tris-buffered saline Search Results


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  • 99
    Thermo Fisher tris buffered saline
    Tris Buffered Saline, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 7131 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tbs buffer
    Purification of the <t>Ndi1</t> cross-linked by 2 . The UQ-free Ndi1 (0.34 mg of protein/mL) was cross-linked by a 20-fold excess of 2 , and subjected to acetone precipitation. The precipitate was solubilized in 4% SDS and subjected to the purification procedures described in “Experimental Procedures” by repeated rotation and centrifugation. The supernatant from each step was analyzed by SDS-PAGE and Western blotting: Input , the supernatant before the incubation with the avidin resin (1.2% of total volume, about 0.8 μg of protein/well); Flow , the supernatant after the incubation with the avidin resin (1.2% of total volume); Wash 1 , the supernatant after the wash with 0.5% Triton X-100 in <t>TBS</t> buffer; Wash 2 , the supernatant after the wash with TBS buffer; Elute , the supernatant after the treatment with Laemmli’s buffer (50% of total volume). Data shown are representative of three independent experiments.
    Tbs Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1970 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Bio-Rad tris buffered saline
    Purification of the <t>Ndi1</t> cross-linked by 2 . The UQ-free Ndi1 (0.34 mg of protein/mL) was cross-linked by a 20-fold excess of 2 , and subjected to acetone precipitation. The precipitate was solubilized in 4% SDS and subjected to the purification procedures described in “Experimental Procedures” by repeated rotation and centrifugation. The supernatant from each step was analyzed by SDS-PAGE and Western blotting: Input , the supernatant before the incubation with the avidin resin (1.2% of total volume, about 0.8 μg of protein/well); Flow , the supernatant after the incubation with the avidin resin (1.2% of total volume); Wash 1 , the supernatant after the wash with 0.5% Triton X-100 in <t>TBS</t> buffer; Wash 2 , the supernatant after the wash with TBS buffer; Elute , the supernatant after the treatment with Laemmli’s buffer (50% of total volume). Data shown are representative of three independent experiments.
    Tris Buffered Saline, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 4135 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tris buffered saline solution
    Effect of fermented ginseng (FG) extract on the level of soluble β-amyloid (Aβ) 42 protein in the mouse cerebral cortex. Transgenic (TG) mouse brain tissue was collected after behavioral test at 11 mo of age. The brain samples (100 mg) were homogenized in <t>Tris-buffered</t> saline solution (20 mM Tris, 137 mM <t>NaCl,</t> pH 7.4) containing complete protease inhibitors tablets. The extraction ratio (brain tissue:Tris-buffered saline) was 1:5 or 1:10 (w/v). The tissue homogenates were centrifuged at 100,000 g for 1 h at 4℃. Soluble Aβ42 level in the resulting supernatants were measured using the sandwich ELISA kit according to the manufacturer’s protocol. The data represent the mean±SEM ( n =7). * p
    Tris Buffered Saline Solution, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 327 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Cell Signaling Technology Inc tbs buffer
    Effect of fermented ginseng (FG) extract on the level of soluble β-amyloid (Aβ) 42 protein in the mouse cerebral cortex. Transgenic (TG) mouse brain tissue was collected after behavioral test at 11 mo of age. The brain samples (100 mg) were homogenized in <t>Tris-buffered</t> saline solution (20 mM Tris, 137 mM <t>NaCl,</t> pH 7.4) containing complete protease inhibitors tablets. The extraction ratio (brain tissue:Tris-buffered saline) was 1:5 or 1:10 (w/v). The tissue homogenates were centrifuged at 100,000 g for 1 h at 4℃. Soluble Aβ42 level in the resulting supernatants were measured using the sandwich ELISA kit according to the manufacturer’s protocol. The data represent the mean±SEM ( n =7). * p
    Tbs Buffer, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 295 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    TaKaRa tris buffered saline
