non-transfected cells Search Results


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  • 99
    ATCC control non transfected l cells
    Control Non Transfected L Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore non transfected cos 7 parent cells
    DAGLα overexpression does not affect <t>COS-7</t> physiology and induces 2-AG accumulation. (a–b 2 ) Endogenously produced DAGLα in <t>non-transfected</t> COS-7 (“parent”) cells is undetectable by indirect immunohistochemistry ( open arrowheads ; a–a 2 ). In contrast, DAGLα, when highly expressed in COS-7 cells transfected with a DAGLα-V5 vector, accumulates in the plasma membrane ( solid arrowheads ; b–b 2 ). (c) COS-7-DAGLα cells expressed DAGLα protein and (c 1 ) synthesized 2-AG in a tetrahydrolipstatin (THL)-sensitive fashion. (d–d 3 ) DAGLα overexpression did not influence COS-7 cell morphology (d,d 1 ), including their surface area (d 2 ) and density in culture (d 3 ). Data were normalized to mean values from COS-7 “parent” cells. Abbreviations : n.s. = non significant. Scale bars = 20 μm (b,d 1 ).
    Non Transfected Cos 7 Parent Cells, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    GraphPad Prism Inc non transfected cells
    Activated caspase-8 and -9 positive cells were analyzed by flow cytometry at 3 days post transfection. Representative histogram showing the increase in caspase-8 and -9 staining in mutPKR (blue) and wtPKR (green) <t>transfected</t> cells relative to non-transfected control cells (white, in front).
    Non Transfected Cells, supplied by GraphPad Prism Inc, used in various techniques. Bioz Stars score: 94/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC non transfected l cells
    Activated caspase-8 and -9 positive cells were analyzed by flow cytometry at 3 days post transfection. Representative histogram showing the increase in caspase-8 and -9 staining in mutPKR (blue) and wtPKR (green) <t>transfected</t> cells relative to non-transfected control cells (white, in front).
    Non Transfected L Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    EUROIMMUN nontransfected control hek293 cells
    Activated caspase-8 and -9 positive cells were analyzed by flow cytometry at 3 days post transfection. Representative histogram showing the increase in caspase-8 and -9 staining in mutPKR (blue) and wtPKR (green) <t>transfected</t> cells relative to non-transfected control cells (white, in front).
    Nontransfected Control Hek293 Cells, supplied by EUROIMMUN, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    a549  (ATCC)
    99
    ATCC a549
    TGF-β1-induced CREB1 promotes the transcription of miR-1290. (A) A luciferase reporter vector with the miR-1290 promoter was constructed and co-transfected into 293 cells with pcDNA3.1/CREB1. Luciferase activity was determined in the presence or absence of TGF-β1. (B) CREB1 overexpression was achieved in <t>A549</t> cells by transfection of the CREB1 overexpression vector (CREB1 OE), as confirmed by RT-qPCR. (C) miR-1290 expression was determined in CREB1-overexpressing A549 cells by RT-qPCR. (D) Schematic diagram showing that TGF-β1-induced CREB1 promotes the transcription of miR-1290, therefore inhibiting Napsin A expression and promoting pulmonary fibrosis. * P
    A549, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 8394 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Santa Cruz Biotechnology and mouse non transfected cell lysates
    TGF-β1-induced CREB1 promotes the transcription of miR-1290. (A) A luciferase reporter vector with the miR-1290 promoter was constructed and co-transfected into 293 cells with pcDNA3.1/CREB1. Luciferase activity was determined in the presence or absence of TGF-β1. (B) CREB1 overexpression was achieved in <t>A549</t> cells by transfection of the CREB1 overexpression vector (CREB1 OE), as confirmed by RT-qPCR. (C) miR-1290 expression was determined in CREB1-overexpressing A549 cells by RT-qPCR. (D) Schematic diagram showing that TGF-β1-induced CREB1 promotes the transcription of miR-1290, therefore inhibiting Napsin A expression and promoting pulmonary fibrosis. * P
    And Mouse Non Transfected Cell Lysates, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC nontransfected hek293 cells
    TGF-β1-induced CREB1 promotes the transcription of miR-1290. (A) A luciferase reporter vector with the miR-1290 promoter was constructed and co-transfected into 293 cells with pcDNA3.1/CREB1. Luciferase activity was determined in the presence or absence of TGF-β1. (B) CREB1 overexpression was achieved in <t>A549</t> cells by transfection of the CREB1 overexpression vector (CREB1 OE), as confirmed by RT-qPCR. (C) miR-1290 expression was determined in CREB1-overexpressing A549 cells by RT-qPCR. (D) Schematic diagram showing that TGF-β1-induced CREB1 promotes the transcription of miR-1290, therefore inhibiting Napsin A expression and promoting pulmonary fibrosis. * P
    Nontransfected Hek293 Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Becton Dickinson control non transfected cells
    scFv1 A1 binds to human Kit-expressing MCBS1 mouse mast cells. Kit expression was confirmed by flow cytometry ( a ) and immunofluorescence ( b ). a Fluorescent histograms (red lines), plotted with corresponding isotype controls (blue line) demonstrate A1 and Kit expression in the W1-AA677 human Kit-expressing mouse mast cell line, but not in E1-AA685 <t>mock-transfected</t> cells or non-transfected control cells. The mean fluorescent intensity was determined minus the total binding of matched isotype controls for A1 and Kit, scFv E4 and mouse IgG respectively. Representative of 3 independent experiments. b Immunofluorescent staining of W1-AA677, E1-AA685 and control cells. Nuclei stained blue with DAPI, A1 and Kit stained red (RPE); inset: isotype control. Representative of two independent experiments
    Control Non Transfected Cells, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 88/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC hela cells
    Steady-state levels of wild-type and G319S HNF-1α protein. <t>HeLa</t> cells were <t>transfected</t> with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.
    Hela Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 24553 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    ATCC human squamous esophageal cell line transfected non tumorigenic sv40 t
    Steady-state levels of wild-type and G319S HNF-1α protein. <t>HeLa</t> cells were <t>transfected</t> with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.
    Human Squamous Esophageal Cell Line Transfected Non Tumorigenic Sv40 T, supplied by ATCC, used in various techniques. Bioz Stars score: 98/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC transfections human non invasive breast cancer cells mcf 7
    Steady-state levels of wild-type and G319S HNF-1α protein. <t>HeLa</t> cells were <t>transfected</t> with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.
    Transfections Human Non Invasive Breast Cancer Cells Mcf 7, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    ATCC transfection mcf 12f non cancerous mammary cells
    Steady-state levels of wild-type and G319S HNF-1α protein. <t>HeLa</t> cells were <t>transfected</t> with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.
    Transfection Mcf 12f Non Cancerous Mammary Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC transfections non cancerous rwpe 1 human prostate epithelial cells
    Steady-state levels of wild-type and G319S HNF-1α protein. <t>HeLa</t> cells were <t>transfected</t> with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.
