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  • 99
    Lonza trypsin ethylenediaminetetraacetic acid
    Trypsin Ethylenediaminetetraacetic Acid, supplied by Lonza, used in various techniques. Bioz Stars score: 99/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher trypsin edta
    Trypsin Edta, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 51487 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore edta
    Edta, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 32373 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher edta
    Edta, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 16222 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore trypsin edta
    Trypsin Edta, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 10138 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher trypsin edta solution
    Trypsin Edta Solution, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 6282 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore ethylenediaminetetraacetic acid edta
    Ethylenediaminetetraacetic Acid Edta, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4190 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam antigen retrieval
    Antigen Retrieval, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 5337 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Becton Dickinson edta
    Edta, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 93/100, based on 3601 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad edta
    Edta, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1360 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Becton Dickinson edta tubes
    Study 3: Comparison of PBMC isolation methods and SMN measures from various blood fractions. Due to the variability in SMN signal and protein concentrations seen with <t>CPT</t> tube PBMC isolation, other methods were explored using the four subjects from Study 2. A : PBMC yield was greatest in samples collected with <t>EDTA</t> tubes and subsequent Lymphoprep gradient separation, and showed no statistically significant changes with isolation delays of up to 24 h. B : Total soluble protein tended to increase with 24 h delays in samples collected by EDTA tube and isolated by CPT tubes, while there was no obvious change in protein concentrations in EDTA/Lymphoprep processing. C : SMN as measured by total protein tended to decrease with isolation delays with EDTA/CPT processing. SMN signals were similar with delays up to 24 h with EDTA/Lymphoprep processing. D : SMN by PBMC counts was variable for both EDTA/CPT and EDTA/Lymphoprep processing methods. However, the EDTA/Lymphoprep values were generally overlapping and did not appear to decrease from the no-delay timepoint (t = 0). In Figure 3 body of the boxplots indicate the first and third quartiles, while the horizontal bar indicates the median.
    Edta Tubes, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 94/100, based on 1752 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher versene solution
    Study 3: Comparison of PBMC isolation methods and SMN measures from various blood fractions. Due to the variability in SMN signal and protein concentrations seen with <t>CPT</t> tube PBMC isolation, other methods were explored using the four subjects from Study 2. A : PBMC yield was greatest in samples collected with <t>EDTA</t> tubes and subsequent Lymphoprep gradient separation, and showed no statistically significant changes with isolation delays of up to 24 h. B : Total soluble protein tended to increase with 24 h delays in samples collected by EDTA tube and isolated by CPT tubes, while there was no obvious change in protein concentrations in EDTA/Lymphoprep processing. C : SMN as measured by total protein tended to decrease with isolation delays with EDTA/CPT processing. SMN signals were similar with delays up to 24 h with EDTA/Lymphoprep processing. D : SMN by PBMC counts was variable for both EDTA/CPT and EDTA/Lymphoprep processing methods. However, the EDTA/Lymphoprep values were generally overlapping and did not appear to decrease from the no-delay timepoint (t = 0). In Figure 3 body of the boxplots indicate the first and third quartiles, while the horizontal bar indicates the median.
    Versene Solution, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 587 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher tbe buffer
    Study 3: Comparison of PBMC isolation methods and SMN measures from various blood fractions. Due to the variability in SMN signal and protein concentrations seen with <t>CPT</t> tube PBMC isolation, other methods were explored using the four subjects from Study 2. A : PBMC yield was greatest in samples collected with <t>EDTA</t> tubes and subsequent Lymphoprep gradient separation, and showed no statistically significant changes with isolation delays of up to 24 h. B : Total soluble protein tended to increase with 24 h delays in samples collected by EDTA tube and isolated by CPT tubes, while there was no obvious change in protein concentrations in EDTA/Lymphoprep processing. C : SMN as measured by total protein tended to decrease with isolation delays with EDTA/CPT processing. SMN signals were similar with delays up to 24 h with EDTA/Lymphoprep processing. D : SMN by PBMC counts was variable for both EDTA/CPT and EDTA/Lymphoprep processing methods. However, the EDTA/Lymphoprep values were generally overlapping and did not appear to decrease from the no-delay timepoint (t = 0). In Figure 3 body of the boxplots indicate the first and third quartiles, while the horizontal bar indicates the median.
