCD28 ( C G ) or unspecific IgG2a only ( E F ). The stamped areas were subsequently overlaid with 5 µg/ml αCD28 ( B F ); 5 µg/ml αCD3 ( C E ) or unspecific IgG2a only ( D G ). B-G ) Top left panels: transmission image; top right panels: CD28-GFP; bottom left: αphosphotyrosine; bottom right panels: overlay of the stamped pattern (blue) and the αphosphotyrosine label (grayscale). In the CD28-GFP and overlay panels the contrast and brightness are adjusted proportionally for clarity. Scale bars 20 µm.
    Electroporation Cuvettes, supplied by Kaneka Corp, used in various techniques. Bioz Stars score: 92/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Amaxa amaxa electroporation
    The effect of CD28 expression and segregated, stripe-shaped stimuli on tyrosine phosphorylation. The effect of receptor expression on signaling was studied using CD28-GFP transfected Jurkat ACC-282 T cells. After <t>electroporation,</t> cells were cultured for 48 h, serum starved for 6 h and then incubated on striped stimulatory surfaces for 10 minutes, fixed with 3% PFA and immunolabeled with αphosphotyrosine ( A ). The stimulatory surfaces were prepared using stamps coated with either 25 µg/ml αCD3 ( B D ); 25 µg/ml αCD28 ( C G ) or unspecific IgG2a only ( E F ). The stamped areas were subsequently overlaid with 5 µg/ml αCD28 ( B F ); 5 µg/ml αCD3 ( C E ) or unspecific IgG2a only ( D G ). B-G ) Top left panels: transmission image; top right panels: CD28-GFP; bottom left: αphosphotyrosine; bottom right panels: overlay of the stamped pattern (blue) and the αphosphotyrosine label (grayscale). In the CD28-GFP and overlay panels the contrast and brightness are adjusted proportionally for clarity. Scale bars 20 µm.
    Amaxa Electroporation, supplied by Amaxa, used in various techniques. Bioz Stars score: 91/100, based on 694 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    MaxCyte electroporation buffer
    Similar signaling capacity and cytotocixity of mRNA electroporated and retrovirally transduced T cells . ( a ) Sensitivity of T-cell activation using T cells produced by mRNA <t>electroporation</t> compared with retroviral transduction. Results are displayed as percentage of maximum IFN-γ response obtained from intracellular cytokine staining. ( b ) Dose dependent lysis of HepG2-env targets (solid symbols and line) or HepG2-core targets (open symbols and dotted line) by electroporated T cells (triangle) compared with retrovirally transduced T cells (circle). Results are displayed as mean of triplicate measurements + SD. ( c ) Expression of perforin (left panel) and granzyme (right panel) on a representative activated T cells electroporated (red histograms) or retrovirally transduced (blue histograms) with s183-TCR, after 5 hours coculture with peptide-loaded T2 cells. Coculture with unpulsed T2 cells served as negative control (gray histograms). MFI of perforin and granzyme are indicated. ( d ) mRNA electroporated T cells have T CM -like phenotype. Phenotype of total lymphocytes (left panel), CD8 + pentamer + T cells (middle panel) and CD4 + Vb3 + T cells (right panel) in s183-TCR mRNA electroporated T cells (red shaded area) compared with retrovirally transduced T cells (blue shaded area). The percentages of CD45RA +/- and CD62L +/- cells within total lymphocytes or the gated CD8 + pentamer + or CD4 + Vb3 + populations were determined by FACS. Cells were classified into different subsets: naive (CD45RA + CD62L + ), T CM (CD45RA − CD62L + ), T EM (CD45RA − CD62L − ) and terminally differentiated EM (CD45RA + CD62L − ). Results expressed as mean + SD ( n = 3).
    Electroporation Buffer, supplied by MaxCyte, used in various techniques. Bioz Stars score: 92/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Eppendorf AG electroporation cuvette
    CRF protein homo- and heterodimerization. (A) CRF proteins CRF1–CRF8 and just the CRF domain of CRF2 (otherwise noted as CRFD) were analysed for potential homo- and heterodimerization using both BiFC and Y2H. Positive interactions are noted as a (+), (+*) for both BiFC and Y2H together, and (–) for non-interactions. (B) A cartoon of the conserved regions of CRF1–CRF6 proteins, the highly related CRF7 and CRF8 proteins (lacking the C-terminal third of the protein, but containing both the CRF domain and the AP2/ERF domain), and CRFD (just the CRF domain of CRF2). (C, D) Representative examples of positive CRF protein homo- and heterodimerization by BiFC as indicated in A are shown both under UV light in the presence of Hoechst 33342 dye denoting the nucleus and using a YFP wavelength filter to visualize BiFC interaction. Additionally, representative examples of empty vector (EV) controls for both N- and C-terminal BiFC vectors (EVn and EVc) examined in A are shown versus various CRFs and each other. (C) BiFC interactions in protoplasts transformed via <t>electroporation.</t> (D) BiFC interactions in tobacco leaves transformed via Agrobacterium .
    Electroporation Cuvette, supplied by Eppendorf AG, used in various techniques. Bioz Stars score: 93/100, based on 178 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    EBNA3C competes with p21 for Pim-1 binding. A–B) 10 million HEK-293 cells were transfected with different combinations of Myc-tagged Pim-1, Flag-tagged p21, untagged-EBNA3C expression vectors as indicated by electroporation. A) IP was performed with anti-Myc antibody and IP complexes were resolved by 10% SDS-PAGE. Western blot was performed with indicated antibodies. B) Above mentioned transfected cells were treated with MG132 drug for 6 hrs and protein lysates were prepared by RIPA buffer. Western blot analysis was performed by indicated antibodies.

    Journal: PLoS Pathogens

    Article Title: EBNA3C Augments Pim-1 Mediated Phosphorylation and Degradation of p21 to Promote B-Cell Proliferation

    doi: 10.1371/journal.ppat.1004304

    Figure Lengend Snippet: EBNA3C competes with p21 for Pim-1 binding. A–B) 10 million HEK-293 cells were transfected with different combinations of Myc-tagged Pim-1, Flag-tagged p21, untagged-EBNA3C expression vectors as indicated by electroporation. A) IP was performed with anti-Myc antibody and IP complexes were resolved by 10% SDS-PAGE. Western blot was performed with indicated antibodies. B) Above mentioned transfected cells were treated with MG132 drug for 6 hrs and protein lysates were prepared by RIPA buffer. Western blot analysis was performed by indicated antibodies.

