pbs solution  (Thermo Fisher)


Bioz Verified Symbol Thermo Fisher is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99

    Structured Review

    Thermo Fisher pbs solution
    Confocal micrographs showing the uptake by MCs of C6-LP ( A ), 6%-TRX-C6-LP ( B ), 11%-TRX-C6-LP ( C ), and 14%-TRX-C6-LP ( D ) after 24 h incubation (C6: green). Notes: MCs were incubated with C6-LP (control) or TRX-C6-LPs at a lipid concentration of 0.8 mg/mL for 2 h in serum-free RPMI 1640 at <t>37°C</t> and then washed with <t>PBS</t> to terminate the uptake process. After fixation in 10% neutral buffer formalin, the cells were counterstained with DAPI (blue) for observation under a laser confocal microscope. Magnification ×400. Abbreviations: C6, Coumarin-6; C6-LP, Coumarin-6-loaded liposomes; DAPI, dihydrochloride; MCs, mesangial cells; PBS, phosphate-buffered saline; TRX-C6-LP, TRX-20-modified Coumarin-6-loaded liposomes.
    Pbs Solution, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 369 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pbs solution/product/Thermo Fisher
    Average 99 stars, based on 369 article reviews
    Price from $9.99 to $1999.99
    pbs solution - by Bioz Stars, 2020-08
    99/100 stars

    Images

    1) Product Images from "Renal-targeted delivery of triptolide by entrapment in pegylated TRX-20-modified liposomes"

    Article Title: Renal-targeted delivery of triptolide by entrapment in pegylated TRX-20-modified liposomes

    Journal: International Journal of Nanomedicine

    doi: 10.2147/IJN.S141095

    Confocal micrographs showing the uptake by MCs of C6-LP ( A ), 6%-TRX-C6-LP ( B ), 11%-TRX-C6-LP ( C ), and 14%-TRX-C6-LP ( D ) after 24 h incubation (C6: green). Notes: MCs were incubated with C6-LP (control) or TRX-C6-LPs at a lipid concentration of 0.8 mg/mL for 2 h in serum-free RPMI 1640 at 37°C and then washed with PBS to terminate the uptake process. After fixation in 10% neutral buffer formalin, the cells were counterstained with DAPI (blue) for observation under a laser confocal microscope. Magnification ×400. Abbreviations: C6, Coumarin-6; C6-LP, Coumarin-6-loaded liposomes; DAPI, dihydrochloride; MCs, mesangial cells; PBS, phosphate-buffered saline; TRX-C6-LP, TRX-20-modified Coumarin-6-loaded liposomes.
    Figure Legend Snippet: Confocal micrographs showing the uptake by MCs of C6-LP ( A ), 6%-TRX-C6-LP ( B ), 11%-TRX-C6-LP ( C ), and 14%-TRX-C6-LP ( D ) after 24 h incubation (C6: green). Notes: MCs were incubated with C6-LP (control) or TRX-C6-LPs at a lipid concentration of 0.8 mg/mL for 2 h in serum-free RPMI 1640 at 37°C and then washed with PBS to terminate the uptake process. After fixation in 10% neutral buffer formalin, the cells were counterstained with DAPI (blue) for observation under a laser confocal microscope. Magnification ×400. Abbreviations: C6, Coumarin-6; C6-LP, Coumarin-6-loaded liposomes; DAPI, dihydrochloride; MCs, mesangial cells; PBS, phosphate-buffered saline; TRX-C6-LP, TRX-20-modified Coumarin-6-loaded liposomes.

    Techniques Used: Incubation, Concentration Assay, Microscopy, Modification

    2) Product Images from "Liposomes for HIV prophylaxis"

    Article Title: Liposomes for HIV prophylaxis

    Journal: Biomaterials

    doi: 10.1016/j.biomaterials.2011.07.068

    A. Live animal imaging after intravaginal instillation of CL 40 DMPC 60 liposomes encapsulating Dylight 649 (20 mg/mL) or PBS (middle animal in each image) at various time points . B. Quantification of radiant efficiency at each time point around the region of interest. Data are means ± SD with n = 8 in each group
    Figure Legend Snippet: A. Live animal imaging after intravaginal instillation of CL 40 DMPC 60 liposomes encapsulating Dylight 649 (20 mg/mL) or PBS (middle animal in each image) at various time points . B. Quantification of radiant efficiency at each time point around the region of interest. Data are means ± SD with n = 8 in each group

