Structured Review

Millipore dpbs
Initial tobramycin treatment is required for the combination to be effective. 24-hr old <t>biofilms</t> grown on MBEC plates were treated sequentially. First, biofilms were treated for 3-hours with tobramycin (500 µM) and then washed three times in <t>DPBS</t> for 3-mins each, before being treated with triclosan (100 µM) for 3-hours or vice versa. As a control, biofilms were also treated for 6-hrs with triclosan and tobramycin. The number of viable cells within the biofilms were quantified by BacTiter-Glo™. The assay was performed twice in in duplicate. The results represent means plus the SEM. A one-way ANOVA followed by Bonferroni’s multiple comparison post-hoc test was used to determine statistical significance between each treatment and the untreated control. *, p
Dpbs, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 213 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Triclosan depletes the membrane potential in Pseudomonas aeruginosa biofilms inhibiting aminoglycoside induced adaptive resistance"

Article Title: Triclosan depletes the membrane potential in Pseudomonas aeruginosa biofilms inhibiting aminoglycoside induced adaptive resistance

Journal: bioRxiv

doi: 10.1101/2020.04.09.034033

Initial tobramycin treatment is required for the combination to be effective. 24-hr old biofilms grown on MBEC plates were treated sequentially. First, biofilms were treated for 3-hours with tobramycin (500 µM) and then washed three times in DPBS for 3-mins each, before being treated with triclosan (100 µM) for 3-hours or vice versa. As a control, biofilms were also treated for 6-hrs with triclosan and tobramycin. The number of viable cells within the biofilms were quantified by BacTiter-Glo™. The assay was performed twice in in duplicate. The results represent means plus the SEM. A one-way ANOVA followed by Bonferroni’s multiple comparison post-hoc test was used to determine statistical significance between each treatment and the untreated control. *, p
Figure Legend Snippet: Initial tobramycin treatment is required for the combination to be effective. 24-hr old biofilms grown on MBEC plates were treated sequentially. First, biofilms were treated for 3-hours with tobramycin (500 µM) and then washed three times in DPBS for 3-mins each, before being treated with triclosan (100 µM) for 3-hours or vice versa. As a control, biofilms were also treated for 6-hrs with triclosan and tobramycin. The number of viable cells within the biofilms were quantified by BacTiter-Glo™. The assay was performed twice in in duplicate. The results represent means plus the SEM. A one-way ANOVA followed by Bonferroni’s multiple comparison post-hoc test was used to determine statistical significance between each treatment and the untreated control. *, p

Techniques Used:

DPBS starved biofilms are not more sensitive to tobramycin alone. 24-hour old biofilms were starved of nutrients by replacing media with DPBS for 5-days. Starved biofilms were treated with triclosan (100 µM), or tobramycin (500 µM), alone and in combination for 6-hrs. The number of viable cells within the biofilms was quantified using the BacTiter-Glo™ assay. The assay was performed once using three biological replicates. The results represent the means plus the SEM. A one-way ANOVA followed by Sidak’s multiple comparison post hoc test was used to determine statistical significance between the combination treatment and the untreated control and between triclosan alone or tobramycin alone and the combination treatment as indicated by the bars. *, P
Figure Legend Snippet: DPBS starved biofilms are not more sensitive to tobramycin alone. 24-hour old biofilms were starved of nutrients by replacing media with DPBS for 5-days. Starved biofilms were treated with triclosan (100 µM), or tobramycin (500 µM), alone and in combination for 6-hrs. The number of viable cells within the biofilms was quantified using the BacTiter-Glo™ assay. The assay was performed once using three biological replicates. The results represent the means plus the SEM. A one-way ANOVA followed by Sidak’s multiple comparison post hoc test was used to determine statistical significance between the combination treatment and the untreated control and between triclosan alone or tobramycin alone and the combination treatment as indicated by the bars. *, P

Techniques Used: Glo Assay

Triclosan results in increased cellular accumulation and extrusion of Texas Red conjugated tobramycin (TbTR). 24-hr old biofilms grown in glass test tubes were treated for 30-mins with triclosan (100 µM), CCCP (100 µM) and TbTR (250 µg/mL). (A) Then cells were disrupted from the biofilms and lysed with 0.2% Triton-X 100® to measure intercellular accumulation of TbTR. (B) To measure extrusion, biofilms were first treated for 30-mins and washed three-times in DPBS. Biofilms then recovered in treatment free media for 30-mins and fluorescence of the media was measured. TbTR was measured by relative fluorescence units using excitation 595 nm and emission 615 nm . Results represent the average arbitrary fluorescence units ±SEM (n=6). For panel A, a One-Way-ANOVA was performed comparing TbTR alone vs CCCP and TbTR and vs triclosan and TbTR. For panel B, an unpaired t-test was performed comparing TbTR versus triclosan and TbTR. *, p
Figure Legend Snippet: Triclosan results in increased cellular accumulation and extrusion of Texas Red conjugated tobramycin (TbTR). 24-hr old biofilms grown in glass test tubes were treated for 30-mins with triclosan (100 µM), CCCP (100 µM) and TbTR (250 µg/mL). (A) Then cells were disrupted from the biofilms and lysed with 0.2% Triton-X 100® to measure intercellular accumulation of TbTR. (B) To measure extrusion, biofilms were first treated for 30-mins and washed three-times in DPBS. Biofilms then recovered in treatment free media for 30-mins and fluorescence of the media was measured. TbTR was measured by relative fluorescence units using excitation 595 nm and emission 615 nm . Results represent the average arbitrary fluorescence units ±SEM (n=6). For panel A, a One-Way-ANOVA was performed comparing TbTR alone vs CCCP and TbTR and vs triclosan and TbTR. For panel B, an unpaired t-test was performed comparing TbTR versus triclosan and TbTR. *, p