    Article Snippet: Transfections Transfection in HEK-293, MEF and B-cells were performed by electroporation system with Bio-Rad Gene Pulser II electroporator.

    Techniques: Binding Assay, Transfection, Expressing, Electroporation, SDS Page, Western Blot

    EBNA3C destabilizes p21 through Pim-1 independent of the DNA damage response. A) 10 million HEK-293 cells were transfected with combinations of Myc-tagged Pim-1, Flag-tagged p21, untagged-EBNA3C expression by electroporation. After 36 hrs of post-transfection, cells were treated with cyclohexamide for indicated time points in DMEM medium containing either serum/DMSO or 0.1% FBS with 5 µM etoposide. Protein samples were resolved by 10% SDS-PAGE and Western blots were performed with indicated antibodies. B–C) 50 million EBV negative BJAB cells, EBNA3C expressing BJAB10, EBV transformed LCL1, sh-Ctrl, sh-E3C LCL1 cells were incubated with cyclohexamide for specific time points in RPMI medium containing serum/DMSO or 0.1% FBS with 5 µM etoposide. Samples were resolved by 10% SDS-PAGE and Western blot analysis was performed with specific antibodies.

    Journal: PLoS Pathogens

    Article Title: EBNA3C Augments Pim-1 Mediated Phosphorylation and Degradation of p21 to Promote B-Cell Proliferation

    doi: 10.1371/journal.ppat.1004304

    Figure Lengend Snippet: EBNA3C destabilizes p21 through Pim-1 independent of the DNA damage response. A) 10 million HEK-293 cells were transfected with combinations of Myc-tagged Pim-1, Flag-tagged p21, untagged-EBNA3C expression by electroporation. After 36 hrs of post-transfection, cells were treated with cyclohexamide for indicated time points in DMEM medium containing either serum/DMSO or 0.1% FBS with 5 µM etoposide. Protein samples were resolved by 10% SDS-PAGE and Western blots were performed with indicated antibodies. B–C) 50 million EBV negative BJAB cells, EBNA3C expressing BJAB10, EBV transformed LCL1, sh-Ctrl, sh-E3C LCL1 cells were incubated with cyclohexamide for specific time points in RPMI medium containing serum/DMSO or 0.1% FBS with 5 µM etoposide. Samples were resolved by 10% SDS-PAGE and Western blot analysis was performed with specific antibodies.

    Article Snippet: Transfections Transfection in HEK-293, MEF and B-cells were performed by electroporation system with Bio-Rad Gene Pulser II electroporator.

    Techniques: Transfection, Expressing, Electroporation, SDS Page, Western Blot, Transformation Assay, Incubation

    Adrx Knockdown augmented TNFα-induced expression of ICAM-1 and VCAM-1, and monocyte adherence to HUVEC. ( a) HUVECs were transiently transfected with short interfering RNA targeting on Adrx (si-Adrx) or non-specific short interfering RNA (si-Control) by electroporation (Amaxa). Transfected cells were quiescent for 24 hours and then treated with or without TNFα for 8 hours. Expression of Adrx, ICAM-1 and VCAM-1 were detected using Western blot analysis. ( b) Band intensity was quantified by Gel-Pro Analyzer software and normalized protein levels of ICAM-1 and VCAM-1 are shown in Fig. 4b ; n = 3, *P

    Journal: Scientific Reports

    Article Title: Adiporedoxin suppresses endothelial activation via inhibiting MAPK and NF-κB signaling

    doi: 10.1038/srep38975

    Figure Lengend Snippet: Adrx Knockdown augmented TNFα-induced expression of ICAM-1 and VCAM-1, and monocyte adherence to HUVEC. ( a) HUVECs were transiently transfected with short interfering RNA targeting on Adrx (si-Adrx) or non-specific short interfering RNA (si-Control) by electroporation (Amaxa). Transfected cells were quiescent for 24 hours and then treated with or without TNFα for 8 hours. Expression of Adrx, ICAM-1 and VCAM-1 were detected using Western blot analysis. ( b) Band intensity was quantified by Gel-Pro Analyzer software and normalized protein levels of ICAM-1 and VCAM-1 are shown in Fig. 4b ; n = 3, *P

    Article Snippet: Cells were collected and washed once with medium, and resuspended with the electroporation buffer (Amaxa).

    Techniques: Expressing, Transfection, Small Interfering RNA, Electroporation, Western Blot, Software

    Assessment of EV and siRNA uptake following sonication To assess EV uptake, flow cytometry analysis of PKH67-labeled HEK293T-derived EVs and Cy3-labeled siRNA was conducted. PKH67+ and Cy3+ populations were gated from live cells, with the upper right quadrant indicative of cells containing both labeled EVs and labeled siRNA. The upper four panels show control conditions: cells incubated with unlabeled EVs alone (Unlabeled EVs), siRNA alone (siRNA), labeled EVs alone (EVs), or transfected with labeled siRNA (Transfected). The lower three panels represent cells incubated with EVs loaded with siRNA by different methods: passively by mixing (No Stimulation), sonication as described in Materials and Methods (Sonication), or electroporation as described in Materials and Methods (Electroporation).

    Journal: Cellular and molecular bioengineering

    Article Title: Oncogene Knockdown via Active Loading of Small RNAs into Extracellular Vesicles by Sonication

    doi: 10.1007/s12195-016-0457-4

    Figure Lengend Snippet: Assessment of EV and siRNA uptake following sonication To assess EV uptake, flow cytometry analysis of PKH67-labeled HEK293T-derived EVs and Cy3-labeled siRNA was conducted. PKH67+ and Cy3+ populations were gated from live cells, with the upper right quadrant indicative of cells containing both labeled EVs and labeled siRNA. The upper four panels show control conditions: cells incubated with unlabeled EVs alone (Unlabeled EVs), siRNA alone (siRNA), labeled EVs alone (EVs), or transfected with labeled siRNA (Transfected). The lower three panels represent cells incubated with EVs loaded with siRNA by different methods: passively by mixing (No Stimulation), sonication as described in Materials and Methods (Sonication), or electroporation as described in Materials and Methods (Electroporation).

    Article Snippet: Briefly, EVs were mixed with nucleic acids in electroporation buffer (1.15mM potassium phosphate, pH=7.2, 25mM potassium chloride, 21% Optiprep) and electroporation was carried out at 400V and 125μF with two pulses using Gene Pulser/Micropulser Cuvettes (Bio-Rad #165-2089) in a GenePulser Xcell electroporator (Bio-Rad).