    Techniques Used: Imaging

    3) Product Images from "Transglutaminase-2 facilitates extracellular vesicle-mediated establishment of the metastatic niche"

    Article Title: Transglutaminase-2 facilitates extracellular vesicle-mediated establishment of the metastatic niche

    Journal: bioRxiv

    doi: 10.1101/2019.12.16.875948

    Transglutaminase-2 promotes fibronectin crosslinking on the surface of extracellular vesicles. (A) Transmission electron micrographs of extracellular vesicles derived from control (GFP) and TGM2 overexpressing HME2, and control (shMT) and TGM2 depleted (shTGM2) HME2-BM cells. (B) Immunoblot analysis of EVs derived from the HME2 and HME2-BM cells described in panel A. Differential expression of TGM2 was verified in these EV lysates and correlated with covalent linkage of FN dimers that are insensitive to reducing conditions of the SDS-PAGE. CD63 served as a loading control. (C) Extracellular vesicle preparations derived from the cell types described in panel A were stained with CM-Dil (yellow) to verify the presence of a lipid containing particles. These preparations were also stained with antibodies specific for CD63 (green) and FN3 (red) and imaged using confocal microscope. The green (CD63) and red (FN3) channels were merged. A blank control sample (PBS) stained with the CM-Dil and appropriate secondary antibodies is also shown. (D) Extracellular vesicles derived from HME2-BM and HME2-TGM2 cells were stained with CM-Dil (yellow), and antibodies specific for TGM2 (green) and FN3 (red) and imaged using a confocal microscope. The green (TGM2) and red (FN3) channels were merged. Scale bars on panels C and D are 500 nm.
    Figure Legend Snippet: Transglutaminase-2 promotes fibronectin crosslinking on the surface of extracellular vesicles. (A) Transmission electron micrographs of extracellular vesicles derived from control (GFP) and TGM2 overexpressing HME2, and control (shMT) and TGM2 depleted (shTGM2) HME2-BM cells. (B) Immunoblot analysis of EVs derived from the HME2 and HME2-BM cells described in panel A. Differential expression of TGM2 was verified in these EV lysates and correlated with covalent linkage of FN dimers that are insensitive to reducing conditions of the SDS-PAGE. CD63 served as a loading control. (C) Extracellular vesicle preparations derived from the cell types described in panel A were stained with CM-Dil (yellow) to verify the presence of a lipid containing particles. These preparations were also stained with antibodies specific for CD63 (green) and FN3 (red) and imaged using confocal microscope. The green (CD63) and red (FN3) channels were merged. A blank control sample (PBS) stained with the CM-Dil and appropriate secondary antibodies is also shown. (D) Extracellular vesicles derived from HME2-BM and HME2-TGM2 cells were stained with CM-Dil (yellow), and antibodies specific for TGM2 (green) and FN3 (red) and imaged using a confocal microscope. The green (TGM2) and red (FN3) channels were merged. Scale bars on panels C and D are 500 nm.

    Techniques Used: Transmission Assay, Derivative Assay, Expressing, SDS Page, Staining, Microscopy

    4) Product Images from "Studying protein degradation pathways in vivo using a cranial window-based approach"

    Article Title: Studying protein degradation pathways in vivo using a cranial window-based approach

    Journal: Methods (San Diego, Calif.)

    doi: 10.1016/j.ymeth.2010.12.032

    Surgical procedure for short-term dual chamber treatment of cortex. (A) View of mouse skull after removal of two symmetric hemi-cranial bone flaps and dura. (B) Application of paraffin wax to create two wells filled with PBS. (C) View of Fluoro-Ruby dextran-containing
    Figure Legend Snippet: Surgical procedure for short-term dual chamber treatment of cortex. (A) View of mouse skull after removal of two symmetric hemi-cranial bone flaps and dura. (B) Application of paraffin wax to create two wells filled with PBS. (C) View of Fluoro-Ruby dextran-containing

    Techniques Used:

    5) Product Images from "Mitigation of a nitrate reducing Pseudomonas aeruginosa biofilm and anaerobic biocorrosion using ciprofloxacin enhanced by D-tyrosine"

    Article Title: Mitigation of a nitrate reducing Pseudomonas aeruginosa biofilm and anaerobic biocorrosion using ciprofloxacin enhanced by D-tyrosine