    Effect of fermented ginseng (FG) extract on the level of soluble β-amyloid (Aβ) 42 protein in the mouse cerebral cortex. Transgenic (TG) mouse brain tissue was collected after behavioral test at 11 mo of age. The brain samples (100 mg) were homogenized in <t>Tris-buffered</t> saline solution (20 mM Tris, 137 mM <t>NaCl,</t> pH 7.4) containing complete protease inhibitors tablets. The extraction ratio (brain tissue:Tris-buffered saline) was 1:5 or 1:10 (w/v). The tissue homogenates were centrifuged at 100,000 g for 1 h at 4℃. Soluble Aβ42 level in the resulting supernatants were measured using the sandwich ELISA kit according to the manufacturer’s protocol. The data represent the mean±SEM ( n =7). * p
    Tris Buffered Saline, supplied by TaKaRa, used in various techniques. Bioz Stars score: 94/100, based on 315 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc tris buffered saline
    Chemical modification of cellular and recombinant <t>PTEN</t> by 1,4-NQ and suppression of 1,4-NQ modification of cellular PTEN. ( A ) Primary mouse hepatocytes were simultaneously treated with DMSO or 1,4-NQ and 10 (upper) or 100 (lower) µM Na 2 S 4 for 30 min, then PTEN was immunoprecipitated using anti-PTEN antibody. Western blotting was performed using the indicated antibodies. Representative blots are shown from three independent experiments. ( B ) Recombinant GST-tagged human PTEN (1 μg) was incubated with 1,4-NQ (1–8 μM) at 25 °C for 1 h. The reaction mixture was then subjected to immunoblotting, with the anti-1,4-NQ antibody, and SDS-PAGE, with Coomassie Brilliant Blue staining. Representative blots are shown from three independent experiments. ( C ) Results of nanoUPLC-MS E analysis of 1,4-NQ-modified cysteine residues in GST-tagged human PTEN. Recombinant GST-tagged human PTEN (1.7 μg) was incubated with 1,4-NQ (10 μM) at 25 °C for 30 min in a total volume of 10 μL 50 mM <t>Tris-HCl</t> (pH 7.5). After the reaction, PTEN protein was digested with trypsin and analyzed by nanoUPLC-MS E . The corresponding MS E data are shown in Table 1 .
    Tris Buffered Saline, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 10124 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Boster Bio tris buffered saline
    Chemical modification of cellular and recombinant <t>PTEN</t> by 1,4-NQ and suppression of 1,4-NQ modification of cellular PTEN. ( A ) Primary mouse hepatocytes were simultaneously treated with DMSO or 1,4-NQ and 10 (upper) or 100 (lower) µM Na 2 S 4 for 30 min, then PTEN was immunoprecipitated using anti-PTEN antibody. Western blotting was performed using the indicated antibodies. Representative blots are shown from three independent experiments. ( B ) Recombinant GST-tagged human PTEN (1 μg) was incubated with 1,4-NQ (1–8 μM) at 25 °C for 1 h. The reaction mixture was then subjected to immunoblotting, with the anti-1,4-NQ antibody, and SDS-PAGE, with Coomassie Brilliant Blue staining. Representative blots are shown from three independent experiments. ( C ) Results of nanoUPLC-MS E analysis of 1,4-NQ-modified cysteine residues in GST-tagged human PTEN. Recombinant GST-tagged human PTEN (1.7 μg) was incubated with 1,4-NQ (10 μM) at 25 °C for 30 min in a total volume of 10 μL 50 mM <t>Tris-HCl</t> (pH 7.5). After the reaction, PTEN protein was digested with trypsin and analyzed by nanoUPLC-MS E . The corresponding MS E data are shown in Table 1 .
    Tris Buffered Saline, supplied by Boster Bio, used in various techniques. Bioz Stars score: 97/100, based on 981 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Bio-Rad 10x tris buffered saline buffer
    Chemical modification of cellular and recombinant <t>PTEN</t> by 1,4-NQ and suppression of 1,4-NQ modification of cellular PTEN. ( A ) Primary mouse hepatocytes were simultaneously treated with DMSO or 1,4-NQ and 10 (upper) or 100 (lower) µM Na 2 S 4 for 30 min, then PTEN was immunoprecipitated using anti-PTEN antibody. Western blotting was performed using the indicated antibodies. Representative blots are shown from three independent experiments. ( B ) Recombinant GST-tagged human PTEN (1 μg) was incubated with 1,4-NQ (1–8 μM) at 25 °C for 1 h. The reaction mixture was then subjected to immunoblotting, with the anti-1,4-NQ antibody, and SDS-PAGE, with Coomassie Brilliant Blue staining. Representative blots are shown from three independent experiments. ( C ) Results of nanoUPLC-MS E analysis of 1,4-NQ-modified cysteine residues in GST-tagged human PTEN. Recombinant GST-tagged human PTEN (1.7 μg) was incubated with 1,4-NQ (10 μM) at 25 °C for 30 min in a total volume of 10 μL 50 mM <t>Tris-HCl</t> (pH 7.5). After the reaction, PTEN protein was digested with trypsin and analyzed by nanoUPLC-MS E . The corresponding MS E data are shown in Table 1 .