    Techniques: Sonication, Flow Cytometry, Cytometry, Labeling, Derivative Assay, Incubation, Transfection, Electroporation

    Growth curves of genetically modified T cells . Patient PBMCs were transfected with the scFvFc:ζ plasmid by electroporation after stimulation with OKT3. For patients A, B, and D, populations of G418-resistant T cells were generated by limiting

    Journal:

    Article Title: Adoptive immunotherapy for indolent non-Hodgkin lymphoma and mantle cell lymphoma using genetically modified autologous CD20-specific T cells

    doi: 10.1182/blood-2007-12-128843

    Figure Lengend Snippet: Growth curves of genetically modified T cells . Patient PBMCs were transfected with the scFvFc:ζ plasmid by electroporation after stimulation with OKT3. For patients A, B, and D, populations of G418-resistant T cells were generated by limiting

    Article Snippet: On day 4 of culture, cells were harvested and resuspended in chilled hypo-osmolar electroporation buffer (Eppendorf North America, New York, NY) at 20 × 106 cells/mL.

    Techniques: Genetically Modified, Transfection, Plasmid Preparation, Electroporation, Generated

    GFP and VEGF gene expression of electroporated BMMSCs. Green fluorescence represents the successful electroporation of plasmid into BMMSCs. Electroporated cells after 48 h ( a and b ). G418 selection after 20 days ( d and e ) ( bright vision

    Journal: Cytotechnology

    Article Title: VEGF165 expressing bone marrow mesenchymal stem cells differentiate into hepatocytes under HGF and EGF induction in vitro

    doi: 10.1007/s10616-012-9439-0

    Figure Lengend Snippet: GFP and VEGF gene expression of electroporated BMMSCs. Green fluorescence represents the successful electroporation of plasmid into BMMSCs. Electroporated cells after 48 h ( a and b ). G418 selection after 20 days ( d and e ) ( bright vision

    Article Snippet: The 3rd generation BMMSCs were harvested and resuspended in electroporation buffer [containing 750 μl Opti-DMEM (Gibco, USA) without serum and 50 μg VEGF165 -pCMV6-AC-GFP plasmid (OriGene, Rockville/MD, USA) or pCMV6-AC-GFP plasmid (OriGene, USA)].

    Techniques: Expressing, Fluorescence, Electroporation, Plasmid Preparation, Selection

    Robo/Dll1 Signaling Regulates the Balance between Direct Neurogenesis and IPC Abundance in Chick Dorsal Pallium (A–D) Analysis of chick dorsal pallium at 6 days post-ovoposition (dpo), showing many neurons in the VZ (solid arrowheads) in the medial part (mDP; B) and basal mitoses (open arrowheads) in the lateral (lDP; C; n = 3 embryos; t tests). (E–H) ISH in chick DP at 6 dpo, and quantifications of intensity (au, arbitrary units). High magnifications show chkRobo1 (E’ and E”) and chkDll1 (G’ and G”) in the indicated regions. Panel shown in (G) is a tiled image. (I) qPCR analysis in the VZ of the regions and species indicated. Values are ratio Robo1 to Gapdh (n = 12–15 replicates; paired or independent samples t tests). (J–O) Experimental design to manipulate in ovo Robo and Dll1 in mDP and lDP, representative examples and quantifications of neurons in the VZ (Tbr1+) and basal mitoses (PH3, open arrowheads; n = 3-5 embryos per group; t tests in L and Q; one-way ANOVA followed by t tests in M and O). Red shadowing and asterisks in (L) and (O) indicate values within group corresponding to GFP− cells. (P and Q) Expression of Tbr2 in basal PH3+ mitoses (solid arrowhead, Tbr2+; open arrowhead, Tbr2−) upon electroporation of dnR1/2+Dll1 in mDP (as in J and K), and quantification (n = 4–5 embryos; t tests). (R–U) Analysis of neuronal clones (GFP+RFP+Tuj1+) upon overexpression of dnR1/2+Dll1+Gfp, representative examples and quantification (n = 52 clones Gfp, 59 clones dnR1/2+Dll1+Gfp, 3–7 embryos; t test or χ2-test). Values are mean + SEM; ∗ p

    Journal: Cell

    Article Title: Evolution of Cortical Neurogenesis in Amniotes Controlled by Robo Signaling Levels

    doi: 10.1016/j.cell.2018.06.007

    Figure Lengend Snippet: Robo/Dll1 Signaling Regulates the Balance between Direct Neurogenesis and IPC Abundance in Chick Dorsal Pallium (A–D) Analysis of chick dorsal pallium at 6 days post-ovoposition (dpo), showing many neurons in the VZ (solid arrowheads) in the medial part (mDP; B) and basal mitoses (open arrowheads) in the lateral (lDP; C; n = 3 embryos; t tests). (E–H) ISH in chick DP at 6 dpo, and quantifications of intensity (au, arbitrary units). High magnifications show chkRobo1 (E’ and E”) and chkDll1 (G’ and G”) in the indicated regions. Panel shown in (G) is a tiled image. (I) qPCR analysis in the VZ of the regions and species indicated. Values are ratio Robo1 to Gapdh (n = 12–15 replicates; paired or independent samples t tests). (J–O) Experimental design to manipulate in ovo Robo and Dll1 in mDP and lDP, representative examples and quantifications of neurons in the VZ (Tbr1+) and basal mitoses (PH3, open arrowheads; n = 3-5 embryos per group; t tests in L and Q; one-way ANOVA followed by t tests in M and O). Red shadowing and asterisks in (L) and (O) indicate values within group corresponding to GFP− cells. (P and Q) Expression of Tbr2 in basal PH3+ mitoses (solid arrowhead, Tbr2+; open arrowhead, Tbr2−) upon electroporation of dnR1/2+Dll1 in mDP (as in J and K), and quantification (n = 4–5 embryos; t tests). (R–U) Analysis of neuronal clones (GFP+RFP+Tuj1+) upon overexpression of dnR1/2+Dll1+Gfp, representative examples and quantification (n = 52 clones Gfp, 59 clones dnR1/2+Dll1+Gfp, 3–7 embryos; t test or χ2-test). Values are mean + SEM; ∗ p

    Article Snippet: During the electroporation cerebral organoids were placed in an electroporation chamber (Harvard Apparatus, Holliston, MA, USA) under a stereoscope and using a glass microcapillary 1-2 μL of plasmid DNAs was injected together with Fast Green (0.1%, Sigma) into different ventricles of the organoids.