Techniques Used: Fluorescence

2) Product Images from "An Evaluation of Blood Compatibility of Silver Nanoparticles"

Article Title: An Evaluation of Blood Compatibility of Silver Nanoparticles

Journal: Scientific Reports

doi: 10.1038/srep25518

Qualitative analysis of total complement activation by Western blotting. The expression levels of C3-α chain and cleavage products were determined by Western blotting analysis after exposure to human normal plasma to indicated concentrations of AgNPs for 30 min at 37 °C. 1 × DPBS and CVF were used as negative control and positive control, respectively. Representative immunoblotting images ( A , C ) and the band integrated density analyzed by Image J ( B , D ) were presented. Ratio meant the intensity of each protein band relative to that of negative control group. * p
Figure Legend Snippet: Qualitative analysis of total complement activation by Western blotting. The expression levels of C3-α chain and cleavage products were determined by Western blotting analysis after exposure to human normal plasma to indicated concentrations of AgNPs for 30 min at 37 °C. 1 × DPBS and CVF were used as negative control and positive control, respectively. Representative immunoblotting images ( A , C ) and the band integrated density analyzed by Image J ( B , D ) were presented. Ratio meant the intensity of each protein band relative to that of negative control group. * p

Techniques Used: Activation Assay, Western Blot, Expressing, Negative Control, Positive Control

Effect of AgNPs on platelet aggregation and coagulation. Platelet aggregation was detected by incubating PRP with different concentrations of AgNP-PVP-20 ( A ) and AgNP-CIT-20 ( B ) for 15 min. 1 × DPBS and 1.0 mg/mL collagen were used as negative control and positive control, respectively. 20% of platelet aggregation was defined as the assay threshold (dash line). In the coagulation assay, APTT, PT and TT were separately tested after exposure PPP to AgNP-PVP-20 ( C ) and AgNP-CIT-20 ( D ) for 30 min.
Figure Legend Snippet: Effect of AgNPs on platelet aggregation and coagulation. Platelet aggregation was detected by incubating PRP with different concentrations of AgNP-PVP-20 ( A ) and AgNP-CIT-20 ( B ) for 15 min. 1 × DPBS and 1.0 mg/mL collagen were used as negative control and positive control, respectively. 20% of platelet aggregation was defined as the assay threshold (dash line). In the coagulation assay, APTT, PT and TT were separately tested after exposure PPP to AgNP-PVP-20 ( C ) and AgNP-CIT-20 ( D ) for 30 min.

Techniques Used: Coagulation, Negative Control, Positive Control

3) Product Images from "Detection of Cryptosporidium parvum Oocysts on Fresh Produce Using DNA Aptamers"

Article Title: Detection of Cryptosporidium parvum Oocysts on Fresh Produce Using DNA Aptamers

Journal: PLoS ONE

doi: 10.1371/journal.pone.0137455

Affinity analyses of aptamer clones by square wave voltammetry. (A) Square wave voltammograms of developed aptasensors based on 14 aptamer sequences (R1–4 → R8–6) obtained before (violet curve) and after binding of 3,000 Cryptosporidium parvum oocysts (pink curve), whereas a control experiment is performed using an aptasensor based on the ssDNA library. All measurements were carried out after incubating the developed aptasensors with the oocysts in DPBS for 1 h at 25°C. Square wave voltammograms were carried out in the range of-400 to 800 mV with a step potential of 4 mV, amplitude of 5 mV, and frequency of 10 Hz. Electrochemical measurements were performed in PBS (pH 7.4), containing 2.5 mM of K 4 [Fe(CN) 6 ] and 2.5 mM of K 3 [Fe(CN) 6 ]. ( B) Plot of the aptamer sequence vs . the change in current intensity (ΔI) obtained after incubation of the developed respective aptasensors with 3,000 oocysts.
Figure Legend Snippet: Affinity analyses of aptamer clones by square wave voltammetry. (A) Square wave voltammograms of developed aptasensors based on 14 aptamer sequences (R1–4 → R8–6) obtained before (violet curve) and after binding of 3,000 Cryptosporidium parvum oocysts (pink curve), whereas a control experiment is performed using an aptasensor based on the ssDNA library. All measurements were carried out after incubating the developed aptasensors with the oocysts in DPBS for 1 h at 25°C. Square wave voltammograms were carried out in the range of-400 to 800 mV with a step potential of 4 mV, amplitude of 5 mV, and frequency of 10 Hz. Electrochemical measurements were performed in PBS (pH 7.4), containing 2.5 mM of K 4 [Fe(CN) 6 ] and 2.5 mM of K 3 [Fe(CN) 6 ]. ( B) Plot of the aptamer sequence vs . the change in current intensity (ΔI) obtained after incubation of the developed respective aptasensors with 3,000 oocysts.