    Transfections Non Cancerous Rwpe 1 Human Prostate Epithelial Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Millipore es r1 egfp b5 egfp
    Steady-state levels of wild-type and G319S HNF-1α protein. <t>HeLa</t> cells were <t>transfected</t> with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.
    Es R1 Egfp B5 Egfp, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    INCELL Corp ncm460 non transfected human colonic epithelial cells
    Steady-state levels of wild-type and G319S HNF-1α protein. <t>HeLa</t> cells were <t>transfected</t> with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.
    Ncm460 Non Transfected Human Colonic Epithelial Cells, supplied by INCELL Corp, used in various techniques. Bioz Stars score: 89/100, based on 81 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    SIRION Biotech non target transfected bewo cell line
    Steady-state levels of wild-type and G319S HNF-1α protein. <t>HeLa</t> cells were <t>transfected</t> with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.
    Non Target Transfected Bewo Cell Line, supplied by SIRION Biotech, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    InvivoGen non transfected hek cell line
    Steady-state levels of wild-type and G319S HNF-1α protein. <t>HeLa</t> cells were <t>transfected</t> with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.
    Non Transfected Hek Cell Line, supplied by InvivoGen, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC non transfected cho k1 cells
    Roles of SR CD36 (A-E) and SR-A (G-I) as receptors for HOCl-modified proteins. ( A ) Uptake of fluorescently-labelled proteins by <t>CHO</t> cells <t>transfected</t> with human CD36 as compared to non-transfected cells. ( B ) Binding of anti-CD36 mAb and control mouse IgA to CD36-transfected and non-transfected CHO cells, determined by cellular ELISA. ( C ) Binding of rCD36 to plate-adsorbed proteins. ( D ) Effects of 10 or 100 μg/ml of indicated, soluble ligands on rCD36 binding to plate-adsorbed OVA-Cl. ( E ) Binding of polyclonal anti-mouse CD36 Ab and control goat IgG to BM-DC, splenic DC and PEM. A representative histogram of Ab binding to BM-DC is displayed on the left graph. ( F ) Binding of anti-mouse SR-A mAb and control rat IgG2b to BM-DC, splenic DC and PEM. A representative histogram of Ab binding to BM-DC is shown on the left graph. ( G ) Binding of SR-A present in lysates of PEM to plate-adsorbed proteins. ( H ) Effects of anti-SR-A 2F8 mAb and AcLDL on the uptake of fluorescently-labelled proteins by BM-DC. Shown are results of single experiments, each representative of at least 3 similar experiments performed (A-D, G, H) or averages +SEM from 4–6 independent experiments (E, F). The data were analysed with the unpaired (A-C, G) or one-sample (H) Student’s t-test or with ANOVA, followed by the Tukey-Kramer post-test (D). *, p
    Non Transfected Cho K1 Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Agilent technologies non transfected cells
    Roles of SR CD36 (A-E) and SR-A (G-I) as receptors for HOCl-modified proteins. ( A ) Uptake of fluorescently-labelled proteins by <t>CHO</t> cells <t>transfected</t> with human CD36 as compared to non-transfected cells. ( B ) Binding of anti-CD36 mAb and control mouse IgA to CD36-transfected and non-transfected CHO cells, determined by cellular ELISA. ( C ) Binding of rCD36 to plate-adsorbed proteins. ( D ) Effects of 10 or 100 μg/ml of indicated, soluble ligands on rCD36 binding to plate-adsorbed OVA-Cl. ( E ) Binding of polyclonal anti-mouse CD36 Ab and control goat IgG to BM-DC, splenic DC and PEM. A representative histogram of Ab binding to BM-DC is displayed on the left graph. ( F ) Binding of anti-mouse SR-A mAb and control rat IgG2b to BM-DC, splenic DC and PEM. A representative histogram of Ab binding to BM-DC is shown on the left graph. ( G ) Binding of SR-A present in lysates of PEM to plate-adsorbed proteins. ( H ) Effects of anti-SR-A 2F8 mAb and AcLDL on the uptake of fluorescently-labelled proteins by BM-DC. Shown are results of single experiments, each representative of at least 3 similar experiments performed (A-D, G, H) or averages +SEM from 4–6 independent experiments (E, F). The data were analysed with the unpaired (A-C, G) or one-sample (H) Student’s t-test or with ANOVA, followed by the Tukey-Kramer post-test (D). *, p
    Non Transfected Cells, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 91/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Amaxa non transfected cells
    The down-regulation of SUMO-1 made mouse cortical neurons more sensitive to OGD/ROG and the SUMO-1-depleted neurons show reduced protection by preconditioning. (a) SUMO-1 (left panel) and SUMO-2/3 (right panel) protein levels in total cell lysates from mouse cortical neurons treated with various siRNAs. Upper panels: representative PAGE/WB pictures. Lower panels: quantitative analyses of densities. Data are shown as means ± SD ( n = 3). (b) Sensitivities to OGD/ROG among siRNA-treated cells. Cell death was measured with Hoechst 33342 and PI followed by FACS analysis. Data here are shown as means ± SD ( n = 3). (c) Mouse cortical neurons that had been <t>transfected</t> with AllStar siRNA or SUMO-1 siRNA were subjected to a harmful OGD/ROG with or without preconditioning (30 min OGD). Cell deaths were measured as mentioned above. Data here are shown as means ± SD ( n = 3).
    Non Transfected Cells, supplied by Amaxa, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    MatTek non transfected cells
    Caveolin1-GFP Clusters Are Generated by EHD Proteins (A) TIR microscopy to show the distribution of caveolin1-GFP in gene-edited WT and ΔEHD1,2,4 NIH 3T3 cells. Scale bar, 10 μm. (B) Quantification of puncta size in TIR images as shown in (A), shown as frequency distribution of all sizes detected in 10 cells of each genotype shown. (C) Confocal and stimulated emission depletion (STED) microscopy of WT cells, ΔEHD1,2,4 cells, and ΔEHD1,2,4 cells expressing mCherry-EHD1, mCherry-EHD2, and mCherry-EHD4 by transient transfection. All cells are gene edited to express caveolin1-GFP. The STED images are of the boxed region in the confocal images. Scale bars, 5 μm (in confocal images) and 1 μm (in STED images). (D) Electron micrographs of ΔEHD1,2,4 cells expressing mitochondrially targeted APEX, mCherry-EHD1, mCherry-EHD2, and mCherry-EHD4 by transient transfection. Cells were stained with diaminobenzidine, producing electron-dense deposits in the mitochondria of <t>transfected</t> cells. Two cells are shown; arrows highlight mitochondria, and the boxed regions are shown at higher magnification in the additional panels. Scale bars, 500 nm.
    Non Transfected Cells, supplied by MatTek, used in various techniques. Bioz Stars score: 91/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    DAGLα overexpression does not affect COS-7 physiology and induces 2-AG accumulation. (a–b 2 ) Endogenously produced DAGLα in non-transfected COS-7 (“parent”) cells is undetectable by indirect immunohistochemistry ( open arrowheads ; a–a 2 ). In contrast, DAGLα, when highly expressed in COS-7 cells transfected with a DAGLα-V5 vector, accumulates in the plasma membrane ( solid arrowheads ; b–b 2 ). (c) COS-7-DAGLα cells expressed DAGLα protein and (c 1 ) synthesized 2-AG in a tetrahydrolipstatin (THL)-sensitive fashion. (d–d 3 ) DAGLα overexpression did not influence COS-7 cell morphology (d,d 1 ), including their surface area (d 2 ) and density in culture (d 3 ). Data were normalized to mean values from COS-7 “parent” cells. Abbreviations : n.s. = non significant. Scale bars = 20 μm (b,d 1 ).