    Techniques: In Situ Hybridization, Real-time Polymerase Chain Reaction, In Ovo, Expressing, Electroporation, Clone Assay, Over Expression

    ( a and b ) The normalized fluorescence ( NF ) of intracellular Fluorescein-Dextran as a result of double-pulse electroporation. ( Symbols ) Experimental data; ( curves ) least-square fitting. For all cases, the first pulse was always E 1 = 100,000 V/m and t 1 = 0.001s. To see this figure in color, go online.

    Journal: Biophysical Journal

    Article Title: Scaling Relationship and Optimization of Double-Pulse Electroporation

    doi: 10.1016/j.bpj.2013.12.045

    Figure Lengend Snippet: ( a and b ) The normalized fluorescence ( NF ) of intracellular Fluorescein-Dextran as a result of double-pulse electroporation. ( Symbols ) Experimental data; ( curves ) least-square fitting. For all cases, the first pulse was always E 1 = 100,000 V/m and t 1 = 0.001s. To see this figure in color, go online.

    Article Snippet: A volume of 90 μ L of cell suspension was placed into an electroporation cuvette (model No. 89047-206; VWR, Philadelphia, PA).

    Techniques: Fluorescence, Electroporation

    The percentage of viable cells after double-pulse electroporation. ( Symbols ) Experimental data; ( curves ) least-square fitting. For all cases, the first pulse was always E 1 = 100,000 V/m and t 1 = 0.001 s. To see this figure in color, go online.

    Journal: Biophysical Journal

    Article Title: Scaling Relationship and Optimization of Double-Pulse Electroporation

    doi: 10.1016/j.bpj.2013.12.045

    Figure Lengend Snippet: The percentage of viable cells after double-pulse electroporation. ( Symbols ) Experimental data; ( curves ) least-square fitting. For all cases, the first pulse was always E 1 = 100,000 V/m and t 1 = 0.001 s. To see this figure in color, go online.

    Article Snippet: A volume of 90 μ L of cell suspension was placed into an electroporation cuvette (model No. 89047-206; VWR, Philadelphia, PA).

    Techniques: Electroporation

    Cerebellar organoids electroporation with Otx2 / c-MYC induces Group 3 MB in vivo. a Schematic representation of in vivo injection of modified cerebellar organoids. b DAPI staining and GFP immunofluorescence (Venus) of the sagittal brain section of nude mouse 1 month after injection of human cerebellar organoids electroporated with pPBase + pPBMyc + pPBOtx2 + pPBVenus. c Confocal images of GFP (Venus) and PCNA immunofluorescence of tumors in nude mouse 1 month after injection of human cerebellar organoids electroporated with pPBase + pPBMyc + pPBOtx2 + pPBVenus. d NPR3 immunohistochemistry and Hematoxylin staining of tumor in nude mouse 1 month after injection of human cerebellar organoids electroporated with pPBase + pPBMyc + pPBOtx2 + pPBVenus. e MDS (multidimensional scaling) analysis performed on the 1000 most variable probes of the whole-genome DNA methylation data shows a close similarity between organoids and group 3 MBs. Color legend of the MDS plot as follows: OM Organoids (Organoids_OM, black); GM Organoids (Organoids_GM, gray); WNT, Wingless MB (blue); SHH-A, Sonic Hedgehog MB-adulthood and childhood (red); SHH-B Sonic Hedgehog MB infant (dark red); G3, Group 3 MB (yellow); G4, Group 4 MB (green). f Hierarchical clustering and heatmap of beta values relative to the 39 high-quality CpG islands better discriminating MB subgroup in the Hovestadt set (Hovestadt et al.) 35 . The heatmap shows normalized methylation levels in organoid samples and MB samples. Clusters were obtained by means of Ward’s minimum variance method, using the Euclidean distance. Color legend: OM Organoids (Organoids_OM, black); GM Organoids (Organoids_ GM, gray); WNT, Wingless MB (blue); SHH-A, Sonic Hedgehog MB-adulthood and childhood (red); SHH-B Sonic Hedgehog MB infant (dark red); G3, Group 3 MB (yellow); G4, Group 4 MB (green). Scale bars 1 mm in ( b ), 100 µm in ( c , d ).

    Journal: Nature Communications

    Article Title: Modeling medulloblastoma in vivo and with human cerebellar organoids

    doi: 10.1038/s41467-019-13989-3

    Figure Lengend Snippet: Cerebellar organoids electroporation with Otx2 / c-MYC induces Group 3 MB in vivo. a Schematic representation of in vivo injection of modified cerebellar organoids. b DAPI staining and GFP immunofluorescence (Venus) of the sagittal brain section of nude mouse 1 month after injection of human cerebellar organoids electroporated with pPBase + pPBMyc + pPBOtx2 + pPBVenus. c Confocal images of GFP (Venus) and PCNA immunofluorescence of tumors in nude mouse 1 month after injection of human cerebellar organoids electroporated with pPBase + pPBMyc + pPBOtx2 + pPBVenus. d NPR3 immunohistochemistry and Hematoxylin staining of tumor in nude mouse 1 month after injection of human cerebellar organoids electroporated with pPBase + pPBMyc + pPBOtx2 + pPBVenus. e MDS (multidimensional scaling) analysis performed on the 1000 most variable probes of the whole-genome DNA methylation data shows a close similarity between organoids and group 3 MBs. Color legend of the MDS plot as follows: OM Organoids (Organoids_OM, black); GM Organoids (Organoids_GM, gray); WNT, Wingless MB (blue); SHH-A, Sonic Hedgehog MB-adulthood and childhood (red); SHH-B Sonic Hedgehog MB infant (dark red); G3, Group 3 MB (yellow); G4, Group 4 MB (green). f Hierarchical clustering and heatmap of beta values relative to the 39 high-quality CpG islands better discriminating MB subgroup in the Hovestadt set (Hovestadt et al.) 35 . The heatmap shows normalized methylation levels in organoid samples and MB samples. Clusters were obtained by means of Ward’s minimum variance method, using the Euclidean distance. Color legend: OM Organoids (Organoids_OM, black); GM Organoids (Organoids_ GM, gray); WNT, Wingless MB (blue); SHH-A, Sonic Hedgehog MB-adulthood and childhood (red); SHH-B Sonic Hedgehog MB infant (dark red); G3, Group 3 MB (yellow); G4, Group 4 MB (green). Scale bars 1 mm in ( b ), 100 µm in ( c , d ).

    Article Snippet: Organoids were transferred inside the Electroporation cuvettes (VWR, ECN 732-1136, 2 mm), and electroporation was performed with the Gene Pulser XcellTM.