Techniques Used: Clone Assay, Binding Assay, Sequencing, Incubation

4) Product Images from "Detection of Cryptosporidium parvum Oocysts on Fresh Produce Using DNA Aptamers"

Article Title: Detection of Cryptosporidium parvum Oocysts on Fresh Produce Using DNA Aptamers

Journal: PLoS ONE

doi: 10.1371/journal.pone.0137455

Affinity analyses of aptamer clones by square wave voltammetry. (A) Square wave voltammograms of developed aptasensors based on 14 aptamer sequences (R1–4 → R8–6) obtained before (violet curve) and after binding of 3,000 Cryptosporidium parvum oocysts (pink curve), whereas a control experiment is performed using an aptasensor based on the ssDNA library. All measurements were carried out after incubating the developed aptasensors with the oocysts in DPBS for 1 h at 25°C. Square wave voltammograms were carried out in the range of-400 to 800 mV with a step potential of 4 mV, amplitude of 5 mV, and frequency of 10 Hz. Electrochemical measurements were performed in PBS (pH 7.4), containing 2.5 mM of K 4 [Fe(CN) 6 ] and 2.5 mM of K 3 [Fe(CN) 6 ]. ( B) Plot of the aptamer sequence vs . the change in current intensity (ΔI) obtained after incubation of the developed respective aptasensors with 3,000 oocysts.
Figure Legend Snippet: Affinity analyses of aptamer clones by square wave voltammetry. (A) Square wave voltammograms of developed aptasensors based on 14 aptamer sequences (R1–4 → R8–6) obtained before (violet curve) and after binding of 3,000 Cryptosporidium parvum oocysts (pink curve), whereas a control experiment is performed using an aptasensor based on the ssDNA library. All measurements were carried out after incubating the developed aptasensors with the oocysts in DPBS for 1 h at 25°C. Square wave voltammograms were carried out in the range of-400 to 800 mV with a step potential of 4 mV, amplitude of 5 mV, and frequency of 10 Hz. Electrochemical measurements were performed in PBS (pH 7.4), containing 2.5 mM of K 4 [Fe(CN) 6 ] and 2.5 mM of K 3 [Fe(CN) 6 ]. ( B) Plot of the aptamer sequence vs . the change in current intensity (ΔI) obtained after incubation of the developed respective aptasensors with 3,000 oocysts.

Techniques Used: Clone Assay, Binding Assay, Sequencing, Incubation

5) Product Images from "An Evaluation of Blood Compatibility of Silver Nanoparticles"

Article Title: An Evaluation of Blood Compatibility of Silver Nanoparticles

Journal: Scientific Reports

doi: 10.1038/srep25518

Qualitative analysis of total complement activation by Western blotting. The expression levels of C3-α chain and cleavage products were determined by Western blotting analysis after exposure to human normal plasma to indicated concentrations of AgNPs for 30 min at 37 °C. 1 × DPBS and CVF were used as negative control and positive control, respectively. Representative immunoblotting images ( A , C ) and the band integrated density analyzed by Image J ( B , D ) were presented. Ratio meant the intensity of each protein band relative to that of negative control group. * p
Figure Legend Snippet: Qualitative analysis of total complement activation by Western blotting. The expression levels of C3-α chain and cleavage products were determined by Western blotting analysis after exposure to human normal plasma to indicated concentrations of AgNPs for 30 min at 37 °C. 1 × DPBS and CVF were used as negative control and positive control, respectively. Representative immunoblotting images ( A , C ) and the band integrated density analyzed by Image J ( B , D ) were presented. Ratio meant the intensity of each protein band relative to that of negative control group. * p

Techniques Used: Activation Assay, Western Blot, Expressing, Negative Control, Positive Control

Effect of AgNPs on platelet aggregation and coagulation. Platelet aggregation was detected by incubating PRP with different concentrations of AgNP-PVP-20 ( A ) and AgNP-CIT-20 ( B ) for 15 min. 1 × DPBS and 1.0 mg/mL collagen were used as negative control and positive control, respectively. 20% of platelet aggregation was defined as the assay threshold (dash line). In the coagulation assay, APTT, PT and TT were separately tested after exposure PPP to AgNP-PVP-20 ( C ) and AgNP-CIT-20 ( D ) for 30 min.
Figure Legend Snippet: Effect of AgNPs on platelet aggregation and coagulation. Platelet aggregation was detected by incubating PRP with different concentrations of AgNP-PVP-20 ( A ) and AgNP-CIT-20 ( B ) for 15 min. 1 × DPBS and 1.0 mg/mL collagen were used as negative control and positive control, respectively. 20% of platelet aggregation was defined as the assay threshold (dash line). In the coagulation assay, APTT, PT and TT were separately tested after exposure PPP to AgNP-PVP-20 ( C ) and AgNP-CIT-20 ( D ) for 30 min.