    Journal: Scientific Reports

    Article Title: Diacylglycerol lipase ? manipulation reveals developmental roles for intercellular endocannabinoid signaling

    doi: 10.1038/srep02093

    Figure Lengend Snippet: DAGLα overexpression does not affect COS-7 physiology and induces 2-AG accumulation. (a–b 2 ) Endogenously produced DAGLα in non-transfected COS-7 (“parent”) cells is undetectable by indirect immunohistochemistry ( open arrowheads ; a–a 2 ). In contrast, DAGLα, when highly expressed in COS-7 cells transfected with a DAGLα-V5 vector, accumulates in the plasma membrane ( solid arrowheads ; b–b 2 ). (c) COS-7-DAGLα cells expressed DAGLα protein and (c 1 ) synthesized 2-AG in a tetrahydrolipstatin (THL)-sensitive fashion. (d–d 3 ) DAGLα overexpression did not influence COS-7 cell morphology (d,d 1 ), including their surface area (d 2 ) and density in culture (d 3 ). Data were normalized to mean values from COS-7 “parent” cells. Abbreviations : n.s. = non significant. Scale bars = 20 μm (b,d 1 ).

    Article Snippet: We verified DAGLα overexpression by lysing COS-7-DAGLα and non-transfected COS-7 (“parent”) cells in modified radioimmunoprecipitation assay buffer containing 5 mM NaF, 5 mM Na3 VO4 , 1% Triton X-100, 0.1% N -octyl-β-D-glucopyranoside (Calbiochem) and a mixture of protease inhibitors (Complete®, EDTA-free, Roche), denatured in Laemmli's buffer, and analyzed by SDS-PAGE.

    Techniques: Over Expression, Produced, Transfection, Immunohistochemistry, Plasmid Preparation, Synthesized

    Activated caspase-8 and -9 positive cells were analyzed by flow cytometry at 3 days post transfection. Representative histogram showing the increase in caspase-8 and -9 staining in mutPKR (blue) and wtPKR (green) transfected cells relative to non-transfected control cells (white, in front).

    Journal: Viruses

    Article Title: Apoptosis Induction by dsRNA-Dependent Protein Kinase R (PKR) in EPC Cells via Caspase 8 and 9 Pathways

    doi: 10.3390/v10100526

    Figure Lengend Snippet: Activated caspase-8 and -9 positive cells were analyzed by flow cytometry at 3 days post transfection. Representative histogram showing the increase in caspase-8 and -9 staining in mutPKR (blue) and wtPKR (green) transfected cells relative to non-transfected control cells (white, in front).

    Article Snippet: This is in contrast to the mutPKR transfected cells that had a fluorescence intensity level not different from the non-transfected cells ( ).

    Techniques: Flow Cytometry, Cytometry, Transfection, Staining

    Percentage activated caspase-8 positive cells was about three-fold higher in the wtPKR transfected cells than in mutPKR cells ( p = 0.0083), while activated caspase-9 was 2.5-fold higher in wtPKR compared to mutPKR transfected cells ( p = 0.0008). The p -values for wtPKR versus non-transfected (NT) are also shown while p values for mutPKR versus NT were both > 0.05.

    Journal: Viruses

    Article Title: Apoptosis Induction by dsRNA-Dependent Protein Kinase R (PKR) in EPC Cells via Caspase 8 and 9 Pathways

    doi: 10.3390/v10100526

    Figure Lengend Snippet: Percentage activated caspase-8 positive cells was about three-fold higher in the wtPKR transfected cells than in mutPKR cells ( p = 0.0083), while activated caspase-9 was 2.5-fold higher in wtPKR compared to mutPKR transfected cells ( p = 0.0008). The p -values for wtPKR versus non-transfected (NT) are also shown while p values for mutPKR versus NT were both > 0.05.

    Article Snippet: This is in contrast to the mutPKR transfected cells that had a fluorescence intensity level not different from the non-transfected cells ( ).

    Techniques: Transfection

    Expression of protein kinase R (PKR), phosphorylated eIF2α (p-eIF2α), and β-actin in Epithelioma papulosum cyprini (EPC) cells transfected with the wild type pcDNA-wtcarpPKR (wtPKR) and mutant pcDNA-mutcarpPKR (mutPKR), respectively. Negative control, non-transfected cells, were NF. Samples were analyzed at three time-points, 16, 24, and 40 h post transfection (hpt). PKR was not detected at any time point in wtPKR transfected cells, but positive in mutPKR cells, progressively increasing from 16 to 40 hpt. eIF2α was phosphorylated wtPKR cells, decreasing from 16 to 40 hpt. No difference in the phosphorylation levels of eIF2α between mutPKR and NF. β-actin was expressed at the same level from all samples at all sampling points.

    Journal: Viruses

    Article Title: Apoptosis Induction by dsRNA-Dependent Protein Kinase R (PKR) in EPC Cells via Caspase 8 and 9 Pathways

    doi: 10.3390/v10100526

    Figure Lengend Snippet: Expression of protein kinase R (PKR), phosphorylated eIF2α (p-eIF2α), and β-actin in Epithelioma papulosum cyprini (EPC) cells transfected with the wild type pcDNA-wtcarpPKR (wtPKR) and mutant pcDNA-mutcarpPKR (mutPKR), respectively. Negative control, non-transfected cells, were NF. Samples were analyzed at three time-points, 16, 24, and 40 h post transfection (hpt). PKR was not detected at any time point in wtPKR transfected cells, but positive in mutPKR cells, progressively increasing from 16 to 40 hpt. eIF2α was phosphorylated wtPKR cells, decreasing from 16 to 40 hpt. No difference in the phosphorylation levels of eIF2α between mutPKR and NF. β-actin was expressed at the same level from all samples at all sampling points.

    Article Snippet: This is in contrast to the mutPKR transfected cells that had a fluorescence intensity level not different from the non-transfected cells ( ).

    Techniques: Expressing, Transfection, Mutagenesis, Negative Control, Sampling

    Quantification of eIF2α phosphorylation after transfection of pcDNA-wtPKR and pcDNA-mutPKR, and non-transfected controls in EPC and AGK cells at different time. p-eIF2α is measured by densitometry, expressed relative to β-actin. Representative data from three independent experiments are shown (mean ± SEM, n = 3). The different letters above the bars indicate significant differences ( p

    Journal: Viruses

    Article Title: Apoptosis Induction by dsRNA-Dependent Protein Kinase R (PKR) in EPC Cells via Caspase 8 and 9 Pathways

    doi: 10.3390/v10100526

    Figure Lengend Snippet: Quantification of eIF2α phosphorylation after transfection of pcDNA-wtPKR and pcDNA-mutPKR, and non-transfected controls in EPC and AGK cells at different time. p-eIF2α is measured by densitometry, expressed relative to β-actin. Representative data from three independent experiments are shown (mean ± SEM, n = 3). The different letters above the bars indicate significant differences ( p

    Article Snippet: This is in contrast to the mutPKR transfected cells that had a fluorescence intensity level not different from the non-transfected cells ( ).