    Tbe Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2279 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher tae buffer
    Study 3: Comparison of PBMC isolation methods and SMN measures from various blood fractions. Due to the variability in SMN signal and protein concentrations seen with <t>CPT</t> tube PBMC isolation, other methods were explored using the four subjects from Study 2. A : PBMC yield was greatest in samples collected with <t>EDTA</t> tubes and subsequent Lymphoprep gradient separation, and showed no statistically significant changes with isolation delays of up to 24 h. B : Total soluble protein tended to increase with 24 h delays in samples collected by EDTA tube and isolated by CPT tubes, while there was no obvious change in protein concentrations in EDTA/Lymphoprep processing. C : SMN as measured by total protein tended to decrease with isolation delays with EDTA/CPT processing. SMN signals were similar with delays up to 24 h with EDTA/Lymphoprep processing. D : SMN by PBMC counts was variable for both EDTA/CPT and EDTA/Lymphoprep processing methods. However, the EDTA/Lymphoprep values were generally overlapping and did not appear to decrease from the no-delay timepoint (t = 0). In Figure 3 body of the boxplots indicate the first and third quartiles, while the horizontal bar indicates the median.
    Tae Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2058 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher ethylenediaminetetraacetic acid edta
    Study 3: Comparison of PBMC isolation methods and SMN measures from various blood fractions. Due to the variability in SMN signal and protein concentrations seen with <t>CPT</t> tube PBMC isolation, other methods were explored using the four subjects from Study 2. A : PBMC yield was greatest in samples collected with <t>EDTA</t> tubes and subsequent Lymphoprep gradient separation, and showed no statistically significant changes with isolation delays of up to 24 h. B : Total soluble protein tended to increase with 24 h delays in samples collected by EDTA tube and isolated by CPT tubes, while there was no obvious change in protein concentrations in EDTA/Lymphoprep processing. C : SMN as measured by total protein tended to decrease with isolation delays with EDTA/CPT processing. SMN signals were similar with delays up to 24 h with EDTA/Lymphoprep processing. D : SMN by PBMC counts was variable for both EDTA/CPT and EDTA/Lymphoprep processing methods. However, the EDTA/Lymphoprep values were generally overlapping and did not appear to decrease from the no-delay timepoint (t = 0). In Figure 3 body of the boxplots indicate the first and third quartiles, while the horizontal bar indicates the median.
    Ethylenediaminetetraacetic Acid Edta, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1225 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tris edta buffer
    Study 3: Comparison of PBMC isolation methods and SMN measures from various blood fractions. Due to the variability in SMN signal and protein concentrations seen with <t>CPT</t> tube PBMC isolation, other methods were explored using the four subjects from Study 2. A : PBMC yield was greatest in samples collected with <t>EDTA</t> tubes and subsequent Lymphoprep gradient separation, and showed no statistically significant changes with isolation delays of up to 24 h. B : Total soluble protein tended to increase with 24 h delays in samples collected by EDTA tube and isolated by CPT tubes, while there was no obvious change in protein concentrations in EDTA/Lymphoprep processing. C : SMN as measured by total protein tended to decrease with isolation delays with EDTA/CPT processing. SMN signals were similar with delays up to 24 h with EDTA/Lymphoprep processing. D : SMN by PBMC counts was variable for both EDTA/CPT and EDTA/Lymphoprep processing methods. However, the EDTA/Lymphoprep values were generally overlapping and did not appear to decrease from the no-delay timepoint (t = 0). In Figure 3 body of the boxplots indicate the first and third quartiles, while the horizontal bar indicates the median.
    Tris Edta Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1089 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore edta free protease inhibitor cocktail