Techniques Used: Coagulation, Negative Control, Positive Control

6) Product Images from "An Evaluation of Blood Compatibility of Silver Nanoparticles"

Article Title: An Evaluation of Blood Compatibility of Silver Nanoparticles

Journal: Scientific Reports

doi: 10.1038/srep25518

Qualitative analysis of total complement activation by Western blotting. The expression levels of C3-α chain and cleavage products were determined by Western blotting analysis after exposure to human normal plasma to indicated concentrations of AgNPs for 30 min at 37 °C. 1 × DPBS and CVF were used as negative control and positive control, respectively. Representative immunoblotting images ( A , C ) and the band integrated density analyzed by Image J ( B , D ) were presented. Ratio meant the intensity of each protein band relative to that of negative control group. * p
Figure Legend Snippet: Qualitative analysis of total complement activation by Western blotting. The expression levels of C3-α chain and cleavage products were determined by Western blotting analysis after exposure to human normal plasma to indicated concentrations of AgNPs for 30 min at 37 °C. 1 × DPBS and CVF were used as negative control and positive control, respectively. Representative immunoblotting images ( A , C ) and the band integrated density analyzed by Image J ( B , D ) were presented. Ratio meant the intensity of each protein band relative to that of negative control group. * p

Techniques Used: Activation Assay, Western Blot, Expressing, Negative Control, Positive Control

Effect of AgNPs on platelet aggregation and coagulation. Platelet aggregation was detected by incubating PRP with different concentrations of AgNP-PVP-20 ( A ) and AgNP-CIT-20 ( B ) for 15 min. 1 × DPBS and 1.0 mg/mL collagen were used as negative control and positive control, respectively. 20% of platelet aggregation was defined as the assay threshold (dash line). In the coagulation assay, APTT, PT and TT were separately tested after exposure PPP to AgNP-PVP-20 ( C ) and AgNP-CIT-20 ( D ) for 30 min.
Figure Legend Snippet: Effect of AgNPs on platelet aggregation and coagulation. Platelet aggregation was detected by incubating PRP with different concentrations of AgNP-PVP-20 ( A ) and AgNP-CIT-20 ( B ) for 15 min. 1 × DPBS and 1.0 mg/mL collagen were used as negative control and positive control, respectively. 20% of platelet aggregation was defined as the assay threshold (dash line). In the coagulation assay, APTT, PT and TT were separately tested after exposure PPP to AgNP-PVP-20 ( C ) and AgNP-CIT-20 ( D ) for 30 min.

Techniques Used: Coagulation, Negative Control, Positive Control

7) Product Images from "An Evaluation of Blood Compatibility of Silver Nanoparticles"

Article Title: An Evaluation of Blood Compatibility of Silver Nanoparticles

Journal: Scientific Reports

doi: 10.1038/srep25518

Qualitative analysis of total complement activation by Western blotting. The expression levels of C3-α chain and cleavage products were determined by Western blotting analysis after exposure to human normal plasma to indicated concentrations of AgNPs for 30 min at 37 °C. 1 × DPBS and CVF were used as negative control and positive control, respectively. Representative immunoblotting images ( A , C ) and the band integrated density analyzed by Image J ( B , D ) were presented. Ratio meant the intensity of each protein band relative to that of negative control group. * p
Figure Legend Snippet: Qualitative analysis of total complement activation by Western blotting. The expression levels of C3-α chain and cleavage products were determined by Western blotting analysis after exposure to human normal plasma to indicated concentrations of AgNPs for 30 min at 37 °C. 1 × DPBS and CVF were used as negative control and positive control, respectively. Representative immunoblotting images ( A , C ) and the band integrated density analyzed by Image J ( B , D ) were presented. Ratio meant the intensity of each protein band relative to that of negative control group. * p

Techniques Used: Activation Assay, Western Blot, Expressing, Negative Control, Positive Control

Effect of AgNPs on platelet aggregation and coagulation. Platelet aggregation was detected by incubating PRP with different concentrations of AgNP-PVP-20 ( A ) and AgNP-CIT-20 ( B ) for 15 min. 1 × DPBS and 1.0 mg/mL collagen were used as negative control and positive control, respectively. 20% of platelet aggregation was defined as the assay threshold (dash line). In the coagulation assay, APTT, PT and TT were separately tested after exposure PPP to AgNP-PVP-20 ( C ) and AgNP-CIT-20 ( D ) for 30 min.
Figure Legend Snippet: Effect of AgNPs on platelet aggregation and coagulation. Platelet aggregation was detected by incubating PRP with different concentrations of AgNP-PVP-20 ( A ) and AgNP-CIT-20 ( B ) for 15 min. 1 × DPBS and 1.0 mg/mL collagen were used as negative control and positive control, respectively. 20% of platelet aggregation was defined as the assay threshold (dash line). In the coagulation assay, APTT, PT and TT were separately tested after exposure PPP to AgNP-PVP-20 ( C ) and AgNP-CIT-20 ( D ) for 30 min.