    Techniques: Transfection

    Cytopathic effects (CPE) and the percentage of apoptotic cells in EPC cells transfected with the wtPKR, mutPKR, and pcDNA3.1-myc-His plasmids (controls), respectively, 72 h post transfection. ( a ) Distinct CPE in cells transfected with the wtPKR. Cells transfected with mutPKR and pcDNA3.1-myc-His had insignificant CPE and both showing confluent monolayers, 72 h post transfection. Bar = 10 μm. ( b ) Flow cytometry analysis of Annexin V-Fluos and propidium iodide staining of apoptotic cells at 72 h post transfection. Each bar represents the average results of two independent experiments, three replicates in each. Percentage apoptotic cells in the wtPKR transfected cells was two-fold higher than in mutPKR cells ( p = 0.0004) and compared to empty plasmid control, at 3 days post transfection (dpt). There was no significant difference between mutPKR and pcDNA3.1-myc-His transfected cells.

    Journal: Viruses

    Article Title: Apoptosis Induction by dsRNA-Dependent Protein Kinase R (PKR) in EPC Cells via Caspase 8 and 9 Pathways

    doi: 10.3390/v10100526

    Figure Lengend Snippet: Cytopathic effects (CPE) and the percentage of apoptotic cells in EPC cells transfected with the wtPKR, mutPKR, and pcDNA3.1-myc-His plasmids (controls), respectively, 72 h post transfection. ( a ) Distinct CPE in cells transfected with the wtPKR. Cells transfected with mutPKR and pcDNA3.1-myc-His had insignificant CPE and both showing confluent monolayers, 72 h post transfection. Bar = 10 μm. ( b ) Flow cytometry analysis of Annexin V-Fluos and propidium iodide staining of apoptotic cells at 72 h post transfection. Each bar represents the average results of two independent experiments, three replicates in each. Percentage apoptotic cells in the wtPKR transfected cells was two-fold higher than in mutPKR cells ( p = 0.0004) and compared to empty plasmid control, at 3 days post transfection (dpt). There was no significant difference between mutPKR and pcDNA3.1-myc-His transfected cells.

    Article Snippet: This is in contrast to the mutPKR transfected cells that had a fluorescence intensity level not different from the non-transfected cells ( ).

    Techniques: Transfection, Flow Cytometry, Cytometry, Staining, Plasmid Preparation

    TGF-β1-induced CREB1 promotes the transcription of miR-1290. (A) A luciferase reporter vector with the miR-1290 promoter was constructed and co-transfected into 293 cells with pcDNA3.1/CREB1. Luciferase activity was determined in the presence or absence of TGF-β1. (B) CREB1 overexpression was achieved in A549 cells by transfection of the CREB1 overexpression vector (CREB1 OE), as confirmed by RT-qPCR. (C) miR-1290 expression was determined in CREB1-overexpressing A549 cells by RT-qPCR. (D) Schematic diagram showing that TGF-β1-induced CREB1 promotes the transcription of miR-1290, therefore inhibiting Napsin A expression and promoting pulmonary fibrosis. * P

    Journal: International Journal of Molecular Medicine

    Article Title: TGF-β1 induces CREB1-mediated miR-1290 upregulation to antagonize lung fibrosis via Napsin A

    doi: 10.3892/ijmm.2020.4565

    Figure Lengend Snippet: TGF-β1-induced CREB1 promotes the transcription of miR-1290. (A) A luciferase reporter vector with the miR-1290 promoter was constructed and co-transfected into 293 cells with pcDNA3.1/CREB1. Luciferase activity was determined in the presence or absence of TGF-β1. (B) CREB1 overexpression was achieved in A549 cells by transfection of the CREB1 overexpression vector (CREB1 OE), as confirmed by RT-qPCR. (C) miR-1290 expression was determined in CREB1-overexpressing A549 cells by RT-qPCR. (D) Schematic diagram showing that TGF-β1-induced CREB1 promotes the transcription of miR-1290, therefore inhibiting Napsin A expression and promoting pulmonary fibrosis. * P

    Article Snippet: Cell lines and cell transfection A human non-small cell lung cancer cell line (A549; ATCC® CCL-185) and a normal human lung epithelial cell line (BEAS-2B; ATCC® CRL-9609) were purchased from ATCC and cultured in F-12K medium (for A549 cells, cat. no. 30-2004, ATCC) or bronchial epithelial basal medium BEBM (for BEAS-2B cells, Lonza/Clonetics Corp.) supplemented with 10% FBS.

    Techniques: Luciferase, Plasmid Preparation, Construct, Transfection, Activity Assay, Over Expression, Quantitative RT-PCR, Expressing

    miR-1290 expression is upregulated in blood samples from patients with pulmonary fibrosis and in TGF-β1-stimulated A549 cells. (A and B) miR-1290 and Napsin A expression levels in blood samples obtained from healthy volunteers (negative control) and patients with pulmonary fibrosis. (C) The correlation of miR-1290 and Napsin A expression in blood samples was analyzed by Pearson's correlation analysis. A549 cells were treated with TGF-β1 and examined for (D) α-SMA protein content (green) by immunofluorescence staining. (E) Protein levels of Napsin A, α-SMA, Collagen I, AKT and p-AKT were assessed by western blot analysis. (F) Expression of miR-1290 was assessed by RT-qPCR. * P

    Journal: International Journal of Molecular Medicine

    Article Title: TGF-β1 induces CREB1-mediated miR-1290 upregulation to antagonize lung fibrosis via Napsin A

    doi: 10.3892/ijmm.2020.4565

    Figure Lengend Snippet: miR-1290 expression is upregulated in blood samples from patients with pulmonary fibrosis and in TGF-β1-stimulated A549 cells. (A and B) miR-1290 and Napsin A expression levels in blood samples obtained from healthy volunteers (negative control) and patients with pulmonary fibrosis. (C) The correlation of miR-1290 and Napsin A expression in blood samples was analyzed by Pearson's correlation analysis. A549 cells were treated with TGF-β1 and examined for (D) α-SMA protein content (green) by immunofluorescence staining. (E) Protein levels of Napsin A, α-SMA, Collagen I, AKT and p-AKT were assessed by western blot analysis. (F) Expression of miR-1290 was assessed by RT-qPCR. * P

    Article Snippet: Cell lines and cell transfection A human non-small cell lung cancer cell line (A549; ATCC® CCL-185) and a normal human lung epithelial cell line (BEAS-2B; ATCC® CRL-9609) were purchased from ATCC and cultured in F-12K medium (for A549 cells, cat. no. 30-2004, ATCC) or bronchial epithelial basal medium BEBM (for BEAS-2B cells, Lonza/Clonetics Corp.) supplemented with 10% FBS.