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-07312-7

    CLSM images of PA biofilms (Dimensions: X = 224 µm, Y = 224 µm) after the 3-hour biofilm removal test in the pH 7.4 PBS buffer containing: ( a ) no treatment (control) (biofilm thickness = 72 µm), ( b ) 5 ppm D-tyr (biofilm thickness = 69 µm), ( c ) 80 ppm CIP (biofilm thickness = 49 µm), and ( d ) 80 ppm CIP + 5 ppm D-tyr (biofilm thickness = 28 µm). The calculated numbers of live/dead cells are shown in ( e ) and ( f ). (Error bars represent standard deviations, statistical reference point n = 6).
    Figure Legend Snippet: CLSM images of PA biofilms (Dimensions: X = 224 µm, Y = 224 µm) after the 3-hour biofilm removal test in the pH 7.4 PBS buffer containing: ( a ) no treatment (control) (biofilm thickness = 72 µm), ( b ) 5 ppm D-tyr (biofilm thickness = 69 µm), ( c ) 80 ppm CIP (biofilm thickness = 49 µm), and ( d ) 80 ppm CIP + 5 ppm D-tyr (biofilm thickness = 28 µm). The calculated numbers of live/dead cells are shown in ( e ) and ( f ). (Error bars represent standard deviations, statistical reference point n = 6).

    Techniques Used: Confocal Laser Scanning Microscopy

    6) Product Images from "Evaluation of Lapatinib Powder-Entrapped Biodegradable Polymeric Microstructures Fabricated by X-Ray Lithography for a Targeted and Sustained Drug Delivery System"

    Article Title: Evaluation of Lapatinib Powder-Entrapped Biodegradable Polymeric Microstructures Fabricated by X-Ray Lithography for a Targeted and Sustained Drug Delivery System

    Journal: Materials

    doi: 10.3390/ma8020519

    HPLC analysis results from one hundred of the 40-μm sizedmicrostructures in PBS solution. ( A ) Chromatogram of the microstructures without lapatinib powder; ( B) –( H ) Chromatograms of the lapatinib powder-entrapped microstructures after 24, 48, 72, 96, 120, 144, and 600 h; ( I ) Amounts of lapatinib released from one hundred of the 40-μm sized microstructures after 24, 48, 72, 96, 120, 144, and 600 h were 0.27, 0.37, 0.56, 0.66, 0.90, 1.15, and 4.01 μM, respectively.
    Figure Legend Snippet: HPLC analysis results from one hundred of the 40-μm sizedmicrostructures in PBS solution. ( A ) Chromatogram of the microstructures without lapatinib powder; ( B) –( H ) Chromatograms of the lapatinib powder-entrapped microstructures after 24, 48, 72, 96, 120, 144, and 600 h; ( I ) Amounts of lapatinib released from one hundred of the 40-μm sized microstructures after 24, 48, 72, 96, 120, 144, and 600 h were 0.27, 0.37, 0.56, 0.66, 0.90, 1.15, and 4.01 μM, respectively.

    Techniques Used: High Performance Liquid Chromatography

    7) Product Images from "Microfluidic-Based Technique for Measuring RBC Aggregation and Blood Viscosity in a Continuous and Simultaneous Fashion"

    Article Title: Microfluidic-Based Technique for Measuring RBC Aggregation and Blood Viscosity in a Continuous and Simultaneous Fashion

    Journal: Micromachines

    doi: 10.3390/mi9090467

    Quantitative evaluations of RBC aggregation index and blood viscosity under pulsatile blood flow conditions (Q max = 0.5 mL/h, Q min = 0.2 mL/h, and period (T)). Blood and PBS solution were periodically supplied into the microfluidic device, at the same flow rate. ( A ) Quantitative evaluation of the effect of period (T) on RBC aggregation index and blood viscosity for blood (Hct = 50%). Blood (Hct = 50%) was prepared by adding normal RBCs into specific concentration of dextran solution (C dextran = 10 mg/mL). (a) Variations of
    Figure Legend Snippet: Quantitative evaluations of RBC aggregation index and blood viscosity under pulsatile blood flow conditions (Q max = 0.5 mL/h, Q min = 0.2 mL/h, and period (T)). Blood and PBS solution were periodically supplied into the microfluidic device, at the same flow rate. ( A ) Quantitative evaluation of the effect of period (T) on RBC aggregation index and blood viscosity for blood (Hct = 50%). Blood (Hct = 50%) was prepared by adding normal RBCs into specific concentration of dextran solution (C dextran = 10 mg/mL). (a) Variations of