    Techniques: Electroporation, In Vivo, Injection, Modification, Staining, Immunofluorescence, Immunohistochemistry, DNA Methylation Assay, Methylation

    Cerebellar organoids electroporation with Gfi1 / c-MYC and Otx2 / c-MYC induces overproliferation. a Schematic representation of organoids electroporation. b Brightfield and fluorescence images of cerebellar organoids at day 60 electroporated at day 35 with pPBVenus. c Brightfield and fluorescence images of cerebellar organoids at day 60 electroporated at day 35 with pPBase + pPBMyc + pPBGfi1 + pPBVenus. d Brightfield and fluorescence images of cerebellar organoids at day 60 electroporated at day 35 with pPBase + pPBMyc + pPBOtx2 + pPBVenus. Arrows in ( b , c , d ) indicate Venus-positive cells. e Confocal images of GFP (Venus) and PCNA immunofluorescence of cerebellar organoids at day 60 electroporated at day 35 with pPBase + pPBVenus + pPBMyc and pPBOtx2. Arrows indicate double-positive cells. f Confocal images of GFP (Venus) and β3-tubulin immunofluorescence of cerebellar organoids at day 60 electroporated at day 35 with pPBase + pPBMyc + pPBOtx2 + pPBVenus. Arrows indicate β3-tubulin-negative cells. g Quantification of cerebellar organoids at day 60, electroporated at day 35 with either pPBVenus or pPBase + pPBMyc + pPBOtx2 + pPBVenus (OM) or pPBase + pPBMyc + pPBGfi1 + pPBVenus (GM). n = 6 biologically independent organoids. h Quantification of cerebellar organoids at day 40, electroporated at day 35 with either pPBVenus or pPBase + pPBMyc + pPBOtx2 + pPBVenus (OM) or pPBase + pPBMyc + pPBGfi1 + pPBVenus (GM). n = 6 biologically independent organoids. Error bars in ( g , e ) represent standard error of the mean. Scale bars 250 µm in ( b – d ),100 µm in ( e , f ). Paired Student's t test, two tails. * p -value

    Journal: Nature Communications

    Article Title: Modeling medulloblastoma in vivo and with human cerebellar organoids

    doi: 10.1038/s41467-019-13989-3

    Figure Lengend Snippet: Cerebellar organoids electroporation with Gfi1 / c-MYC and Otx2 / c-MYC induces overproliferation. a Schematic representation of organoids electroporation. b Brightfield and fluorescence images of cerebellar organoids at day 60 electroporated at day 35 with pPBVenus. c Brightfield and fluorescence images of cerebellar organoids at day 60 electroporated at day 35 with pPBase + pPBMyc + pPBGfi1 + pPBVenus. d Brightfield and fluorescence images of cerebellar organoids at day 60 electroporated at day 35 with pPBase + pPBMyc + pPBOtx2 + pPBVenus. Arrows in ( b , c , d ) indicate Venus-positive cells. e Confocal images of GFP (Venus) and PCNA immunofluorescence of cerebellar organoids at day 60 electroporated at day 35 with pPBase + pPBVenus + pPBMyc and pPBOtx2. Arrows indicate double-positive cells. f Confocal images of GFP (Venus) and β3-tubulin immunofluorescence of cerebellar organoids at day 60 electroporated at day 35 with pPBase + pPBMyc + pPBOtx2 + pPBVenus. Arrows indicate β3-tubulin-negative cells. g Quantification of cerebellar organoids at day 60, electroporated at day 35 with either pPBVenus or pPBase + pPBMyc + pPBOtx2 + pPBVenus (OM) or pPBase + pPBMyc + pPBGfi1 + pPBVenus (GM). n = 6 biologically independent organoids. h Quantification of cerebellar organoids at day 40, electroporated at day 35 with either pPBVenus or pPBase + pPBMyc + pPBOtx2 + pPBVenus (OM) or pPBase + pPBMyc + pPBGfi1 + pPBVenus (GM). n = 6 biologically independent organoids. Error bars in ( g , e ) represent standard error of the mean. Scale bars 250 µm in ( b – d ),100 µm in ( e , f ). Paired Student's t test, two tails. * p -value

    Article Snippet: Organoids were transferred inside the Electroporation cuvettes (VWR, ECN 732-1136, 2 mm), and electroporation was performed with the Gene Pulser XcellTM.

    Techniques: Electroporation, Fluorescence, Immunofluorescence

    Electric field enhancement by CNT in electroporation. (a) Sketch of electroporation with CNT-free (left) and CNT associated cells (right). Table insert: theoretical electric field ( E ) enhancement over the applied field ( E 0 ) by a nanotube of 1 μ m long. d denotes the distance to nanotube tip. a 1 and a 2 are the aspect ratios (i.e. diameter/length) of nanotubes, and equal to 0.1 and 0.5 respectively. (b) Electroporation time constants versus the voltages. A series of time constants of the CNT associated Bal17 cells were obtained under various voltages. They were compared to the time constant of regular Bal17 cells at 230 V. (c) Improvement of EGFP transfection by CNT mediated electroporation in Bal17 cells. The gates of EGFP positive cells were adjusted based on the Neg Contl and Pos Contl . The mean values of EGFP levels (left axis) and the percentages (right axis) of gated viable cells are shown. Neg Contl : negative control, cells speared and electroporated without plasmid; Pos Contl : positive control, cells without spearing and electroporated at 230 V with EGFP plasmid; 180, 200 and 220 V: CNT associated cells and electroporated with EGFP plasmids at corresponding voltages.

    Journal: Nanotechnology

    Article Title: Interaction between carbon nanotubes and mammalian cells: characterization by flow cytometry and application

    doi: 10.1088/0957-4484/19/34/345102

    Figure Lengend Snippet: Electric field enhancement by CNT in electroporation. (a) Sketch of electroporation with CNT-free (left) and CNT associated cells (right). Table insert: theoretical electric field ( E ) enhancement over the applied field ( E 0 ) by a nanotube of 1 μ m long. d denotes the distance to nanotube tip. a 1 and a 2 are the aspect ratios (i.e. diameter/length) of nanotubes, and equal to 0.1 and 0.5 respectively. (b) Electroporation time constants versus the voltages. A series of time constants of the CNT associated Bal17 cells were obtained under various voltages. They were compared to the time constant of regular Bal17 cells at 230 V. (c) Improvement of EGFP transfection by CNT mediated electroporation in Bal17 cells. The gates of EGFP positive cells were adjusted based on the Neg Contl and Pos Contl . The mean values of EGFP levels (left axis) and the percentages (right axis) of gated viable cells are shown. Neg Contl : negative control, cells speared and electroporated without plasmid; Pos Contl : positive control, cells without spearing and electroporated at 230 V with EGFP plasmid; 180, 200 and 220 V: CNT associated cells and electroporated with EGFP plasmids at corresponding voltages.