    Techniques: Expressing, Negative Control, Immunofluorescence, Staining, Western Blot, Quantitative RT-PCR

    miR-1290 directly targets Napsin A to modulate A549 cell proliferation and TGF-β1-induced fibrosis. (A) Schematic diagram showing the predicted binding site between miR-1290 and Napsin A 3′UTR. Wild- and mutant-type Napsin A 3′UTR luciferase reporter vectors were constructed. The mutant-type Napsin A 3′UTR vector contained a 7-bp mutation in the predicted miR-1290 binding site. These vectors were co-transfected into 293 cells with miR-1290 mimics or inhibitor and the luciferase activity was determined. (B) miR-1290 overexpression and inhibition in A549 cells were achieved by transfection with miR-1290 mimics or an inhibitor, and results were confirmed by RT-qPCR. (C) Napsin A mRNA expression in response to miR-1290 overexpression or inhibition was determined by RT-qPCR. (D) Viability of A549 cells in which miR-1290 was overexpressed or inhibited was determined by MTT assays. (E) Protein levels of Napsin A, α-SMA, Collagen I, AKT and p-AKT in A549 cells in which miR-1290 was overexpressed or inhibited were determined by western blot analysis. * P

    Journal: International Journal of Molecular Medicine

    Article Title: TGF-β1 induces CREB1-mediated miR-1290 upregulation to antagonize lung fibrosis via Napsin A

    doi: 10.3892/ijmm.2020.4565

    Figure Lengend Snippet: miR-1290 directly targets Napsin A to modulate A549 cell proliferation and TGF-β1-induced fibrosis. (A) Schematic diagram showing the predicted binding site between miR-1290 and Napsin A 3′UTR. Wild- and mutant-type Napsin A 3′UTR luciferase reporter vectors were constructed. The mutant-type Napsin A 3′UTR vector contained a 7-bp mutation in the predicted miR-1290 binding site. These vectors were co-transfected into 293 cells with miR-1290 mimics or inhibitor and the luciferase activity was determined. (B) miR-1290 overexpression and inhibition in A549 cells were achieved by transfection with miR-1290 mimics or an inhibitor, and results were confirmed by RT-qPCR. (C) Napsin A mRNA expression in response to miR-1290 overexpression or inhibition was determined by RT-qPCR. (D) Viability of A549 cells in which miR-1290 was overexpressed or inhibited was determined by MTT assays. (E) Protein levels of Napsin A, α-SMA, Collagen I, AKT and p-AKT in A549 cells in which miR-1290 was overexpressed or inhibited were determined by western blot analysis. * P

    Article Snippet: Cell lines and cell transfection A human non-small cell lung cancer cell line (A549; ATCC® CCL-185) and a normal human lung epithelial cell line (BEAS-2B; ATCC® CRL-9609) were purchased from ATCC and cultured in F-12K medium (for A549 cells, cat. no. 30-2004, ATCC) or bronchial epithelial basal medium BEBM (for BEAS-2B cells, Lonza/Clonetics Corp.) supplemented with 10% FBS.

    Techniques: Binding Assay, Mutagenesis, Luciferase, Construct, Plasmid Preparation, Transfection, Activity Assay, Over Expression, Inhibition, Quantitative RT-PCR, Expressing, MTT Assay, Western Blot

    Dynamic effects of miR-1290 and Napsin A on A549 cell proliferation and TGF-β1-induced fibrosis (A) Napsin A knockdown was conducted by the transfection of si-Napsin A, as confirmed by RT-qPCR. A549 cells were co-transfected with miR-1290 inhibitor and si-Napsin A upon TGF-β1 stimulation and examined for (B) the expression of Napsin A, as determined by RT-qPCR; (C) cell viability, as determined by MTT assays; and (D) the protein levels of Napsin A, α-SMA, Collagen I, AKT and p-AKT as determined by western blot analysis. * P

    Journal: International Journal of Molecular Medicine

    Article Title: TGF-β1 induces CREB1-mediated miR-1290 upregulation to antagonize lung fibrosis via Napsin A

    doi: 10.3892/ijmm.2020.4565

    Figure Lengend Snippet: Dynamic effects of miR-1290 and Napsin A on A549 cell proliferation and TGF-β1-induced fibrosis (A) Napsin A knockdown was conducted by the transfection of si-Napsin A, as confirmed by RT-qPCR. A549 cells were co-transfected with miR-1290 inhibitor and si-Napsin A upon TGF-β1 stimulation and examined for (B) the expression of Napsin A, as determined by RT-qPCR; (C) cell viability, as determined by MTT assays; and (D) the protein levels of Napsin A, α-SMA, Collagen I, AKT and p-AKT as determined by western blot analysis. * P

    Article Snippet: Cell lines and cell transfection A human non-small cell lung cancer cell line (A549; ATCC® CCL-185) and a normal human lung epithelial cell line (BEAS-2B; ATCC® CRL-9609) were purchased from ATCC and cultured in F-12K medium (for A549 cells, cat. no. 30-2004, ATCC) or bronchial epithelial basal medium BEBM (for BEAS-2B cells, Lonza/Clonetics Corp.) supplemented with 10% FBS.

    Techniques: Transfection, Quantitative RT-PCR, Expressing, MTT Assay, Western Blot

    scFv1 A1 binds to human Kit-expressing MCBS1 mouse mast cells. Kit expression was confirmed by flow cytometry ( a ) and immunofluorescence ( b ). a Fluorescent histograms (red lines), plotted with corresponding isotype controls (blue line) demonstrate A1 and Kit expression in the W1-AA677 human Kit-expressing mouse mast cell line, but not in E1-AA685 mock-transfected cells or non-transfected control cells. The mean fluorescent intensity was determined minus the total binding of matched isotype controls for A1 and Kit, scFv E4 and mouse IgG respectively. Representative of 3 independent experiments. b Immunofluorescent staining of W1-AA677, E1-AA685 and control cells. Nuclei stained blue with DAPI, A1 and Kit stained red (RPE); inset: isotype control. Representative of two independent experiments

    Journal: Respiratory Research

    Article Title: Evidence for a novel Kit adhesion domain mediating human mast cell adhesion to structural airway cells

    doi: 10.1186/s12931-015-0245-z

    Figure Lengend Snippet: scFv1 A1 binds to human Kit-expressing MCBS1 mouse mast cells. Kit expression was confirmed by flow cytometry ( a ) and immunofluorescence ( b ). a Fluorescent histograms (red lines), plotted with corresponding isotype controls (blue line) demonstrate A1 and Kit expression in the W1-AA677 human Kit-expressing mouse mast cell line, but not in E1-AA685 mock-transfected cells or non-transfected control cells. The mean fluorescent intensity was determined minus the total binding of matched isotype controls for A1 and Kit, scFv E4 and mouse IgG respectively. Representative of 3 independent experiments. b Immunofluorescent staining of W1-AA677, E1-AA685 and control cells. Nuclei stained blue with DAPI, A1 and Kit stained red (RPE); inset: isotype control. Representative of two independent experiments

    Article Snippet: Control non transfected cells, mock transfected cells (E1-AA685) or human Kit-transfected cells (W1-AA677) were stained with 4 ug/mL PE-labelled anti-Kit mAb (BD Bioscience, Oxford, UK) or 5 μg/mL A1 scFv antibody followed by 9E10 (anti-myc) secondary antibody, which was then indirectly labelled with R-Phycoerythrin (PE)-labelled rabbit anti-mouse antibody (Dako, UK).