    Techniques Used: Flow Cytometry, Concentration Assay

    Quantitative evaluations of RBC aggregation index (AI PM ) under constant blood flow. Blood (Hct = 50%) was prepared by adding normal RBCs into various concentrations of dextran solution (C dextran ) (C dextran = 0 mg/mL, 5 mg/mL, 10 mg/mL, and 15 mg/mL). Blood and PBS solution were delivered into the microfluidic device at the same flow rate (Q PBS = Q Blood = Q) (Q = 0.1 mL/h, 0.2 mL/h, 0.3 mL/h, 0.4 mL/h, and 0.5 mL/h). ( A ) Variations of RBC aggregation with respect to C dextran and Q. (a) Microscopic images for representing RBC aggregation of blood (RBCs suspended in dextran solution of C dextran = 5 mg/mL) with respect to Q. (b) Microscopic images for representing RBC aggregation of blood (RBCs suspended in dextran solution (C dextran = 15 mg/mL)) with respect to Q. (c) Variations of
    Figure Legend Snippet: Quantitative evaluations of RBC aggregation index (AI PM ) under constant blood flow. Blood (Hct = 50%) was prepared by adding normal RBCs into various concentrations of dextran solution (C dextran ) (C dextran = 0 mg/mL, 5 mg/mL, 10 mg/mL, and 15 mg/mL). Blood and PBS solution were delivered into the microfluidic device at the same flow rate (Q PBS = Q Blood = Q) (Q = 0.1 mL/h, 0.2 mL/h, 0.3 mL/h, 0.4 mL/h, and 0.5 mL/h). ( A ) Variations of RBC aggregation with respect to C dextran and Q. (a) Microscopic images for representing RBC aggregation of blood (RBCs suspended in dextran solution of C dextran = 5 mg/mL) with respect to Q. (b) Microscopic images for representing RBC aggregation of blood (RBCs suspended in dextran solution (C dextran = 15 mg/mL)) with respect to Q. (c) Variations of

    Techniques Used: Flow Cytometry

    8) Product Images from "Intraperitoneal Administration of Neural Stem Cell-Nanoparticle Conjugates Targets Chemotherapy to Ovarian Tumors"

    Article Title: Intraperitoneal Administration of Neural Stem Cell-Nanoparticle Conjugates Targets Chemotherapy to Ovarian Tumors

    Journal: Bioconjugate chemistry

    doi: 10.1021/acs.bioconjchem.7b00237

    Neural stem cell tropism to peritoneal ovarian cancer metastasis (A,E,I) Representative confocal z-stack images of native neural stem cells (A), and two different NSC/NP constructs in which the NPs are either localized to the cell surface (E) or internalized (I). Cell nuclei and cytoskeleton are respectively visualized using DAPI (blue) and phalloidin staining (pseudo-colored white). Tumor cells expressed GFP (green). Note: The kidney has a very strong background signal when visualizing GFP. (B–D) NSCs labeled with CellTracker CM-DiI demonstrate good distribution in tumor but not in adjacent normal kidney (2 million NSC.DiI in 200 µL PBS injected IP on Day 38; then harvested 4 days post-NSC injection). ( F–H ) NSCs with surface conjugated NPs demonstrate good distribution in tumor but not adjacent normal liver (4 million NSC.NP in 1 mL PBS injected IP on Day 13: harvested 4 days post-NSC injection). (J–I) NSCs with internalized NPs demonstrate good distribution in tumor but not adjacent normal liver (4 million NSC/NPs in 1 mL PBS injected IP on Day 25: harvested 4 days post-NSC injection). Scale bars: B,F,J: 1000 microns; C,G,K: 500 microns; D,H,L: 200 microns.
    Figure Legend Snippet: Neural stem cell tropism to peritoneal ovarian cancer metastasis (A,E,I) Representative confocal z-stack images of native neural stem cells (A), and two different NSC/NP constructs in which the NPs are either localized to the cell surface (E) or internalized (I). Cell nuclei and cytoskeleton are respectively visualized using DAPI (blue) and phalloidin staining (pseudo-colored white). Tumor cells expressed GFP (green). Note: The kidney has a very strong background signal when visualizing GFP. (B–D) NSCs labeled with CellTracker CM-DiI demonstrate good distribution in tumor but not in adjacent normal kidney (2 million NSC.DiI in 200 µL PBS injected IP on Day 38; then harvested 4 days post-NSC injection). ( F–H ) NSCs with surface conjugated NPs demonstrate good distribution in tumor but not adjacent normal liver (4 million NSC.NP in 1 mL PBS injected IP on Day 13: harvested 4 days post-NSC injection). (J–I) NSCs with internalized NPs demonstrate good distribution in tumor but not adjacent normal liver (4 million NSC/NPs in 1 mL PBS injected IP on Day 25: harvested 4 days post-NSC injection). Scale bars: B,F,J: 1000 microns; C,G,K: 500 microns; D,H,L: 200 microns.