Techniques Used: Coagulation, Negative Control, Positive Control

8) Product Images from "An Evaluation of Blood Compatibility of Silver Nanoparticles"

Article Title: An Evaluation of Blood Compatibility of Silver Nanoparticles

Journal: Scientific Reports

doi: 10.1038/srep25518

Qualitative analysis of total complement activation by Western blotting. The expression levels of C3-α chain and cleavage products were determined by Western blotting analysis after exposure to human normal plasma to indicated concentrations of AgNPs for 30 min at 37 °C. 1 × DPBS and CVF were used as negative control and positive control, respectively. Representative immunoblotting images ( A , C ) and the band integrated density analyzed by Image J ( B , D ) were presented. Ratio meant the intensity of each protein band relative to that of negative control group. * p
Figure Legend Snippet: Qualitative analysis of total complement activation by Western blotting. The expression levels of C3-α chain and cleavage products were determined by Western blotting analysis after exposure to human normal plasma to indicated concentrations of AgNPs for 30 min at 37 °C. 1 × DPBS and CVF were used as negative control and positive control, respectively. Representative immunoblotting images ( A , C ) and the band integrated density analyzed by Image J ( B , D ) were presented. Ratio meant the intensity of each protein band relative to that of negative control group. * p

Techniques Used: Activation Assay, Western Blot, Expressing, Negative Control, Positive Control

Effect of AgNPs on platelet aggregation and coagulation. Platelet aggregation was detected by incubating PRP with different concentrations of AgNP-PVP-20 ( A ) and AgNP-CIT-20 ( B ) for 15 min. 1 × DPBS and 1.0 mg/mL collagen were used as negative control and positive control, respectively. 20% of platelet aggregation was defined as the assay threshold (dash line). In the coagulation assay, APTT, PT and TT were separately tested after exposure PPP to AgNP-PVP-20 ( C ) and AgNP-CIT-20 ( D ) for 30 min.
Figure Legend Snippet: Effect of AgNPs on platelet aggregation and coagulation. Platelet aggregation was detected by incubating PRP with different concentrations of AgNP-PVP-20 ( A ) and AgNP-CIT-20 ( B ) for 15 min. 1 × DPBS and 1.0 mg/mL collagen were used as negative control and positive control, respectively. 20% of platelet aggregation was defined as the assay threshold (dash line). In the coagulation assay, APTT, PT and TT were separately tested after exposure PPP to AgNP-PVP-20 ( C ) and AgNP-CIT-20 ( D ) for 30 min.

Techniques Used: Coagulation, Negative Control, Positive Control

9) Product Images from "PTH1 Receptor Is Involved in Mediating Cellular Response to Long-Chain Polyunsaturated Fatty Acids"

Article Title: PTH1 Receptor Is Involved in Mediating Cellular Response to Long-Chain Polyunsaturated Fatty Acids

Journal: PLoS ONE

doi: 10.1371/journal.pone.0052583

PTH1R antagonist inhibits ERK1/2 response to PTH(1–34) and fatty acids. (A) Effect of 1 µM of PTH1R antagonist [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) on pERK stimulated with: 10 nM PTH(1–34), 1 µM EPA and 1 µM DHA in DPBS for 5 minutes in HEK293 cells transfected with PTH1R. (B) Effect of 1 µM of PTH1R antagonist, [Nle 8,18 ,Tyr 34 ]PTH(3–34), on pERK stimulated with 10 nM PTH(1–34), 1 µM EPA, and 1 µM DHA in MC3T3-E1 cells expressing endogenous PTH1R. (C) Dose response to EPA at different concentrations of antagonist [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) in HEK293 cells. (D) Schild plot of [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) antagonism on EPA-stimulated PTH1R in HEK293 cells. Experiments were done 24 h after transfection of HEK293 cells with PTH1R in 12-well plates. Ratio of pERK to ERK was measured using western blots. Data represents the mean of at least four independent experiments.
Figure Legend Snippet: PTH1R antagonist inhibits ERK1/2 response to PTH(1–34) and fatty acids. (A) Effect of 1 µM of PTH1R antagonist [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) on pERK stimulated with: 10 nM PTH(1–34), 1 µM EPA and 1 µM DHA in DPBS for 5 minutes in HEK293 cells transfected with PTH1R. (B) Effect of 1 µM of PTH1R antagonist, [Nle 8,18 ,Tyr 34 ]PTH(3–34), on pERK stimulated with 10 nM PTH(1–34), 1 µM EPA, and 1 µM DHA in MC3T3-E1 cells expressing endogenous PTH1R. (C) Dose response to EPA at different concentrations of antagonist [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) in HEK293 cells. (D) Schild plot of [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) antagonism on EPA-stimulated PTH1R in HEK293 cells. Experiments were done 24 h after transfection of HEK293 cells with PTH1R in 12-well plates. Ratio of pERK to ERK was measured using western blots. Data represents the mean of at least four independent experiments.