    Study 3: Comparison of PBMC isolation methods and SMN measures from various blood fractions. Due to the variability in SMN signal and protein concentrations seen with <t>CPT</t> tube PBMC isolation, other methods were explored using the four subjects from Study 2. A : PBMC yield was greatest in samples collected with <t>EDTA</t> tubes and subsequent Lymphoprep gradient separation, and showed no statistically significant changes with isolation delays of up to 24 h. B : Total soluble protein tended to increase with 24 h delays in samples collected by EDTA tube and isolated by CPT tubes, while there was no obvious change in protein concentrations in EDTA/Lymphoprep processing. C : SMN as measured by total protein tended to decrease with isolation delays with EDTA/CPT processing. SMN signals were similar with delays up to 24 h with EDTA/Lymphoprep processing. D : SMN by PBMC counts was variable for both EDTA/CPT and EDTA/Lymphoprep processing methods. However, the EDTA/Lymphoprep values were generally overlapping and did not appear to decrease from the no-delay timepoint (t = 0). In Figure 3 body of the boxplots indicate the first and third quartiles, while the horizontal bar indicates the median.
    Edta Free Protease Inhibitor Cocktail, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1594 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Becton Dickinson trypsin edta
    Knockdown of P-gp in 4T1-R (top panel), SKBR-3 (middle panel) and MCF-7 (bottom panel) breast cancer cells with/without aptamer-labeled F31 nanoparticles compared to lipofectamine transfection. In both cases of lipofectamine and aptamer-labeled nanoparticle transfection, the cells were transfected with 100 pmol siRNA for 24h, and then the cells were scraped by using <t>trypsin-EDTA,</t> washed with <t>PBS,</t> pelleted and the expression of P-gp was measured by Western blot analysis.
    Trypsin Edta, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 94/100, based on 2166 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fisher Scientific edta
    GO as a hydroxyl-radical scavenger. A: Addition of 100 ppm GO protects phenol red from oxidation by Fenton-generated · OH over 8 hrs. B: Addition of GO protects the spin-trap DMPO from oxidation by Fenton-generated · OH detected by EPR spectroscopy. The protective effect is concentration dependent over the range 0.1-90 ppm GO. C: Both phenol red monitoring and EPR were used to test if the GO-mediated protective effect is due to radical scavenging or Fenton suppression by Fe-binding. The protective effect of GO is still present when GO-Fe binding is suppressed by <t>EDTA,</t> confirming the importance of radical scavenging. D: GO also protects DMPO when · OH is generated sonochemically, in a non-Fenton assay, providing additional evidence for true radical scavenging. All experiments were done in <t>PBS</t> (pH 3.5).
    Edta, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 93/100, based on 567 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson edta vacutainer tubes
    Analysis of circulating lymphocytes following influenza virus infection. For each virus, three to five ferrets were inoculated i.n. with 1 × 10 6 PFU. Blood was collected on days 3 (A), 7 (B), and 19 (C) p.i. into <t>EDTA</t> <t>Vacutainer</t> tubes and was
    Edta Vacutainer Tubes, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 94/100, based on 790 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Becton Dickinson k2 edta
    Analysis of circulating lymphocytes following influenza virus infection. For each virus, three to five ferrets were inoculated i.n. with 1 × 10 6 PFU. Blood was collected on days 3 (A), 7 (B), and 19 (C) p.i. into <t>EDTA</t> <t>Vacutainer</t> tubes and was
    K2 Edta, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 94/100, based on 601 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Corning Life Sciences trypsin edta
    Analysis of circulating lymphocytes following influenza virus infection. For each virus, three to five ferrets were inoculated i.n. with 1 × 10 6 PFU. Blood was collected on days 3 (A), 7 (B), and 19 (C) p.i. into <t>EDTA</t> <t>Vacutainer</t> tubes and was
    Trypsin Edta, supplied by Corning Life Sciences, used in various techniques. Bioz Stars score: 92/100, based on 861 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Study 3: Comparison of PBMC isolation methods and SMN measures from various blood fractions. Due to the variability in SMN signal and protein concentrations seen with CPT tube PBMC isolation, other methods were explored using the four subjects from Study 2. A : PBMC yield was greatest in samples collected with EDTA tubes and subsequent Lymphoprep gradient separation, and showed no statistically significant changes with isolation delays of up to 24 h. B : Total soluble protein tended to increase with 24 h delays in samples collected by EDTA tube and isolated by CPT tubes, while there was no obvious change in protein concentrations in EDTA/Lymphoprep processing. C : SMN as measured by total protein tended to decrease with isolation delays with EDTA/CPT processing. SMN signals were similar with delays up to 24 h with EDTA/Lymphoprep processing. D : SMN by PBMC counts was variable for both EDTA/CPT and EDTA/Lymphoprep processing methods. However, the EDTA/Lymphoprep values were generally overlapping and did not appear to decrease from the no-delay timepoint (t = 0). In Figure 3 body of the boxplots indicate the first and third quartiles, while the horizontal bar indicates the median.