    Techniques Used: Construct, Staining, Labeling, Injection

    9) Product Images from "Prognostic Impact of Circulating Tumor Cell Detected Using a Novel Fluidic Cell Microarray Chip System in Patients with Breast Cancer"

    Article Title: Prognostic Impact of Circulating Tumor Cell Detected Using a Novel Fluidic Cell Microarray Chip System in Patients with Breast Cancer

    Journal: EBioMedicine

    doi: 10.1016/j.ebiom.2016.07.027

    Workflow of sample processing and movement of cells in the FCMC device. (A) Workflow of sample processing and CTC detection. (a) Blood sample collection and enrichment using Ficoll-Paque PLUS. (b) The cell suspension is loaded into the FCMC device. The cells form monolayers in the microchambers and are immunostained by using a syringe pump. (c) All microchambers are scanned using a fluorescent microscope. (d) CTC are detected from the fluorescent images. (B) Movement of cells in the FCMC device. (a) The new CM chip, which is made from polystyrene (PS), is cleaned with UV ozone and coated with BSA. (b) The FCMC device is washed with PBS. (c) A cell suspension (68 uL) that is equivalent to 0.4 mL of blood is loaded into one FCMC device. (d) After “Suction for Trapping”, untrapped cells move into downstream microchambers and settle down on the bottom of these microchambers. The blue arrows indicate flow. (e) After “Suction for Monolayer”, overlapped cells are discharged from microchambers and move to the outside of microchambers or to the inside of downstream microchambers. (f) After repetitions of (d) and (e), all cells are trapped in a monolayer. (g), (h), (i) Immunostaining solutions are loaded, incubated and washed.
    Figure Legend Snippet: Workflow of sample processing and movement of cells in the FCMC device. (A) Workflow of sample processing and CTC detection. (a) Blood sample collection and enrichment using Ficoll-Paque PLUS. (b) The cell suspension is loaded into the FCMC device. The cells form monolayers in the microchambers and are immunostained by using a syringe pump. (c) All microchambers are scanned using a fluorescent microscope. (d) CTC are detected from the fluorescent images. (B) Movement of cells in the FCMC device. (a) The new CM chip, which is made from polystyrene (PS), is cleaned with UV ozone and coated with BSA. (b) The FCMC device is washed with PBS. (c) A cell suspension (68 uL) that is equivalent to 0.4 mL of blood is loaded into one FCMC device. (d) After “Suction for Trapping”, untrapped cells move into downstream microchambers and settle down on the bottom of these microchambers. The blue arrows indicate flow. (e) After “Suction for Monolayer”, overlapped cells are discharged from microchambers and move to the outside of microchambers or to the inside of downstream microchambers. (f) After repetitions of (d) and (e), all cells are trapped in a monolayer. (g), (h), (i) Immunostaining solutions are loaded, incubated and washed.

    Techniques Used: Microscopy, Chromatin Immunoprecipitation, Flow Cytometry, Immunostaining, Incubation

    10) Product Images from "Periodic and simultaneous quantification of blood viscosity and red blood cell aggregation using a microfluidic platform under in-vitro closed-loop circulation"

    Article Title: Periodic and simultaneous quantification of blood viscosity and red blood cell aggregation using a microfluidic platform under in-vitro closed-loop circulation

