Structured Review

Millipore dpbs
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 <t>AgNPs</t> for 30 min at 37 °C. 1 × <t>DPBS</t> 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
Dpbs, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 78 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/dpbs/product/Millipore
Average 95 stars, based on 78 article reviews
Price from $9.99 to $1999.99
dpbs - by Bioz Stars, 2020-05
95/100 stars

Images

1) 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

2) 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

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 "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

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 "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

9) 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

10) Product Images from "An Inactivated Antibiotic-Exposed Whole-Cell Vaccine Enhances Bactericidal Activities Against Multidrug-Resistant Acinetobacter baumannii"

Article Title: An Inactivated Antibiotic-Exposed Whole-Cell Vaccine Enhances Bactericidal Activities Against Multidrug-Resistant Acinetobacter baumannii

Journal: Scientific Reports

doi: 10.1038/srep22332

Complement-mediated bacteriolysis activity of sera from mice inoculated with I-M28-47 and I-M28-47-114 against two different MDR A. baumannii growth conditions. The lysis activity percentages were determined using sera from mice inoculated with I-M28-47-114, I-M28-47 (control) or DPBS (placebo control) in presence of baby rabbit complement against MDR A. baumannii ( a ) cultured without imipenem treatment or ( b ) treated with 32 mg/L imipenem. The values are the means ± S.D. tested in duplicate. * P
Figure Legend Snippet: Complement-mediated bacteriolysis activity of sera from mice inoculated with I-M28-47 and I-M28-47-114 against two different MDR A. baumannii growth conditions. The lysis activity percentages were determined using sera from mice inoculated with I-M28-47-114, I-M28-47 (control) or DPBS (placebo control) in presence of baby rabbit complement against MDR A. baumannii ( a ) cultured without imipenem treatment or ( b ) treated with 32 mg/L imipenem. The values are the means ± S.D. tested in duplicate. * P

Techniques Used: Activity Assay, Mouse Assay, Lysis, Cell Culture

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.

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).

Protease Inhibitor:

Article Title: PTH1 Receptor Is Involved in Mediating Cellular Response to Long-Chain Polyunsaturated Fatty Acids
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. .. SDS sample buffer was added to the lysate and incubated at 95°C for 5 min.

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).

Western Blot:

Article Title: PTH1 Receptor Is Involved in Mediating Cellular Response to Long-Chain Polyunsaturated Fatty Acids
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. .. SDS sample buffer was added to the lysate and incubated at 95°C for 5 min.

Lysis:

Article Title: PTH1 Receptor Is Involved in Mediating Cellular Response to Long-Chain Polyunsaturated Fatty Acids
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. .. SDS sample buffer was added to the lysate and incubated at 95°C for 5 min.

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95
    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: 95/100, based on 78 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dpbs/product/Millipore
    Average 95 stars, based on 78 article reviews
    Price from $9.99 to $1999.99
    dpbs - by Bioz Stars, 2020-05
    95/100 stars
      Buy from Supplier

    Image Search Results


    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