    10x Tris Buffered Saline Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc tris buffered saline tbs
    Chemical modification of cellular and recombinant <t>PTEN</t> by 1,4-NQ and suppression of 1,4-NQ modification of cellular PTEN. ( A ) Primary mouse hepatocytes were simultaneously treated with DMSO or 1,4-NQ and 10 (upper) or 100 (lower) µM Na 2 S 4 for 30 min, then PTEN was immunoprecipitated using anti-PTEN antibody. Western blotting was performed using the indicated antibodies. Representative blots are shown from three independent experiments. ( B ) Recombinant GST-tagged human PTEN (1 μg) was incubated with 1,4-NQ (1–8 μM) at 25 °C for 1 h. The reaction mixture was then subjected to immunoblotting, with the anti-1,4-NQ antibody, and SDS-PAGE, with Coomassie Brilliant Blue staining. Representative blots are shown from three independent experiments. ( C ) Results of nanoUPLC-MS E analysis of 1,4-NQ-modified cysteine residues in GST-tagged human PTEN. Recombinant GST-tagged human PTEN (1.7 μg) was incubated with 1,4-NQ (10 μM) at 25 °C for 30 min in a total volume of 10 μL 50 mM <t>Tris-HCl</t> (pH 7.5). After the reaction, PTEN protein was digested with trypsin and analyzed by nanoUPLC-MS E . The corresponding MS E data are shown in Table 1 .
    Tris Buffered Saline Tbs, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1811 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cell Signaling Technology Inc 1x tbs
    Chemical modification of cellular and recombinant <t>PTEN</t> by 1,4-NQ and suppression of 1,4-NQ modification of cellular PTEN. ( A ) Primary mouse hepatocytes were simultaneously treated with DMSO or 1,4-NQ and 10 (upper) or 100 (lower) µM Na 2 S 4 for 30 min, then PTEN was immunoprecipitated using anti-PTEN antibody. Western blotting was performed using the indicated antibodies. Representative blots are shown from three independent experiments. ( B ) Recombinant GST-tagged human PTEN (1 μg) was incubated with 1,4-NQ (1–8 μM) at 25 °C for 1 h. The reaction mixture was then subjected to immunoblotting, with the anti-1,4-NQ antibody, and SDS-PAGE, with Coomassie Brilliant Blue staining. Representative blots are shown from three independent experiments. ( C ) Results of nanoUPLC-MS E analysis of 1,4-NQ-modified cysteine residues in GST-tagged human PTEN. Recombinant GST-tagged human PTEN (1.7 μg) was incubated with 1,4-NQ (10 μM) at 25 °C for 30 min in a total volume of 10 μL 50 mM <t>Tris-HCl</t> (pH 7.5). After the reaction, PTEN protein was digested with trypsin and analyzed by nanoUPLC-MS E . The corresponding MS E data are shown in Table 1 .
    1x Tbs, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 123 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Purification of the Ndi1 cross-linked by 2 . The UQ-free Ndi1 (0.34 mg of protein/mL) was cross-linked by a 20-fold excess of 2 , and subjected to acetone precipitation. The precipitate was solubilized in 4% SDS and subjected to the purification procedures described in “Experimental Procedures” by repeated rotation and centrifugation. The supernatant from each step was analyzed by SDS-PAGE and Western blotting: Input , the supernatant before the incubation with the avidin resin (1.2% of total volume, about 0.8 μg of protein/well); Flow , the supernatant after the incubation with the avidin resin (1.2% of total volume); Wash 1 , the supernatant after the wash with 0.5% Triton X-100 in TBS buffer; Wash 2 , the supernatant after the wash with TBS buffer; Elute , the supernatant after the treatment with Laemmli’s buffer (50% of total volume). Data shown are representative of three independent experiments.