Techniques Used: Transfection, Expressing, Western Blot

10) Product Images from "Activity of Bradykinin B2 Receptor Is Regulated by Long-Chain Polyunsaturated Fatty Acids"

Article Title: Activity of Bradykinin B2 Receptor Is Regulated by Long-Chain Polyunsaturated Fatty Acids

Journal: PLoS ONE

doi: 10.1371/journal.pone.0068151

B 2 R antagonist inhibits ERK1/2 response to bradykinin and fatty acids. (A) Effect of 1µM of B 2 R antagonist HOE-140 on pERK stimulated with: 100 nM bradykinin, 1 µM EPA and 10 µM DHA in DPBS for 5 minutes at 37°C. Experiments were done 24 h after transfection of HEK293 cells with B 2 R in 12-well plates. (B) Effect of 1 µM of B 2 R antagonist HOE-140, on pERK stimulated with 10 nM BK, 1 µM EPA and 1 µM DHA in BAECs expressing endogenous B 2 R. Ratio of pERK to ERK was measured using western blots. (C) Effect of 1 µM of B 2 R antagonist HOE-140, on pERK stimulated with 100 nM NA in BAECs expressing endogenous adrenergic receptors. Data represent the mean of at least four independent experiments.
Figure Legend Snippet: B 2 R antagonist inhibits ERK1/2 response to bradykinin and fatty acids. (A) Effect of 1µM of B 2 R antagonist HOE-140 on pERK stimulated with: 100 nM bradykinin, 1 µM EPA and 10 µM DHA in DPBS for 5 minutes at 37°C. Experiments were done 24 h after transfection of HEK293 cells with B 2 R in 12-well plates. (B) Effect of 1 µM of B 2 R antagonist HOE-140, on pERK stimulated with 10 nM BK, 1 µM EPA and 1 µM DHA in BAECs expressing endogenous B 2 R. Ratio of pERK to ERK was measured using western blots. (C) Effect of 1 µM of B 2 R antagonist HOE-140, on pERK stimulated with 100 nM NA in BAECs expressing endogenous adrenergic receptors. Data represent the mean of at least four independent experiments.

Techniques Used: Transfection, Expressing, Western Blot

Related Articles

Negative Control:

Article Title: An Evaluation of Blood Compatibility of Silver Nanoparticles
Article Snippet: .. 100 μL 1 × DPBS as blank, AgNPs solution in 1 × DPBS, polyethylene glycol (PEG, Sigma-Aldrich, USA) as negative control or Triton-X-100 (Sigma-Aldrich, USA) as positive control were added to 700 μL 1 × DPBS in different tubes. ..

Article Title: An Evaluation of Blood Compatibility of Silver Nanoparticles
Article Snippet: .. Platelet aggregation assay Platelet-rich plasma (PRP) was obtained by pooling fresh human plasma from at least three donors by centrifugation at 200 × g for 8 min. 25 μL of AgNPs solution diluted by 1 × DPBS, 1 × DPBS as negative control or 1.0 mg/mL collagen (Sigma-Aldrich, USA) as positive control were mixed with 100 μL PRP, respectively. .. The platelet counting (PC) was performed by XS-800i automatic blood analyzer (Sysmex, Japan).

Selection:

Article Title: Detection of Cryptosporidium parvum Oocysts on Fresh Produce Using DNA Aptamers
Article Snippet: .. Prior to selection experiments, 3x105 C . parvum oocysts (Waterborne, Inc., LA, USA) were washed twice in DPBS at 3,500 x g for 5 min and resuspended in DPBS containing 5mg/mL yeast tRNA (Cat. # 55714, EMD Millipore) and 1mg/mL bovine serum albumen (Cat. # B9000, New England BioLabs, MA, USA), and used for each round of selection. .. In the first round, oocysts were incubated in 100 μL of DPBS containing 1 μM of ssDNA library for 30 min at 25°C and then centrifuged at 14,000 x g for 10 min at 15°C, to remove unbound aptamers, followed by rinsing twice with DPBS.

Centrifugation:

Article Title: An Evaluation of Blood Compatibility of Silver Nanoparticles
Article Snippet: .. Platelet aggregation assay Platelet-rich plasma (PRP) was obtained by pooling fresh human plasma from at least three donors by centrifugation at 200 × g for 8 min. 25 μL of AgNPs solution diluted by 1 × DPBS, 1 × DPBS as negative control or 1.0 mg/mL collagen (Sigma-Aldrich, USA) as positive control were mixed with 100 μL PRP, respectively. .. The platelet counting (PC) was performed by XS-800i automatic blood analyzer (Sysmex, Japan).