    Journal: Biomicrofluidics

    doi: 10.1063/1.5017052

    Schematics for the periodic and simultaneous measurement of blood viscosity RBC aggregation using a microfluidic platform under in-vitro closed-loop circulation. (A) Schematics of the experimental setup including an in-vitro closed-loop circulation and a microfluidic platform. (a) In-vitro closed-loop circulation established by connecting several components (peristaltic pump, ACU, FD, and reservoir) with polyethylene tubes (L 5 , L 6 , L 7 , L 8 , and L 9 ) in series. After the reservoir was filled with blood (10 ml), a peristaltic pump was set to ω = 15 rpm. The air cavity in the ACU was adjusted to 2.5 ml. A specific concentration of dextran solution (i.e., C dextran = 100 mg/ml) was delivered into the reservoir by operating the syringe pump. (b) A microfluidic platform including a microfluidic device (VA), PV, and syringe pump. The outlet of the FD was connected to the inlet (B) of the VA with a polyethylene tube (L 2 ). To control the blood flow from the FD to the VA, a PV was installed in front of the inlet (B). 1× PBS solution was supplied into inlet (A) with a syringe pump. (B) Flow-rate profile of two fluids with a syringe pump (i.e., Q PBS and Q Dextran ) and PV operation (i.e., open and close) for each period. (C) Quantification of image intensity (⟨I⟩) and blood flow-rate (Q μ PIV ). (a) Quantification of the image intensity (⟨I⟩) within the ROI (484 × 150 pixels) in the upper channel. (b) Quantification of blood velocity fields with a time-resolved micro-PIV technique. The blood flow-rate (Q μ PIV ) was quantified by multiplying averaged blood velocity (⟨U⟩) by the cross-sectional area (A c ) (i.e., Q μ PIV = ⟨U⟩·A c ). (c) A simple fluidic circuit with discrete elements including fluidic resistances (R P , R B ), and flow rates (Q PBS , Q Blood ). The interface between two fluids was evaluated by converting the gray image into a binary image. (D) For a preliminary demonstration, blood (Hct = 50%) was prepared by adding normal RBCs to autologous plasma. Here, the period was set to T = 400 s. The inset shows microscopic images at a specific time (t) [(a) t = 10 s, (b) t = 100 s, (c) t = 150 s, (d) t = 200 s, (e) t = 300 s, and (f) t = 400 s]. During each period, at constant blood flow (i.e., 0
    Figure Legend Snippet: Schematics for the periodic and simultaneous measurement of blood viscosity RBC aggregation using a microfluidic platform under in-vitro closed-loop circulation. (A) Schematics of the experimental setup including an in-vitro closed-loop circulation and a microfluidic platform. (a) In-vitro closed-loop circulation established by connecting several components (peristaltic pump, ACU, FD, and reservoir) with polyethylene tubes (L 5 , L 6 , L 7 , L 8 , and L 9 ) in series. After the reservoir was filled with blood (10 ml), a peristaltic pump was set to ω = 15 rpm. The air cavity in the ACU was adjusted to 2.5 ml. A specific concentration of dextran solution (i.e., C dextran = 100 mg/ml) was delivered into the reservoir by operating the syringe pump. (b) A microfluidic platform including a microfluidic device (VA), PV, and syringe pump. The outlet of the FD was connected to the inlet (B) of the VA with a polyethylene tube (L 2 ). To control the blood flow from the FD to the VA, a PV was installed in front of the inlet (B). 1× PBS solution was supplied into inlet (A) with a syringe pump. (B) Flow-rate profile of two fluids with a syringe pump (i.e., Q PBS and Q Dextran ) and PV operation (i.e., open and close) for each period. (C) Quantification of image intensity (⟨I⟩) and blood flow-rate (Q μ PIV ). (a) Quantification of the image intensity (⟨I⟩) within the ROI (484 × 150 pixels) in the upper channel. (b) Quantification of blood velocity fields with a time-resolved micro-PIV technique. The blood flow-rate (Q μ PIV ) was quantified by multiplying averaged blood velocity (⟨U⟩) by the cross-sectional area (A c ) (i.e., Q μ PIV = ⟨U⟩·A c ). (c) A simple fluidic circuit with discrete elements including fluidic resistances (R P , R B ), and flow rates (Q PBS , Q Blood ). The interface between two fluids was evaluated by converting the gray image into a binary image. (D) For a preliminary demonstration, blood (Hct = 50%) was prepared by adding normal RBCs to autologous plasma. Here, the period was set to T = 400 s. The inset shows microscopic images at a specific time (t) [(a) t = 10 s, (b) t = 100 s, (c) t = 150 s, (d) t = 200 s, (e) t = 300 s, and (f) t = 400 s]. During each period, at constant blood flow (i.e., 0