    Journal: Biochemistry

    Article Title: Characterization of the Ubiquinone Binding Site in Alternative NADH-Quinone Oxidoreductase of Saccharomyces cerevisiae by Photoaffinity Labeling †

    doi: 10.1021/bi100005j

    Figure Lengend Snippet: Purification of the Ndi1 cross-linked by 2 . The UQ-free Ndi1 (0.34 mg of protein/mL) was cross-linked by a 20-fold excess of 2 , and subjected to acetone precipitation. The precipitate was solubilized in 4% SDS and subjected to the purification procedures described in “Experimental Procedures” by repeated rotation and centrifugation. The supernatant from each step was analyzed by SDS-PAGE and Western blotting: Input , the supernatant before the incubation with the avidin resin (1.2% of total volume, about 0.8 μg of protein/well); Flow , the supernatant after the incubation with the avidin resin (1.2% of total volume); Wash 1 , the supernatant after the wash with 0.5% Triton X-100 in TBS buffer; Wash 2 , the supernatant after the wash with TBS buffer; Elute , the supernatant after the treatment with Laemmli’s buffer (50% of total volume). Data shown are representative of three independent experiments.

    Article Snippet: Then, the Ndi1 was diluted with 500 μL of 1% Triton X-100 in TBS buffer (0.9% NaCl, 10 mM Tris/HCl, pH 7.4, and 0.21% SDS), and incubated with a 50 μL slurry of Streptavidin-Agarose (Sigma) overnight in a cold room.

    Techniques: Purification, Centrifugation, SDS Page, Western Blot, Incubation, Avidin-Biotin Assay, Flow Cytometry

    ( A ) Fibrinolytic effects of rSKs on human plasma clots. Human plasma (45 μl) was mixed with trace amounts of 125 ). After a wash with Tris-buffered saline (pH 7.4) containing the thrombin inhibitor PPACK (10 μM), the clots were suspended in 2 ml of plasma containing 10 μM PPACK. Various amounts of rSK and rSKΔ59 that had undergone active-site titration (0–50 nM) were added to the plasma, and, after 6 h, the amount of fibrinolysis was determined by measuring the release of soluble 125 ). The means ± SD are shown (but in some cases the SD are too small to be visible). ( B ) Fibrinogen degradation by rSK activator complexes. At the end of the fibrinolysis experiments presented in A ). The means ± SD are shown (but in some cases the SD are too small to be visible).