    Article Snippet: Each electroporation cuvette (cooled on ice) was loaded with 3 × 106 regular or CNT associated Bal17 cells in suspension adjusted to 200 μ l. A Gene Pulser electroporation system (BIO-RAD, Hercules, CA) was High Cap, 960 μ F. Voltages were selected from 100 to 250 V. For the transfection experiments, pEGFP plasmid DNA (Clontech, Mountain View, CA) was supplemented to the cell suspensions in the cuvettes.

    Techniques: Electroporation, Transfection, Negative Control, Plasmid Preparation, Positive Control

    Functional analysis of HmTSP by siRNA knockdown. ( a ) ISH analysis of HmTSP expression in control GFP -transgenic animals electroporated with GFP siRNA. ( b ) ISH analysis showing reduced HmTSP expression in animals electroporated with HmTSP siRNA. Bars = 100 µm. ( c , d ) Demonstration of effective siRNA knockdown for GFP in transgenic hydra with ectodermal GFP expression. ( c ) Untreated control animal. D. Representative animal of the same transgenic strain as in C 8 days after electroporation with GFP siRNA. Bars = 500 µm. ( e– e’) Treatment with combined siGFP and siHmTSP does not induce morphological changes in steady state polyps. ( f , g ) Treatment with ALP of siTSP electroporated animals resulted in a dramatic increase of ectopic tentacles compared to the siGFP-treated control group. f’ and g’ show the reduced GFP expression in the respective animals. Each panel representative of at least 10 hydras examined. ( h ) Quantification of ALP-induced ectopic tentacles in animals electroporated with siGFP or siGFP and siTSP. Animals electroporated with the respective siRNAs without subsequent ALP treatment served as controls. ALP treatment was performed 8 days after electroporation and the numbers of tentacles/animal in each group were counted 5 days after ALP treatment. Animals in d and e were recorded at the same time point after electroporation as animals in f and g. Animals (n) in each group were: siGFP = 67; siGFP/siTSP = 67; siGFP/ALP = 71; siGFP/siTSP/ALP = 71. ( i ) Effect of Wnt3 depletion on ectopic tentacle formation: Animals were electroporated with siRNAs specific for GFP or directed against Wnt3 and GFP followed by ALP- or control treatment as indicated. Ectopic tentacle formation was analyzed as described above ( h ). Number of polyps analyzed in each group was: siGFP: 74, siGFP/siWnt3: 76, siGFP/ALP: 79, and siGFP/siWnt3/ALP: 81. ( h and i show the results from three independent experiments. Each data point represents a single hydra, bars indicate the mean ± S.E.M. ***P value

    Journal: Scientific Reports

    Article Title: Hydra Mesoglea Proteome Identifies Thrombospondin as a Conserved Component Active in Head Organizer Restriction

    doi: 10.1038/s41598-018-30035-2

    Figure Lengend Snippet: Functional analysis of HmTSP by siRNA knockdown. ( a ) ISH analysis of HmTSP expression in control GFP -transgenic animals electroporated with GFP siRNA. ( b ) ISH analysis showing reduced HmTSP expression in animals electroporated with HmTSP siRNA. Bars = 100 µm. ( c , d ) Demonstration of effective siRNA knockdown for GFP in transgenic hydra with ectodermal GFP expression. ( c ) Untreated control animal. D. Representative animal of the same transgenic strain as in C 8 days after electroporation with GFP siRNA. Bars = 500 µm. ( e– e’) Treatment with combined siGFP and siHmTSP does not induce morphological changes in steady state polyps. ( f , g ) Treatment with ALP of siTSP electroporated animals resulted in a dramatic increase of ectopic tentacles compared to the siGFP-treated control group. f’ and g’ show the reduced GFP expression in the respective animals. Each panel representative of at least 10 hydras examined. ( h ) Quantification of ALP-induced ectopic tentacles in animals electroporated with siGFP or siGFP and siTSP. Animals electroporated with the respective siRNAs without subsequent ALP treatment served as controls. ALP treatment was performed 8 days after electroporation and the numbers of tentacles/animal in each group were counted 5 days after ALP treatment. Animals in d and e were recorded at the same time point after electroporation as animals in f and g. Animals (n) in each group were: siGFP = 67; siGFP/siTSP = 67; siGFP/ALP = 71; siGFP/siTSP/ALP = 71. ( i ) Effect of Wnt3 depletion on ectopic tentacle formation: Animals were electroporated with siRNAs specific for GFP or directed against Wnt3 and GFP followed by ALP- or control treatment as indicated. Ectopic tentacle formation was analyzed as described above ( h ). Number of polyps analyzed in each group was: siGFP: 74, siGFP/siWnt3: 76, siGFP/ALP: 79, and siGFP/siWnt3/ALP: 81. ( h and i show the results from three independent experiments. Each data point represents a single hydra, bars indicate the mean ± S.E.M. ***P value

    Article Snippet: For each reaction, 20 animals were transferred to electroporation cuvettes (4 mm gap, Bio-Rad) and excess liquid was removed.

    Techniques: Functional Assay, In Situ Hybridization, Expressing, Transgenic Assay, Electroporation, ALP Assay

    The effect of CD28 expression and segregated, stripe-shaped stimuli on tyrosine phosphorylation. The effect of receptor expression on signaling was studied using CD28-GFP transfected Jurkat ACC-282 T cells. After electroporation, cells were cultured for 48 h, serum starved for 6 h and then incubated on striped stimulatory surfaces for 10 minutes, fixed with 3% PFA and immunolabeled with αphosphotyrosine ( A ). The stimulatory surfaces were prepared using stamps coated with either 25 µg/ml αCD3 ( B D ); 25 µg/ml αCD28 ( C G ) or unspecific IgG2a only ( E F ). The stamped areas were subsequently overlaid with 5 µg/ml αCD28 ( B F ); 5 µg/ml αCD3 ( C E ) or unspecific IgG2a only ( D G ). B-G ) Top left panels: transmission image; top right panels: CD28-GFP; bottom left: αphosphotyrosine; bottom right panels: overlay of the stamped pattern (blue) and the αphosphotyrosine label (grayscale). In the CD28-GFP and overlay panels the contrast and brightness are adjusted proportionally for clarity. Scale bars 20 µm.