    Techniques Used: In Vitro, Concentration Assay, Flow Cytometry

    11) Product Images from "Botulinum Neurotoxin D Uses Synaptic Vesicle Protein SV2 and Gangliosides as Receptors"

    Article Title: Botulinum Neurotoxin D Uses Synaptic Vesicle Protein SV2 and Gangliosides as Receptors

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.1002008

    Stimulation of synaptic vesicle recycling increases the binding and entry of BoNT/D into neurons. A) Cultured rat hippocampal neurons were exposed to BoNT/D (100 pM, 5 min) in either resting condition (PBS) or stimulated conditions (high K + buffer: PBS with 56 mM KCl and 1 mM Ca 2+ ). Cells were washed and further incubated in toxin-free media for 6 hrs. Cell lysates were subjected to immunoblot analysis. Cells that were not exposed to toxins served as the control (No toxin). SNAP-25 was detected as an internal control for loading of cell lysates. The cleavage of Syb by BoNT/D resulted in loss of Syb immunoblot signals. Stimulation of synaptic vesicle recycling with high K + increased the cleavage of Syb. In all the following experiments, high K + buffer was used to load toxins into neurons using the same procedures described here and cell lysates were subjected to immunoblot analysis, unless otherwise indicated in the Figure Legends. B) Neurons were exposed to BoNT/D (100 pM) with (+) or without (−) the presence of 1 µM BoNT/D-HCR. The presence of BoNT/D-HCR reduced the cleavage of Syb by BoNT/D. C) Neurons were exposed to BoNT/D-HCR (80 nM, 5 min) in either PBS or high K + buffer. Cells were washed, fixed, permeabilized, and subjected to immunostaining analysis. Binding of BoNT/D-HCR was detected using an anti-HA antibody. Synapsin was labeled as a marker for presynaptic terminals. High K + buffer increased the binding of BoNT/D-HCR to presynaptic terminals. The “Overlay” panel is enlarged from the center region of the “high K + ” sample, showing high degrees of co-localization between BoNT/D-HCR (green) and synapsin (red). The scale bars represent 20 µm in all figures. D) Neurons were pre-treated with TeNT (1 nM, 12 hrs in media) and then tested for the binding of BoNT/D-HCR as described in panel C. Control cells were not exposed to TeNT. Pre-treatment with TeNT prevented the binding of BoNT/D-HCR to neurons.
    Figure Legend Snippet: Stimulation of synaptic vesicle recycling increases the binding and entry of BoNT/D into neurons. A) Cultured rat hippocampal neurons were exposed to BoNT/D (100 pM, 5 min) in either resting condition (PBS) or stimulated conditions (high K + buffer: PBS with 56 mM KCl and 1 mM Ca 2+ ). Cells were washed and further incubated in toxin-free media for 6 hrs. Cell lysates were subjected to immunoblot analysis. Cells that were not exposed to toxins served as the control (No toxin). SNAP-25 was detected as an internal control for loading of cell lysates. The cleavage of Syb by BoNT/D resulted in loss of Syb immunoblot signals. Stimulation of synaptic vesicle recycling with high K + increased the cleavage of Syb. In all the following experiments, high K + buffer was used to load toxins into neurons using the same procedures described here and cell lysates were subjected to immunoblot analysis, unless otherwise indicated in the Figure Legends. B) Neurons were exposed to BoNT/D (100 pM) with (+) or without (−) the presence of 1 µM BoNT/D-HCR. The presence of BoNT/D-HCR reduced the cleavage of Syb by BoNT/D. C) Neurons were exposed to BoNT/D-HCR (80 nM, 5 min) in either PBS or high K + buffer. Cells were washed, fixed, permeabilized, and subjected to immunostaining analysis. Binding of BoNT/D-HCR was detected using an anti-HA antibody. Synapsin was labeled as a marker for presynaptic terminals. High K + buffer increased the binding of BoNT/D-HCR to presynaptic terminals. The “Overlay” panel is enlarged from the center region of the “high K + ” sample, showing high degrees of co-localization between BoNT/D-HCR (green) and synapsin (red). The scale bars represent 20 µm in all figures. D) Neurons were pre-treated with TeNT (1 nM, 12 hrs in media) and then tested for the binding of BoNT/D-HCR as described in panel C. Control cells were not exposed to TeNT. Pre-treatment with TeNT prevented the binding of BoNT/D-HCR to neurons.