    Techniques: Expressing, Flow Cytometry, Cytometry, Immunofluorescence, Transfection, Binding Assay, Staining

    Steady-state levels of wild-type and G319S HNF-1α protein. HeLa cells were transfected with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: HNF-1? G319S, a transactivation-deficient mutant, is associated with altered dynamics of diabetes onset in an Oji-Cree community

    doi: 10.1073/pnas.062059799

    Figure Lengend Snippet: Steady-state levels of wild-type and G319S HNF-1α protein. HeLa cells were transfected with 4 μg of pcDNA3.1/HisC WT-HNF-1α or pcDNA3 1/HisC G319S HNF-1α and 200 ng of pRL-TK. Equivalent units of Renilla luciferase (expressed from pRL-TK) activity were loaded from each of two replicates that were performed for each construct. HNF-1α was detected with a 1:5,000 dilution of the primary antibody toward the Xpress epitope and a 1:10,000 dilution of the secondary anti-mouse antibody. The ECL signal was detected using Kodak MS x-ray film. In addition, each lane was quantitated (1–268, 2–231, 3–262, and 4–227) as described in Methods . The average signal for the G319S mutant protein was 98% of that of the signal from the wild-type protein. An arrow indicates the HNF-1α protein. This gel is representative of three experiments.

    Article Snippet: Nuclear protein extracts from HeLa cells (nontransfected and transfected with 1 μg of wild-type or G319S-containing cDNA expression vector) were prepared as reported ( ).

    Techniques: Transfection, Luciferase, Activity Assay, Construct, Mass Spectrometry, Mutagenesis

    Transcriptional activity of wild-type (WT) and G319S HNF-1α. HeLa cells were transfected with 400 ng of pcDNA3.1/HisC wild-type HNF-1α, pcDNA3.1/HisC G319S HNF-1α, or the vector pcDNA3.1/HisC together with 1 μg of the reporter vector pGL3-TTR and 100 ng of pRL-TK ( A ; * P

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: HNF-1? G319S, a transactivation-deficient mutant, is associated with altered dynamics of diabetes onset in an Oji-Cree community

    doi: 10.1073/pnas.062059799

    Figure Lengend Snippet: Transcriptional activity of wild-type (WT) and G319S HNF-1α. HeLa cells were transfected with 400 ng of pcDNA3.1/HisC wild-type HNF-1α, pcDNA3.1/HisC G319S HNF-1α, or the vector pcDNA3.1/HisC together with 1 μg of the reporter vector pGL3-TTR and 100 ng of pRL-TK ( A ; * P

    Article Snippet: Nuclear protein extracts from HeLa cells (nontransfected and transfected with 1 μg of wild-type or G319S-containing cDNA expression vector) were prepared as reported ( ).

    Techniques: Activity Assay, Transfection, Plasmid Preparation

    Roles of SR CD36 (A-E) and SR-A (G-I) as receptors for HOCl-modified proteins. ( A ) Uptake of fluorescently-labelled proteins by CHO cells transfected with human CD36 as compared to non-transfected cells. ( B ) Binding of anti-CD36 mAb and control mouse IgA to CD36-transfected and non-transfected CHO cells, determined by cellular ELISA. ( C ) Binding of rCD36 to plate-adsorbed proteins. ( D ) Effects of 10 or 100 μg/ml of indicated, soluble ligands on rCD36 binding to plate-adsorbed OVA-Cl. ( E ) Binding of polyclonal anti-mouse CD36 Ab and control goat IgG to BM-DC, splenic DC and PEM. A representative histogram of Ab binding to BM-DC is displayed on the left graph. ( F ) Binding of anti-mouse SR-A mAb and control rat IgG2b to BM-DC, splenic DC and PEM. A representative histogram of Ab binding to BM-DC is shown on the left graph. ( G ) Binding of SR-A present in lysates of PEM to plate-adsorbed proteins. ( H ) Effects of anti-SR-A 2F8 mAb and AcLDL on the uptake of fluorescently-labelled proteins by BM-DC. Shown are results of single experiments, each representative of at least 3 similar experiments performed (A-D, G, H) or averages +SEM from 4–6 independent experiments (E, F). The data were analysed with the unpaired (A-C, G) or one-sample (H) Student’s t-test or with ANOVA, followed by the Tukey-Kramer post-test (D). *, p

    Journal: PLoS ONE

    Article Title: Oxidation by Neutrophils-Derived HOCl Increases Immunogenicity of Proteins by Converting Them into Ligands of Several Endocytic Receptors Involved in Antigen Uptake by Dendritic Cells and Macrophages

    doi: 10.1371/journal.pone.0123293

    Figure Lengend Snippet: Roles of SR CD36 (A-E) and SR-A (G-I) as receptors for HOCl-modified proteins. ( A ) Uptake of fluorescently-labelled proteins by CHO cells transfected with human CD36 as compared to non-transfected cells. ( B ) Binding of anti-CD36 mAb and control mouse IgA to CD36-transfected and non-transfected CHO cells, determined by cellular ELISA. ( C ) Binding of rCD36 to plate-adsorbed proteins. ( D ) Effects of 10 or 100 μg/ml of indicated, soluble ligands on rCD36 binding to plate-adsorbed OVA-Cl. ( E ) Binding of polyclonal anti-mouse CD36 Ab and control goat IgG to BM-DC, splenic DC and PEM. A representative histogram of Ab binding to BM-DC is displayed on the left graph. ( F ) Binding of anti-mouse SR-A mAb and control rat IgG2b to BM-DC, splenic DC and PEM. A representative histogram of Ab binding to BM-DC is shown on the left graph. ( G ) Binding of SR-A present in lysates of PEM to plate-adsorbed proteins. ( H ) Effects of anti-SR-A 2F8 mAb and AcLDL on the uptake of fluorescently-labelled proteins by BM-DC. Shown are results of single experiments, each representative of at least 3 similar experiments performed (A-D, G, H) or averages +SEM from 4–6 independent experiments (E, F). The data were analysed with the unpaired (A-C, G) or one-sample (H) Student’s t-test or with ANOVA, followed by the Tukey-Kramer post-test (D). *, p

    Article Snippet: CHO-K1 cells stably transfected with human CD36 (CRL-2092) and non-transfected CHO-K1 cells (CCL-61) were obtained from ATCC and cultured in F12 medium (ATCC) supplemented with 10% FCS.

    Techniques: Modification, Transfection, Binding Assay, Enzyme-linked Immunosorbent Assay, End-sequence Profiling

    The down-regulation of SUMO-1 made mouse cortical neurons more sensitive to OGD/ROG and the SUMO-1-depleted neurons show reduced protection by preconditioning. (a) SUMO-1 (left panel) and SUMO-2/3 (right panel) protein levels in total cell lysates from mouse cortical neurons treated with various siRNAs. Upper panels: representative PAGE/WB pictures. Lower panels: quantitative analyses of densities. Data are shown as means ± SD ( n = 3). (b) Sensitivities to OGD/ROG among siRNA-treated cells. Cell death was measured with Hoechst 33342 and PI followed by FACS analysis. Data here are shown as means ± SD ( n = 3). (c) Mouse cortical neurons that had been transfected with AllStar siRNA or SUMO-1 siRNA were subjected to a harmful OGD/ROG with or without preconditioning (30 min OGD). Cell deaths were measured as mentioned above. Data here are shown as means ± SD ( n = 3).