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

    Article Title: A catalytic switch and the conversion of streptokinase to a fibrin-targeted plasminogen activator

    doi:

    Figure Lengend Snippet: ( A ) Fibrinolytic effects of rSKs on human plasma clots. Human plasma (45 μl) was mixed with trace amounts of 125 ). After a wash with Tris-buffered saline (pH 7.4) containing the thrombin inhibitor PPACK (10 μM), the clots were suspended in 2 ml of plasma containing 10 μM PPACK. Various amounts of rSK and rSKΔ59 that had undergone active-site titration (0–50 nM) were added to the plasma, and, after 6 h, the amount of fibrinolysis was determined by measuring the release of soluble 125 ). The means ± SD are shown (but in some cases the SD are too small to be visible). ( B ) Fibrinogen degradation by rSK activator complexes. At the end of the fibrinolysis experiments presented in A ). The means ± SD are shown (but in some cases the SD are too small to be visible).

    Article Snippet: After a wash with Tris-buffered saline (pH 7.4) containing the thrombin inhibitor PPACK (10 μM, d -Phe-Pro-Arg chloromethylketone, Calbiochem), the clots were suspended in 2 ml of plasma containing 10 μM PPACK.

    Techniques: Titration

    Reactivities of CL154C with plasma samples from patients with antiphospholipid syndrome (APS) (n = 21), normal healthy donors (n = 25), and systemic lupus erythematosus (SLE) patients without APS (n = 12). Enzyme-linked immunosorbent assay plates were coated with CL154C peptide (10 μ g/ml) and plasma samples were analyzed at 1:100 dilution in Tris buffered saline/0.1% gelatin. Bound IgG was measured and reported. Each data point represents a test sample; the horizontal bars denote the mean of each group, and the dashed line represents the cutoff for positivity, that is, the mean optical density (O.D.) plus 3 SD of normal controls.

    Journal: Arthritis and rheumatism

    Article Title: Identification and Characterization of a Peptide Mimetic That May Detect a Species of Disease-Associated Anticardiolipin Antibodies in Patients With the Antiphospholipid Syndrome

    doi: 10.1002/art.10836

    Figure Lengend Snippet: Reactivities of CL154C with plasma samples from patients with antiphospholipid syndrome (APS) (n = 21), normal healthy donors (n = 25), and systemic lupus erythematosus (SLE) patients without APS (n = 12). Enzyme-linked immunosorbent assay plates were coated with CL154C peptide (10 μ g/ml) and plasma samples were analyzed at 1:100 dilution in Tris buffered saline/0.1% gelatin. Bound IgG was measured and reported. Each data point represents a test sample; the horizontal bars denote the mean of each group, and the dashed line represents the cutoff for positivity, that is, the mean optical density (O.D.) plus 3 SD of normal controls.

    Article Snippet: After washing with Tris buffered saline (TBS), bound phage in the wells were eluted with 35 μ l elution buffer (0.1 M HCl adjusted to pH 2.2 with glycine, and containing 1 mg/ml bovine serum albumin [BSA]; fraction V; Sigma, St. Louis, MO) per well, followed by incubation for 10 minutes at room temperature (RT).

    Techniques: Enzyme-linked Immunosorbent Assay

    Effect of fermented ginseng (FG) extract on the level of soluble β-amyloid (Aβ) 42 protein in the mouse cerebral cortex. Transgenic (TG) mouse brain tissue was collected after behavioral test at 11 mo of age. The brain samples (100 mg) were homogenized in Tris-buffered saline solution (20 mM Tris, 137 mM NaCl, pH 7.4) containing complete protease inhibitors tablets. The extraction ratio (brain tissue:Tris-buffered saline) was 1:5 or 1:10 (w/v). The tissue homogenates were centrifuged at 100,000 g for 1 h at 4℃. Soluble Aβ42 level in the resulting supernatants were measured using the sandwich ELISA kit according to the manufacturer’s protocol. The data represent the mean±SEM ( n =7). * p