Positive Control:

Article Title: An Evaluation of Blood Compatibility of Silver Nanoparticles
Article Snippet: .. 100 μL 1 × DPBS as blank, AgNPs solution in 1 × DPBS, polyethylene glycol (PEG, Sigma-Aldrich, USA) as negative control or Triton-X-100 (Sigma-Aldrich, USA) as positive control were added to 700 μL 1 × DPBS in different tubes. ..

Article Title: An Evaluation of Blood Compatibility of Silver Nanoparticles
Article Snippet: .. Platelet aggregation assay Platelet-rich plasma (PRP) was obtained by pooling fresh human plasma from at least three donors by centrifugation at 200 × g for 8 min. 25 μL of AgNPs solution diluted by 1 × DPBS, 1 × DPBS as negative control or 1.0 mg/mL collagen (Sigma-Aldrich, USA) as positive control were mixed with 100 μL PRP, respectively. .. The platelet counting (PC) was performed by XS-800i automatic blood analyzer (Sysmex, Japan).

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    Millipore dpbs
    Affinity analyses of aptamer clones by square wave voltammetry. (A) Square wave voltammograms of developed aptasensors based on 14 aptamer sequences (R1–4 → R8–6) obtained before (violet curve) and after binding of 3,000 Cryptosporidium <t>parvum</t> oocysts (pink curve), whereas a control experiment is performed using an aptasensor based on the ssDNA library. All measurements were carried out after incubating the developed aptasensors with the oocysts in <t>DPBS</t> for 1 h at 25°C. Square wave voltammograms were carried out in the range of-400 to 800 mV with a step potential of 4 mV, amplitude of 5 mV, and frequency of 10 Hz. Electrochemical measurements were performed in PBS (pH 7.4), containing 2.5 mM of K 4 [Fe(CN) 6 ] and 2.5 mM of K 3 [Fe(CN) 6 ]. ( B) Plot of the aptamer sequence vs . the change in current intensity (ΔI) obtained after incubation of the developed respective aptasensors with 3,000 oocysts.
    Dpbs, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 213 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Affinity analyses of aptamer clones by square wave voltammetry. (A) Square wave voltammograms of developed aptasensors based on 14 aptamer sequences (R1–4 → R8–6) obtained before (violet curve) and after binding of 3,000 Cryptosporidium parvum oocysts (pink curve), whereas a control experiment is performed using an aptasensor based on the ssDNA library. All measurements were carried out after incubating the developed aptasensors with the oocysts in DPBS for 1 h at 25°C. Square wave voltammograms were carried out in the range of-400 to 800 mV with a step potential of 4 mV, amplitude of 5 mV, and frequency of 10 Hz. Electrochemical measurements were performed in PBS (pH 7.4), containing 2.5 mM of K 4 [Fe(CN) 6 ] and 2.5 mM of K 3 [Fe(CN) 6 ]. ( B) Plot of the aptamer sequence vs . the change in current intensity (ΔI) obtained after incubation of the developed respective aptasensors with 3,000 oocysts.

    Journal: PLoS ONE

    Article Title: Detection of Cryptosporidium parvum Oocysts on Fresh Produce Using DNA Aptamers

    doi: 10.1371/journal.pone.0137455

    Figure Lengend Snippet: Affinity analyses of aptamer clones by square wave voltammetry. (A) Square wave voltammograms of developed aptasensors based on 14 aptamer sequences (R1–4 → R8–6) obtained before (violet curve) and after binding of 3,000 Cryptosporidium parvum oocysts (pink curve), whereas a control experiment is performed using an aptasensor based on the ssDNA library. All measurements were carried out after incubating the developed aptasensors with the oocysts in DPBS for 1 h at 25°C. Square wave voltammograms were carried out in the range of-400 to 800 mV with a step potential of 4 mV, amplitude of 5 mV, and frequency of 10 Hz. Electrochemical measurements were performed in PBS (pH 7.4), containing 2.5 mM of K 4 [Fe(CN) 6 ] and 2.5 mM of K 3 [Fe(CN) 6 ]. ( B) Plot of the aptamer sequence vs . the change in current intensity (ΔI) obtained after incubation of the developed respective aptasensors with 3,000 oocysts.

    Article Snippet: Prior to selection experiments, 3x105 C . parvum oocysts (Waterborne, Inc., LA, USA) were washed twice in DPBS at 3,500 x g for 5 min and resuspended in DPBS containing 5mg/mL yeast tRNA (Cat. # 55714, EMD Millipore) and 1mg/mL bovine serum albumen (Cat. # B9000, New England BioLabs, MA, USA), and used for each round of selection.