    Journal: Journal of neurochemistry

    Article Title: SUMOylation participates in induction of ischemic tolerance

    doi: 10.1111/j.1471-4159.2009.05957.x

    Figure Lengend Snippet: The down-regulation of SUMO-1 made mouse cortical neurons more sensitive to OGD/ROG and the SUMO-1-depleted neurons show reduced protection by preconditioning. (a) SUMO-1 (left panel) and SUMO-2/3 (right panel) protein levels in total cell lysates from mouse cortical neurons treated with various siRNAs. Upper panels: representative PAGE/WB pictures. Lower panels: quantitative analyses of densities. Data are shown as means ± SD ( n = 3). (b) Sensitivities to OGD/ROG among siRNA-treated cells. Cell death was measured with Hoechst 33342 and PI followed by FACS analysis. Data here are shown as means ± SD ( n = 3). (c) Mouse cortical neurons that had been transfected with AllStar siRNA or SUMO-1 siRNA were subjected to a harmful OGD/ROG with or without preconditioning (30 min OGD). Cell deaths were measured as mentioned above. Data here are shown as means ± SD ( n = 3).

    Article Snippet: Cortical neurons were subjected to harmful OGD under all conditions at 5–7 days-in-culture (non-transfected cells and cells transfected by Amaxa or lipfectamine systems).

    Techniques: Polyacrylamide Gel Electrophoresis, Western Blot, FACS, Transfection

    The depletion of SUMO-1 made SHSY5Y cells more sensitive to OGD/ROG and the cells that were depleted of SUMO-1 were not protected by preconditioning. (a) SUMO-1 (left panel) and SUMO-2/3 (right panel) protein levels in total cell lysates from SHSY5Y cells transfected with various shRNA constructs as follows: 1, empty vector; 2, SUMO-1 sh#2; 3, SUMO-2 sh#1; 4, SUMO-2 sh#1 plus SUMO-3 sh#1; 5, SUMO-2 sh#1 plus SUMO-3 sh#2; 6, SUMO-2 sh#1 plus SUMO-3 sh#3. Upper panel: a representative PAGE/WB picture, lower panels: quantitative analyses; solid bars:conjugates; striped bar: free forms. Data are shown as means ± SD ( n = 6). ** p

    Journal: Journal of neurochemistry

    Article Title: SUMOylation participates in induction of ischemic tolerance

    doi: 10.1111/j.1471-4159.2009.05957.x

    Figure Lengend Snippet: The depletion of SUMO-1 made SHSY5Y cells more sensitive to OGD/ROG and the cells that were depleted of SUMO-1 were not protected by preconditioning. (a) SUMO-1 (left panel) and SUMO-2/3 (right panel) protein levels in total cell lysates from SHSY5Y cells transfected with various shRNA constructs as follows: 1, empty vector; 2, SUMO-1 sh#2; 3, SUMO-2 sh#1; 4, SUMO-2 sh#1 plus SUMO-3 sh#1; 5, SUMO-2 sh#1 plus SUMO-3 sh#2; 6, SUMO-2 sh#1 plus SUMO-3 sh#3. Upper panel: a representative PAGE/WB picture, lower panels: quantitative analyses; solid bars:conjugates; striped bar: free forms. Data are shown as means ± SD ( n = 6). ** p

    Article Snippet: Cortical neurons were subjected to harmful OGD under all conditions at 5–7 days-in-culture (non-transfected cells and cells transfected by Amaxa or lipfectamine systems).

    Techniques: Transfection, shRNA, Construct, Plasmid Preparation, Polyacrylamide Gel Electrophoresis, Western Blot

    Caveolin1-GFP Clusters Are Generated by EHD Proteins (A) TIR microscopy to show the distribution of caveolin1-GFP in gene-edited WT and ΔEHD1,2,4 NIH 3T3 cells. Scale bar, 10 μm. (B) Quantification of puncta size in TIR images as shown in (A), shown as frequency distribution of all sizes detected in 10 cells of each genotype shown. (C) Confocal and stimulated emission depletion (STED) microscopy of WT cells, ΔEHD1,2,4 cells, and ΔEHD1,2,4 cells expressing mCherry-EHD1, mCherry-EHD2, and mCherry-EHD4 by transient transfection. All cells are gene edited to express caveolin1-GFP. The STED images are of the boxed region in the confocal images. Scale bars, 5 μm (in confocal images) and 1 μm (in STED images). (D) Electron micrographs of ΔEHD1,2,4 cells expressing mitochondrially targeted APEX, mCherry-EHD1, mCherry-EHD2, and mCherry-EHD4 by transient transfection. Cells were stained with diaminobenzidine, producing electron-dense deposits in the mitochondria of transfected cells. Two cells are shown; arrows highlight mitochondria, and the boxed regions are shown at higher magnification in the additional panels. Scale bars, 500 nm.

    Journal: Current Biology

    Article Title: EHD Proteins Cooperate to Generate Caveolar Clusters and to Maintain Caveolae during Repeated Mechanical Stress

    doi: 10.1016/j.cub.2017.07.047

    Figure Lengend Snippet: Caveolin1-GFP Clusters Are Generated by EHD Proteins (A) TIR microscopy to show the distribution of caveolin1-GFP in gene-edited WT and ΔEHD1,2,4 NIH 3T3 cells. Scale bar, 10 μm. (B) Quantification of puncta size in TIR images as shown in (A), shown as frequency distribution of all sizes detected in 10 cells of each genotype shown. (C) Confocal and stimulated emission depletion (STED) microscopy of WT cells, ΔEHD1,2,4 cells, and ΔEHD1,2,4 cells expressing mCherry-EHD1, mCherry-EHD2, and mCherry-EHD4 by transient transfection. All cells are gene edited to express caveolin1-GFP. The STED images are of the boxed region in the confocal images. Scale bars, 5 μm (in confocal images) and 1 μm (in STED images). (D) Electron micrographs of ΔEHD1,2,4 cells expressing mitochondrially targeted APEX, mCherry-EHD1, mCherry-EHD2, and mCherry-EHD4 by transient transfection. Cells were stained with diaminobenzidine, producing electron-dense deposits in the mitochondria of transfected cells. Two cells are shown; arrows highlight mitochondria, and the boxed regions are shown at higher magnification in the additional panels. Scale bars, 500 nm.

    Article Snippet: For 3′3’-diaminobenzidine (DAB) staining of EHD1,2,4/mitochondrial APEX transfected cells, transiently transfected and non transfected cells grown on MatTek dishes were fixed in pre-chilled 2% glutaraldehyde in 0.1M cacodylate buffer plus 2 mM calcium chloride for 1 hr on ice.

    Techniques: Generated, Microscopy, Expressing, Transfection, Staining

    Co-immunoprecipitation of EHD2 with EHD1 and EHD4 (A) Lysates from cells expressing EHD2-GFP by gene editing of the EHD2 locus or negative controls expressing GFP alone were incubated with anti-GFP antibody beads. The lysate after this incubation is shown as “unbound” and washes from the isolated beads as “wash.” Sample eluted from the beads with sample buffer is shown as “IP eluate” and is concentrated 10× relative to the lysate. (B) Lysates from cells expressing EHD1-GFP by gene editing of the EHD1 locus, EHD4-GFP by gene editing of the EHD4 locus, or negative control cells stably transfected with plasmid to express GFP alone were incubated with anti-GFP antibody beads as in (A). The eluate was concentrated 50× relative to the lysate. Anti-EHD2 antibodies cross-react with EHD1 and EHD4; the cross-reacting bands are indicated with an asterisk and the EHD2 band is arrowed. (C) Lysates from ΔEHD1,2,4 triple-knockout NIH 3T3 cells transiently transfected with EHD-expressing or GFP-expressing plasmids as shown were incubated with anti-GFP antibody beads. The eluate was concentrated 10× relative to the lysate.