    Journal: PLoS ONE

    Article Title: Evaluation of Peripheral Blood Mononuclear Cell Processing and Analysis for Survival Motor Neuron Protein

    doi: 10.1371/journal.pone.0050763

    Figure Lengend Snippet: Study 3: Comparison of PBMC isolation methods and SMN measures from various blood fractions. Due to the variability in SMN signal and protein concentrations seen with CPT tube PBMC isolation, other methods were explored using the four subjects from Study 2. A : PBMC yield was greatest in samples collected with EDTA tubes and subsequent Lymphoprep gradient separation, and showed no statistically significant changes with isolation delays of up to 24 h. B : Total soluble protein tended to increase with 24 h delays in samples collected by EDTA tube and isolated by CPT tubes, while there was no obvious change in protein concentrations in EDTA/Lymphoprep processing. C : SMN as measured by total protein tended to decrease with isolation delays with EDTA/CPT processing. SMN signals were similar with delays up to 24 h with EDTA/Lymphoprep processing. D : SMN by PBMC counts was variable for both EDTA/CPT and EDTA/Lymphoprep processing methods. However, the EDTA/Lymphoprep values were generally overlapping and did not appear to decrease from the no-delay timepoint (t = 0). In Figure 3 body of the boxplots indicate the first and third quartiles, while the horizontal bar indicates the median.

    Article Snippet: Whole blood samples at the Jasper Clinic were collected in BD CPT tubes (#362761, Studies 1–3), EDTA tubes (#22-040-67, Fisher, Pittsburgh, PA in Studies 3–5, and SMAF-001) or ACD tubes (#363083, BD, Franklin Lakes, NJ in Study 5).

    Techniques: Isolation, Cycling Probe Technology

    Knockdown of P-gp in 4T1-R (top panel), SKBR-3 (middle panel) and MCF-7 (bottom panel) breast cancer cells with/without aptamer-labeled F31 nanoparticles compared to lipofectamine transfection. In both cases of lipofectamine and aptamer-labeled nanoparticle transfection, the cells were transfected with 100 pmol siRNA for 24h, and then the cells were scraped by using trypsin-EDTA, washed with PBS, pelleted and the expression of P-gp was measured by Western blot analysis.

    Journal: European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V

    Article Title: Aptamer-functionalized hybrid nanoparticle for the treatment of breast cancer

    doi: 10.1016/j.ejpb.2017.01.011

    Figure Lengend Snippet: Knockdown of P-gp in 4T1-R (top panel), SKBR-3 (middle panel) and MCF-7 (bottom panel) breast cancer cells with/without aptamer-labeled F31 nanoparticles compared to lipofectamine transfection. In both cases of lipofectamine and aptamer-labeled nanoparticle transfection, the cells were transfected with 100 pmol siRNA for 24h, and then the cells were scraped by using trypsin-EDTA, washed with PBS, pelleted and the expression of P-gp was measured by Western blot analysis.

    Article Snippet: After treatment, the cells were scraped by using trypsin-EDTA, washed and resuspended in PBS and kept on ice until they were used to quantify the uptake of the nanoparticles by those cells by FACS (BD FACSCalibur).

    Techniques: Labeling, Transfection, Expressing, Western Blot

    Measurement of the expression of Her-2 (A.) and P-gp (B.) in different mouse ( i.e. 4T1-R and 4T1-S) and human breast cancer cells ( i.e. SKBR-3, MCF-7 and MDA MB-231) and human liver cancer cells ( i.e. Huh-7.5 and HepG2) by Western blot analysis. The cells were cultured for 24h and then they were scraped by using trypsin-EDTA, washed with PBS, pelleted and then equal amount of proteins was loaded to measure the expression of Her-2 (1:1000 dilution) and P-gp (1:1000 dilution) with β-actin (1:20,000 dilution) running as the loading control.