    Journal: Journal of Ginseng Research

    Article Title: Effects of fermented ginseng on memory impairment and ?-amyloid reduction in Alzheimer's disease experimental models

    doi: 10.5142/jgr.2013.37.100

    Figure Lengend Snippet: Effect of fermented ginseng (FG) extract on the level of soluble β-amyloid (Aβ) 42 protein in the mouse cerebral cortex. Transgenic (TG) mouse brain tissue was collected after behavioral test at 11 mo of age. The brain samples (100 mg) were homogenized in Tris-buffered saline solution (20 mM Tris, 137 mM NaCl, pH 7.4) containing complete protease inhibitors tablets. The extraction ratio (brain tissue:Tris-buffered saline) was 1:5 or 1:10 (w/v). The tissue homogenates were centrifuged at 100,000 g for 1 h at 4℃. Soluble Aβ42 level in the resulting supernatants were measured using the sandwich ELISA kit according to the manufacturer’s protocol. The data represent the mean±SEM ( n =7). * p

    Article Snippet: The brain samples (100 mg) were homogenized in Tris-buffered saline solution (20 mM Tris, 137 mM NaCl, pH 7.4) containing a complete protease inhibitors tablet (catalog no. P8340; Sigma, St. Louis, MO, USA).

    Techniques: Transgenic Assay, Sandwich ELISA

    The percentage of ciprofloxacin released from (a) the fibrin hydrogel at 0, 1, 12, 24, 72 and 168 h and (b) the stability of ciprofloxacin in tris-buffered saline solution at 37 °C protected from light.

    Journal: Journal of Dental Sciences

    Article Title: In vitro evaluation of local antibiotic delivery via fibrin hydrogel

    doi: 10.1016/j.jds.2018.08.010

    Figure Lengend Snippet: The percentage of ciprofloxacin released from (a) the fibrin hydrogel at 0, 1, 12, 24, 72 and 168 h and (b) the stability of ciprofloxacin in tris-buffered saline solution at 37 °C protected from light.

    Article Snippet: Standard solution preparation 1000 μg/ml ciprofloxacin hydrochloride USP standard stock solution was prepared by dissolving 10 mg ciprofloxacin hydrochloride (Sigma–Aldrich, St. Louis, Missouri, USA) in 10 ml of tris-buffered saline solution (TBS) which consisted of TrisHCl 100 mM (Sigma–Aldrich) and NaCl 150 mM (Sigma–Aldrich) adjusted pH to 7.6 by using NaOH and HCl.

    Techniques:

    The antibacterial properties of ciprofloxacin delivered by a fibrin hydrogel compared to ciprofloxacin solution. The inhibition zone of 150 and 1500 μg/ml ciprofloxacin delivered by fibrin hydrogel were tested against Streptococcus mutans , Enterococcus faecalis , and Streptococcus sobrinus . Likewise, the standard ciprofloxacin solutions prepared in TBS at the same concentration were verified in parallel. Only TBS, fibrin hydrogel, and calcium hydroxide were loaded into the agar as the control. TBS: tris-buffered saline solution, * p-value

    Journal: Journal of Dental Sciences

    Article Title: In vitro evaluation of local antibiotic delivery via fibrin hydrogel

    doi: 10.1016/j.jds.2018.08.010

    Figure Lengend Snippet: The antibacterial properties of ciprofloxacin delivered by a fibrin hydrogel compared to ciprofloxacin solution. The inhibition zone of 150 and 1500 μg/ml ciprofloxacin delivered by fibrin hydrogel were tested against Streptococcus mutans , Enterococcus faecalis , and Streptococcus sobrinus . Likewise, the standard ciprofloxacin solutions prepared in TBS at the same concentration were verified in parallel. Only TBS, fibrin hydrogel, and calcium hydroxide were loaded into the agar as the control. TBS: tris-buffered saline solution, * p-value

    Article Snippet: Standard solution preparation 1000 μg/ml ciprofloxacin hydrochloride USP standard stock solution was prepared by dissolving 10 mg ciprofloxacin hydrochloride (Sigma–Aldrich, St. Louis, Missouri, USA) in 10 ml of tris-buffered saline solution (TBS) which consisted of TrisHCl 100 mM (Sigma–Aldrich) and NaCl 150 mM (Sigma–Aldrich) adjusted pH to 7.6 by using NaOH and HCl.