    Journal: Current Biology

    Article Title: EHD Proteins Cooperate to Generate Caveolar Clusters and to Maintain Caveolae during Repeated Mechanical Stress

    doi: 10.1016/j.cub.2017.07.047

    Figure Lengend Snippet: Co-immunoprecipitation of EHD2 with EHD1 and EHD4 (A) Lysates from cells expressing EHD2-GFP by gene editing of the EHD2 locus or negative controls expressing GFP alone were incubated with anti-GFP antibody beads. The lysate after this incubation is shown as “unbound” and washes from the isolated beads as “wash.” Sample eluted from the beads with sample buffer is shown as “IP eluate” and is concentrated 10× relative to the lysate. (B) Lysates from cells expressing EHD1-GFP by gene editing of the EHD1 locus, EHD4-GFP by gene editing of the EHD4 locus, or negative control cells stably transfected with plasmid to express GFP alone were incubated with anti-GFP antibody beads as in (A). The eluate was concentrated 50× relative to the lysate. Anti-EHD2 antibodies cross-react with EHD1 and EHD4; the cross-reacting bands are indicated with an asterisk and the EHD2 band is arrowed. (C) Lysates from ΔEHD1,2,4 triple-knockout NIH 3T3 cells transiently transfected with EHD-expressing or GFP-expressing plasmids as shown were incubated with anti-GFP antibody beads. The eluate was concentrated 10× relative to the lysate.

    Article Snippet: For 3′3’-diaminobenzidine (DAB) staining of EHD1,2,4/mitochondrial APEX transfected cells, transiently transfected and non transfected cells grown on MatTek dishes were fixed in pre-chilled 2% glutaraldehyde in 0.1M cacodylate buffer plus 2 mM calcium chloride for 1 hr on ice.

    Techniques: Immunoprecipitation, Expressing, Incubation, Isolation, Negative Control, Stable Transfection, Transfection, Plasmid Preparation, Triple Knockout

    EHD Proteins Are Required for Caveolar Stability under Repeated Mechanical Stress, and Cells Lacking EHD Proteins Are More Likely to Rupture under Repeated Mechanical Stress (A) Quantification of morphologically defined caveolae in ΔEHD1,2,4 triple-knockout NIH 3T3 cells by electron microscopy. Cells were grown on deformable silicon substrate and stretched by 20% at 1.5 Hz for 60 min as indicated. For each genotype, complete reconstructions of the perimeter of 10 cells were generated from 15–70 high-resolution micrographs per cell. Statistical analysis used one-way ANOVA with Dunnett’s multiple comparison. Also see Figure S7 . (B) Quantification of the sizes of clusters of caveolae from immunoelectron microscopy as in Figure 4 E, but with cells fixed during repetitive stretching. For each genotype shown, 50 micrographs of regions selected as containing positive staining were acquired at 6,500× magnification. Statistical analysis used one-way ANOVA with Dunnett’s multiple comparison test. (C) Assay for plasma membrane rupture in cells with genotypes as shown. Rupture is indicated by cytoplasmic accumulation of 150 kDa fluorescein isothiocyanate (FITC)-dextran (green). Cells were stretched for 60 min at 1.5 Hz. White signal is from NucRed Live 647 dye. WT cells were labeled with Cell Tracker red. (D) Quantification of the incidence of plasma membrane rupture as in (C) above, expressed as the proportion of the total number of cells that have green cytoplasmic staining. Each point represents 6–10 images from a single experiment, each image containing 50–150 individual cells. The data from each experiment are paired to allow comparison of cells with different genotypes grown in the same mixed population. Statistical analysis is by paired t test. (E) Assay for plasma membrane rupture in ΔEHD1,2,4 triple-knockout NIH 3T3 cells, some of which are transiently transfected with mCherry-EHD1, mCherry-EHD2, and mCherry-EHD4. White signal is from NucRed Live 647 dye. (F) Quantification of the incidence of plasma membrane rupture in transfected versus non-transfected ΔEHD1,2,4 triple-knockout cells as in (E). Statistical analysis is by paired t test.

    Journal: Current Biology

    Article Title: EHD Proteins Cooperate to Generate Caveolar Clusters and to Maintain Caveolae during Repeated Mechanical Stress

    doi: 10.1016/j.cub.2017.07.047

    Figure Lengend Snippet: EHD Proteins Are Required for Caveolar Stability under Repeated Mechanical Stress, and Cells Lacking EHD Proteins Are More Likely to Rupture under Repeated Mechanical Stress (A) Quantification of morphologically defined caveolae in ΔEHD1,2,4 triple-knockout NIH 3T3 cells by electron microscopy. Cells were grown on deformable silicon substrate and stretched by 20% at 1.5 Hz for 60 min as indicated. For each genotype, complete reconstructions of the perimeter of 10 cells were generated from 15–70 high-resolution micrographs per cell. Statistical analysis used one-way ANOVA with Dunnett’s multiple comparison. Also see Figure S7 . (B) Quantification of the sizes of clusters of caveolae from immunoelectron microscopy as in Figure 4 E, but with cells fixed during repetitive stretching. For each genotype shown, 50 micrographs of regions selected as containing positive staining were acquired at 6,500× magnification. Statistical analysis used one-way ANOVA with Dunnett’s multiple comparison test. (C) Assay for plasma membrane rupture in cells with genotypes as shown. Rupture is indicated by cytoplasmic accumulation of 150 kDa fluorescein isothiocyanate (FITC)-dextran (green). Cells were stretched for 60 min at 1.5 Hz. White signal is from NucRed Live 647 dye. WT cells were labeled with Cell Tracker red. (D) Quantification of the incidence of plasma membrane rupture as in (C) above, expressed as the proportion of the total number of cells that have green cytoplasmic staining. Each point represents 6–10 images from a single experiment, each image containing 50–150 individual cells. The data from each experiment are paired to allow comparison of cells with different genotypes grown in the same mixed population. Statistical analysis is by paired t test. (E) Assay for plasma membrane rupture in ΔEHD1,2,4 triple-knockout NIH 3T3 cells, some of which are transiently transfected with mCherry-EHD1, mCherry-EHD2, and mCherry-EHD4. White signal is from NucRed Live 647 dye. (F) Quantification of the incidence of plasma membrane rupture in transfected versus non-transfected ΔEHD1,2,4 triple-knockout cells as in (E). Statistical analysis is by paired t test.

    Article Snippet: For 3′3’-diaminobenzidine (DAB) staining of EHD1,2,4/mitochondrial APEX transfected cells, transiently transfected and non transfected cells grown on MatTek dishes were fixed in pre-chilled 2% glutaraldehyde in 0.1M cacodylate buffer plus 2 mM calcium chloride for 1 hr on ice.

    Techniques: Triple Knockout, Electron Microscopy, Generated, Immuno-Electron Microscopy, Staining, Labeling, Transfection