    Journal: European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V

    Article Title: Aptamer-functionalized hybrid nanoparticle for the treatment of breast cancer

    doi: 10.1016/j.ejpb.2017.01.011

    Figure Lengend Snippet: Measurement of the expression of Her-2 (A.) and P-gp (B.) in different mouse ( i.e. 4T1-R and 4T1-S) and human breast cancer cells ( i.e. SKBR-3, MCF-7 and MDA MB-231) and human liver cancer cells ( i.e. Huh-7.5 and HepG2) by Western blot analysis. The cells were cultured for 24h and then they were scraped by using trypsin-EDTA, washed with PBS, pelleted and then equal amount of proteins was loaded to measure the expression of Her-2 (1:1000 dilution) and P-gp (1:1000 dilution) with β-actin (1:20,000 dilution) running as the loading control.

    Article Snippet: After treatment, the cells were scraped by using trypsin-EDTA, washed and resuspended in PBS and kept on ice until they were used to quantify the uptake of the nanoparticles by those cells by FACS (BD FACSCalibur).

    Techniques: Expressing, Multiple Displacement Amplification, Western Blot, Cell Culture

    GO as a hydroxyl-radical scavenger. A: Addition of 100 ppm GO protects phenol red from oxidation by Fenton-generated · OH over 8 hrs. B: Addition of GO protects the spin-trap DMPO from oxidation by Fenton-generated · OH detected by EPR spectroscopy. The protective effect is concentration dependent over the range 0.1-90 ppm GO. C: Both phenol red monitoring and EPR were used to test if the GO-mediated protective effect is due to radical scavenging or Fenton suppression by Fe-binding. The protective effect of GO is still present when GO-Fe binding is suppressed by EDTA, confirming the importance of radical scavenging. D: GO also protects DMPO when · OH is generated sonochemically, in a non-Fenton assay, providing additional evidence for true radical scavenging. All experiments were done in PBS (pH 3.5).

    Journal: Nanoscale

    Article Title: Antioxidant Chemistry of Graphene-Based Materials and its Role in Oxidation Protection Technology

    doi: 10.1039/c4nr03275f

    Figure Lengend Snippet: GO as a hydroxyl-radical scavenger. A: Addition of 100 ppm GO protects phenol red from oxidation by Fenton-generated · OH over 8 hrs. B: Addition of GO protects the spin-trap DMPO from oxidation by Fenton-generated · OH detected by EPR spectroscopy. The protective effect is concentration dependent over the range 0.1-90 ppm GO. C: Both phenol red monitoring and EPR were used to test if the GO-mediated protective effect is due to radical scavenging or Fenton suppression by Fe-binding. The protective effect of GO is still present when GO-Fe binding is suppressed by EDTA, confirming the importance of radical scavenging. D: GO also protects DMPO when · OH is generated sonochemically, in a non-Fenton assay, providing additional evidence for true radical scavenging. All experiments were done in PBS (pH 3.5).

    Article Snippet: Hydrogen peroxide (H2 O2 ), phosphate buffered saline (PBS) (pH 7.4), and EDTA were purchased from Fisher Scientific Inc. (Pittsburgh, PA).

    Techniques: Generated, Electron Paramagnetic Resonance, Spectroscopy, Concentration Assay, Binding Assay

    Analysis of circulating lymphocytes following influenza virus infection. For each virus, three to five ferrets were inoculated i.n. with 1 × 10 6 PFU. Blood was collected on days 3 (A), 7 (B), and 19 (C) p.i. into EDTA Vacutainer tubes and was

    Journal: Journal of Virology

    Article Title: PB1-F2 Expression by the 2009 Pandemic H1N1 Influenza Virus Has Minimal Impact on Virulence in Animal Models ▿

    doi: 10.1128/JVI.02717-09

    Figure Lengend Snippet: Analysis of circulating lymphocytes following influenza virus infection. For each virus, three to five ferrets were inoculated i.n. with 1 × 10 6 PFU. Blood was collected on days 3 (A), 7 (B), and 19 (C) p.i. into EDTA Vacutainer tubes and was

    Article Snippet: On days zero, 3, 7, and 19 p.i., blood was collected in EDTA Vacutainer tubes (Becton Dickinson, Franklin Lakes, NJ) from 3 to 5 inoculated ferrets from each virus group.

    Techniques: Infection