    Techniques: Inhibition, Concentration Assay

    Chemical modification of cellular and recombinant PTEN by 1,4-NQ and suppression of 1,4-NQ modification of cellular PTEN. ( A ) Primary mouse hepatocytes were simultaneously treated with DMSO or 1,4-NQ and 10 (upper) or 100 (lower) µM Na 2 S 4 for 30 min, then PTEN was immunoprecipitated using anti-PTEN antibody. Western blotting was performed using the indicated antibodies. Representative blots are shown from three independent experiments. ( B ) Recombinant GST-tagged human PTEN (1 μg) was incubated with 1,4-NQ (1–8 μM) at 25 °C for 1 h. The reaction mixture was then subjected to immunoblotting, with the anti-1,4-NQ antibody, and SDS-PAGE, with Coomassie Brilliant Blue staining. Representative blots are shown from three independent experiments. ( C ) Results of nanoUPLC-MS E analysis of 1,4-NQ-modified cysteine residues in GST-tagged human PTEN. Recombinant GST-tagged human PTEN (1.7 μg) was incubated with 1,4-NQ (10 μM) at 25 °C for 30 min in a total volume of 10 μL 50 mM Tris-HCl (pH 7.5). After the reaction, PTEN protein was digested with trypsin and analyzed by nanoUPLC-MS E . The corresponding MS E data are shown in Table 1 .

    Journal: Scientific Reports

    Article Title: Polysulfide Na2S4 regulates the activation of PTEN/Akt/CREB signaling and cytotoxicity mediated by 1,4-naphthoquinone through formation of sulfur adducts

    doi: 10.1038/s41598-017-04590-z

    Figure Lengend Snippet: Chemical modification of cellular and recombinant PTEN by 1,4-NQ and suppression of 1,4-NQ modification of cellular PTEN. ( A ) Primary mouse hepatocytes were simultaneously treated with DMSO or 1,4-NQ and 10 (upper) or 100 (lower) µM Na 2 S 4 for 30 min, then PTEN was immunoprecipitated using anti-PTEN antibody. Western blotting was performed using the indicated antibodies. Representative blots are shown from three independent experiments. ( B ) Recombinant GST-tagged human PTEN (1 μg) was incubated with 1,4-NQ (1–8 μM) at 25 °C for 1 h. The reaction mixture was then subjected to immunoblotting, with the anti-1,4-NQ antibody, and SDS-PAGE, with Coomassie Brilliant Blue staining. Representative blots are shown from three independent experiments. ( C ) Results of nanoUPLC-MS E analysis of 1,4-NQ-modified cysteine residues in GST-tagged human PTEN. Recombinant GST-tagged human PTEN (1.7 μg) was incubated with 1,4-NQ (10 μM) at 25 °C for 30 min in a total volume of 10 μL 50 mM Tris-HCl (pH 7.5). After the reaction, PTEN protein was digested with trypsin and analyzed by nanoUPLC-MS E . The corresponding MS E data are shown in Table 1 .

    Article Snippet: Anti-rabbit IgG conjugated magnetic beads (100 µL, Dynabeads M-280-sheep anti-rabbit IgG) were washed three times with Tris-buffered saline and Tween 20, then incubated with anti-PTEN antibodies (5 µL, Cell Signaling Technology, #9552) at 4 °C for 3 h. The unbound antibodies were removed and the beads resuspended in 500 µL cell lysate (1 µg/µL).

    Techniques: Modification, Recombinant, Immunoprecipitation, Western Blot, Incubation, SDS Page, Staining, Mass Spectrometry