    Journal: PLoS ONE

    Article Title: A Quantitative Assessment of Costimulation and Phosphatase Activity on Microclusters in Early T Cell Signaling

    doi: 10.1371/journal.pone.0079277

    Figure Lengend Snippet: The effect of CD28 expression and segregated, stripe-shaped stimuli on tyrosine phosphorylation. The effect of receptor expression on signaling was studied using CD28-GFP transfected Jurkat ACC-282 T cells. After electroporation, cells were cultured for 48 h, serum starved for 6 h and then incubated on striped stimulatory surfaces for 10 minutes, fixed with 3% PFA and immunolabeled with αphosphotyrosine ( A ). The stimulatory surfaces were prepared using stamps coated with either 25 µg/ml αCD3 ( B D ); 25 µg/ml αCD28 ( C G ) or unspecific IgG2a only ( E F ). The stamped areas were subsequently overlaid with 5 µg/ml αCD28 ( B F ); 5 µg/ml αCD3 ( C E ) or unspecific IgG2a only ( D G ). B-G ) Top left panels: transmission image; top right panels: CD28-GFP; bottom left: αphosphotyrosine; bottom right panels: overlay of the stamped pattern (blue) and the αphosphotyrosine label (grayscale). In the CD28-GFP and overlay panels the contrast and brightness are adjusted proportionally for clarity. Scale bars 20 µm.

    Article Snippet: Cell Transfection 5 • 106 Jurkat cells (ACC-282) in 100 µl serum free RPMI medium were transfected with 5 µg CD28-GFP (RG211318; OriGene Technologies Rockville, MD, USA) in a 2 mm electroporation cuvette (Cell Projects Limited, Kent, UK).

    Techniques: Expressing, Transfection, Electroporation, Cell Culture, Incubation, Immunolabeling, Transmission Assay

    Similar signaling capacity and cytotocixity of mRNA electroporated and retrovirally transduced T cells . ( a ) Sensitivity of T-cell activation using T cells produced by mRNA electroporation compared with retroviral transduction. Results are displayed as percentage of maximum IFN-γ response obtained from intracellular cytokine staining. ( b ) Dose dependent lysis of HepG2-env targets (solid symbols and line) or HepG2-core targets (open symbols and dotted line) by electroporated T cells (triangle) compared with retrovirally transduced T cells (circle). Results are displayed as mean of triplicate measurements + SD. ( c ) Expression of perforin (left panel) and granzyme (right panel) on a representative activated T cells electroporated (red histograms) or retrovirally transduced (blue histograms) with s183-TCR, after 5 hours coculture with peptide-loaded T2 cells. Coculture with unpulsed T2 cells served as negative control (gray histograms). MFI of perforin and granzyme are indicated. ( d ) mRNA electroporated T cells have T CM -like phenotype. Phenotype of total lymphocytes (left panel), CD8 + pentamer + T cells (middle panel) and CD4 + Vb3 + T cells (right panel) in s183-TCR mRNA electroporated T cells (red shaded area) compared with retrovirally transduced T cells (blue shaded area). The percentages of CD45RA +/- and CD62L +/- cells within total lymphocytes or the gated CD8 + pentamer + or CD4 + Vb3 + populations were determined by FACS. Cells were classified into different subsets: naive (CD45RA + CD62L + ), T CM (CD45RA − CD62L + ), T EM (CD45RA − CD62L − ) and terminally differentiated EM (CD45RA + CD62L − ). Results expressed as mean + SD ( n = 3).

    Journal: Molecular Therapy. Nucleic Acids

    Article Title: A Practical Approach to Immunotherapy of Hepatocellular Carcinoma Using T Cells Redirected Against Hepatitis B Virus

    doi: 10.1038/mtna.2013.43

    Figure Lengend Snippet: Similar signaling capacity and cytotocixity of mRNA electroporated and retrovirally transduced T cells . ( a ) Sensitivity of T-cell activation using T cells produced by mRNA electroporation compared with retroviral transduction. Results are displayed as percentage of maximum IFN-γ response obtained from intracellular cytokine staining. ( b ) Dose dependent lysis of HepG2-env targets (solid symbols and line) or HepG2-core targets (open symbols and dotted line) by electroporated T cells (triangle) compared with retrovirally transduced T cells (circle). Results are displayed as mean of triplicate measurements + SD. ( c ) Expression of perforin (left panel) and granzyme (right panel) on a representative activated T cells electroporated (red histograms) or retrovirally transduced (blue histograms) with s183-TCR, after 5 hours coculture with peptide-loaded T2 cells. Coculture with unpulsed T2 cells served as negative control (gray histograms). MFI of perforin and granzyme are indicated. ( d ) mRNA electroporated T cells have T CM -like phenotype. Phenotype of total lymphocytes (left panel), CD8 + pentamer + T cells (middle panel) and CD4 + Vb3 + T cells (right panel) in s183-TCR mRNA electroporated T cells (red shaded area) compared with retrovirally transduced T cells (blue shaded area). The percentages of CD45RA +/- and CD62L +/- cells within total lymphocytes or the gated CD8 + pentamer + or CD4 + Vb3 + populations were determined by FACS. Cells were classified into different subsets: naive (CD45RA + CD62L + ), T CM (CD45RA − CD62L + ), T EM (CD45RA − CD62L − ) and terminally differentiated EM (CD45RA + CD62L − ). Results expressed as mean + SD ( n = 3).

    Article Snippet: 2.0 × 108 activated T cells were suspended in 5 ml electroporation buffer (MaxCyte, Gaithersburg, MD); s183-TCR mRNA was added at 200 μg/ml.

    Techniques: Activation Assay, Produced, Electroporation, Transduction, Staining, Lysis, Expressing, Negative Control, FACS

    High level of TCR expression and multifunctionality of mRNA electroporated T cells produced in large-scale, clinical-grade conditions . A schematic illustrating cell numbers, efficiency, yield, and functionality of laboratory-grade (top row) vs. clinical-grade (bottom row) electroporation of T cells. Dot plot of CD8 and HLA-A2-HBs183-191 pentamer staining in s183-TCR mRNA electroporated T cells at 24 hours postelectroporation. Bar charts show the frequency of IFN-γ, TNF-α, and IL-2 producing cells out of CD8 or CD4 electroporated T cells.