    Techniques: Clone Assay, Binding Assay, Sequencing, Incubation

    PTH1R antagonist inhibits ERK1/2 response to PTH(1–34) and fatty acids. (A) Effect of 1 µM of PTH1R antagonist [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) on pERK stimulated with: 10 nM PTH(1–34), 1 µM EPA and 1 µM DHA in DPBS for 5 minutes in HEK293 cells transfected with PTH1R. (B) Effect of 1 µM of PTH1R antagonist, [Nle 8,18 ,Tyr 34 ]PTH(3–34), on pERK stimulated with 10 nM PTH(1–34), 1 µM EPA, and 1 µM DHA in MC3T3-E1 cells expressing endogenous PTH1R. (C) Dose response to EPA at different concentrations of antagonist [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) in HEK293 cells. (D) Schild plot of [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) antagonism on EPA-stimulated PTH1R in HEK293 cells. Experiments were done 24 h after transfection of HEK293 cells with PTH1R in 12-well plates. Ratio of pERK to ERK was measured using western blots. Data represents the mean of at least four independent experiments.

    Journal: PLoS ONE

    Article Title: PTH1 Receptor Is Involved in Mediating Cellular Response to Long-Chain Polyunsaturated Fatty Acids

    doi: 10.1371/journal.pone.0052583

    Figure Lengend Snippet: PTH1R antagonist inhibits ERK1/2 response to PTH(1–34) and fatty acids. (A) Effect of 1 µM of PTH1R antagonist [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) on pERK stimulated with: 10 nM PTH(1–34), 1 µM EPA and 1 µM DHA in DPBS for 5 minutes in HEK293 cells transfected with PTH1R. (B) Effect of 1 µM of PTH1R antagonist, [Nle 8,18 ,Tyr 34 ]PTH(3–34), on pERK stimulated with 10 nM PTH(1–34), 1 µM EPA, and 1 µM DHA in MC3T3-E1 cells expressing endogenous PTH1R. (C) Dose response to EPA at different concentrations of antagonist [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) in HEK293 cells. (D) Schild plot of [Leu 11 ,D-Trp 12 ]PTH-rP(7–34) antagonism on EPA-stimulated PTH1R in HEK293 cells. Experiments were done 24 h after transfection of HEK293 cells with PTH1R in 12-well plates. Ratio of pERK to ERK was measured using western blots. Data represents the mean of at least four independent experiments.

    Article Snippet: Western blot analysis Both MC3T3-E1 and HEK293 cells were washed with ice cold DPBS, collected, and lysed in lysis buffer containing 50 mM Tris –HCl, 135 mM NaCl, 60 mM n-octyl beta-D-glucopyranoside (EMD Chemicals, Gibbstown, NJ, USA), protease inhibitor cocktail, and phospahtase inhibitor cocktail (Roche, Basel, Switzerland) for 30 minutes on ice.

    Techniques: Transfection, Expressing, Western Blot

    B 2 R antagonist inhibits ERK1/2 response to bradykinin and fatty acids. (A) Effect of 1µM of B 2 R antagonist HOE-140 on pERK stimulated with: 100 nM bradykinin, 1 µM EPA and 10 µM DHA in DPBS for 5 minutes at 37°C. Experiments were done 24 h after transfection of HEK293 cells with B 2 R in 12-well plates. (B) Effect of 1 µM of B 2 R antagonist HOE-140, on pERK stimulated with 10 nM BK, 1 µM EPA and 1 µM DHA in BAECs expressing endogenous B 2 R. Ratio of pERK to ERK was measured using western blots. (C) Effect of 1 µM of B 2 R antagonist HOE-140, on pERK stimulated with 100 nM NA in BAECs expressing endogenous adrenergic receptors. Data represent the mean of at least four independent experiments.

    Journal: PLoS ONE

    Article Title: Activity of Bradykinin B2 Receptor Is Regulated by Long-Chain Polyunsaturated Fatty Acids

    doi: 10.1371/journal.pone.0068151

    Figure Lengend Snippet: B 2 R antagonist inhibits ERK1/2 response to bradykinin and fatty acids. (A) Effect of 1µM of B 2 R antagonist HOE-140 on pERK stimulated with: 100 nM bradykinin, 1 µM EPA and 10 µM DHA in DPBS for 5 minutes at 37°C. Experiments were done 24 h after transfection of HEK293 cells with B 2 R in 12-well plates. (B) Effect of 1 µM of B 2 R antagonist HOE-140, on pERK stimulated with 10 nM BK, 1 µM EPA and 1 µM DHA in BAECs expressing endogenous B 2 R. Ratio of pERK to ERK was measured using western blots. (C) Effect of 1 µM of B 2 R antagonist HOE-140, on pERK stimulated with 100 nM NA in BAECs expressing endogenous adrenergic receptors. Data represent the mean of at least four independent experiments.

    Article Snippet: Western Blot Analysis HEK293 cells were washed twice in DPBS, collected, and lysed in lysis buffer containing 50 mM Tris –HCl, 135 mM NaCl, 60 mM n-octyl beta-D-glucopyranoside (EMD Chemicals, Gibbstown, NJ, USA), protease inhibitor cocktail, and phospahtase inhibitor cocktail (Roche, Basel, Switzerland) for 30 minutes on ice.

    Techniques: Transfection, Expressing, Western Blot