    Journal: Molecular Therapy. Nucleic Acids

    Article Title: A Practical Approach to Immunotherapy of Hepatocellular Carcinoma Using T Cells Redirected Against Hepatitis B Virus

    doi: 10.1038/mtna.2013.43

    Figure Lengend Snippet: High level of TCR expression and multifunctionality of mRNA electroporated T cells produced in large-scale, clinical-grade conditions . A schematic illustrating cell numbers, efficiency, yield, and functionality of laboratory-grade (top row) vs. clinical-grade (bottom row) electroporation of T cells. Dot plot of CD8 and HLA-A2-HBs183-191 pentamer staining in s183-TCR mRNA electroporated T cells at 24 hours postelectroporation. Bar charts show the frequency of IFN-γ, TNF-α, and IL-2 producing cells out of CD8 or CD4 electroporated T cells.

    Article Snippet: 2.0 × 108 activated T cells were suspended in 5 ml electroporation buffer (MaxCyte, Gaithersburg, MD); s183-TCR mRNA was added at 200 μg/ml.

    Techniques: Expressing, Produced, Electroporation, Staining

    CRF protein homo- and heterodimerization. (A) CRF proteins CRF1–CRF8 and just the CRF domain of CRF2 (otherwise noted as CRFD) were analysed for potential homo- and heterodimerization using both BiFC and Y2H. Positive interactions are noted as a (+), (+*) for both BiFC and Y2H together, and (–) for non-interactions. (B) A cartoon of the conserved regions of CRF1–CRF6 proteins, the highly related CRF7 and CRF8 proteins (lacking the C-terminal third of the protein, but containing both the CRF domain and the AP2/ERF domain), and CRFD (just the CRF domain of CRF2). (C, D) Representative examples of positive CRF protein homo- and heterodimerization by BiFC as indicated in A are shown both under UV light in the presence of Hoechst 33342 dye denoting the nucleus and using a YFP wavelength filter to visualize BiFC interaction. Additionally, representative examples of empty vector (EV) controls for both N- and C-terminal BiFC vectors (EVn and EVc) examined in A are shown versus various CRFs and each other. (C) BiFC interactions in protoplasts transformed via electroporation. (D) BiFC interactions in tobacco leaves transformed via Agrobacterium .

    Journal: Journal of Experimental Botany

    Article Title: CRFs form protein-protein interactions with each other and with members of the cytokinin signalling pathway in Arabidopsis via the CRF domain

    doi: 10.1093/jxb/err199

    Figure Lengend Snippet: CRF protein homo- and heterodimerization. (A) CRF proteins CRF1–CRF8 and just the CRF domain of CRF2 (otherwise noted as CRFD) were analysed for potential homo- and heterodimerization using both BiFC and Y2H. Positive interactions are noted as a (+), (+*) for both BiFC and Y2H together, and (–) for non-interactions. (B) A cartoon of the conserved regions of CRF1–CRF6 proteins, the highly related CRF7 and CRF8 proteins (lacking the C-terminal third of the protein, but containing both the CRF domain and the AP2/ERF domain), and CRFD (just the CRF domain of CRF2). (C, D) Representative examples of positive CRF protein homo- and heterodimerization by BiFC as indicated in A are shown both under UV light in the presence of Hoechst 33342 dye denoting the nucleus and using a YFP wavelength filter to visualize BiFC interaction. Additionally, representative examples of empty vector (EV) controls for both N- and C-terminal BiFC vectors (EVn and EVc) examined in A are shown versus various CRFs and each other. (C) BiFC interactions in protoplasts transformed via electroporation. (D) BiFC interactions in tobacco leaves transformed via Agrobacterium .

    Article Snippet: Protoplasts were centrifuged again, washing buffer was removed, and then protoplasts were resuspended in a final volume of washing/transformation buffer prior to transformation and placed on ice until transformation, usually within 1 h. A 100 μl aliquot of transformation buffer containing ∼105 protoplasts along with ∼40–50 μg of plasmid DNA for each plasmid used were given two rapid pulses of 300 V for electroporation in a 0.1 mm electroporation cuvette using an Eppendorf Electroporator 2510.

    Techniques: Bimolecular Fluorescence Complementation Assay, Plasmid Preparation, Transformation Assay, Electroporation

    CRF protein interactions with members of the cytokinin signalling pathway. (A) CRF proteins, CRF1–CRF8, and CRFD (C-terminal) were analysed for potential interactions with TCS pathway proteins (N-terminal) using BiFC. Positive interactions are noted as (+) and non-interactions as (–). (B, C) Representative examples of positive and negative CRF protein interactions with TCS proteins as well as an empty vector control (EVc: C-terminal) by BiFC as indicated in A are shown both under UV light in the presence of Hoechst 33342 dye denoting the nucleus and using a YFP wavelength filter to visualize BiFC interaction. (B) BiFC interactions in protoplasts transformed via electroporation. (C) BiFC interactions in tobacco leaves transformed via Agrobacterium .

    Journal: Journal of Experimental Botany

    Article Title: CRFs form protein-protein interactions with each other and with members of the cytokinin signalling pathway in Arabidopsis via the CRF domain

    doi: 10.1093/jxb/err199

    Figure Lengend Snippet: CRF protein interactions with members of the cytokinin signalling pathway. (A) CRF proteins, CRF1–CRF8, and CRFD (C-terminal) were analysed for potential interactions with TCS pathway proteins (N-terminal) using BiFC. Positive interactions are noted as (+) and non-interactions as (–). (B, C) Representative examples of positive and negative CRF protein interactions with TCS proteins as well as an empty vector control (EVc: C-terminal) by BiFC as indicated in A are shown both under UV light in the presence of Hoechst 33342 dye denoting the nucleus and using a YFP wavelength filter to visualize BiFC interaction. (B) BiFC interactions in protoplasts transformed via electroporation. (C) BiFC interactions in tobacco leaves transformed via Agrobacterium .

    Article Snippet: Protoplasts were centrifuged again, washing buffer was removed, and then protoplasts were resuspended in a final volume of washing/transformation buffer prior to transformation and placed on ice until transformation, usually within 1 h. A 100 μl aliquot of transformation buffer containing ∼105 protoplasts along with ∼40–50 μg of plasmid DNA for each plasmid used were given two rapid pulses of 300 V for electroporation in a 0.1 mm electroporation cuvette using an Eppendorf Electroporator 2510.

    Techniques: Bimolecular Fluorescence Complementation Assay, Plasmid Preparation, Transformation Assay, Electroporation