    Techniques Used: Binding Assay, Cell Culture, Incubation, Immunostaining, Labeling, Marker

    12) Product Images from "Generation and characterization of novel recombinant anti-hERG1 scFv antibodies for cancer molecular imaging"

    Article Title: Generation and characterization of novel recombinant anti-hERG1 scFv antibodies for cancer molecular imaging

    Journal: Oncotarget

    doi: 10.18632/oncotarget.26200

    In vivo characterization of scFv-hERG1-Cys antibody in healthy mice ( A ) Serum stability of scFv-hERG1-Cys. Antibody concentration was determined by sandwich ELISA at different time points and is expressed as nanomolar concentration of the antibody. Values are means ± SD of two separate experiments. ( B ) Pharmacokinetics of scFv-hERG1-Cys. Immunodeficient nu/nu mice were injected i.v. with 160 μg of the antibody. Plasma was collected by tail vein puncture 5, 15, 30 min and 1, 2, 6, 24 and 48 h after scFv injection and the antibody concentration was determined by sandwich ELISA. Values are means ± SD of data collected in two different injected mice. ( C ) In vivo imaging of Alexa 750 labelled scFv-hERG1-Cys in healthy mice. Each panel shows the fluorescent signal in a mouse treated with scFv-hERG1Cys antibody conjugated with Alexa750 compared to a control mouse treated with PBS solution. Two mice were injected i.v. with 20 μg of antibodies, while one animal was injected with 10 μg. The fluorescent signal of the labeled scFv, was detected at different time points (5, 30, 60 minutes and 24 hours) from the administration. ( D ) Representative pictures of fluorescence analysis on dissected organs have been reported (pancreas, liver, kidneys and heart) collected after 24 hours from the injection of the scFv antibody. No fluorescent signal was detected, except for the kidneys, which showed a very weak fluorescent signal. Autofluorescence was subtracted based on the signal relative to WT non-injected mouse (Control). ( E ) ECG of a Control mice (upper panel) and a mouse treated with 20 μg of scFv (lower panel). The non-torsadogenic effect of the scDb was evalued considering no alterations were found either in the ECG trace and on ECG (Control mouse: QT interval = 34 ms, bpm = 380, QTc = 86. Treated mouse: QT interval = 36 ms; bpm = 372, QTc = 90 ms). No significant cardiac alterations were present. ( F ) Representative images of H E (Hematoxylin and eosin) staining performed on heart sections deriving from immunodeficient nude mice injected with scFv-hERG1-Cys-Alexa750 antibody showing no evident signs of citotoxicity. Left panels, Control. Right panels. Section derived from mice injected with scFv-hERG1-Cys-Alexa750. Scale bars, left panels, 100 μm. Scale bars, right panels, 50 μm.
    Figure Legend Snippet: In vivo characterization of scFv-hERG1-Cys antibody in healthy mice ( A ) Serum stability of scFv-hERG1-Cys. Antibody concentration was determined by sandwich ELISA at different time points and is expressed as nanomolar concentration of the antibody. Values are means ± SD of two separate experiments. ( B ) Pharmacokinetics of scFv-hERG1-Cys. Immunodeficient nu/nu mice were injected i.v. with 160 μg of the antibody. Plasma was collected by tail vein puncture 5, 15, 30 min and 1, 2, 6, 24 and 48 h after scFv injection and the antibody concentration was determined by sandwich ELISA. Values are means ± SD of data collected in two different injected mice. ( C ) In vivo imaging of Alexa 750 labelled scFv-hERG1-Cys in healthy mice. Each panel shows the fluorescent signal in a mouse treated with scFv-hERG1Cys antibody conjugated with Alexa750 compared to a control mouse treated with PBS solution. Two mice were injected i.v. with 20 μg of antibodies, while one animal was injected with 10 μg. The fluorescent signal of the labeled scFv, was detected at different time points (5, 30, 60 minutes and 24 hours) from the administration. ( D ) Representative pictures of fluorescence analysis on dissected organs have been reported (pancreas, liver, kidneys and heart) collected after 24 hours from the injection of the scFv antibody. No fluorescent signal was detected, except for the kidneys, which showed a very weak fluorescent signal. Autofluorescence was subtracted based on the signal relative to WT non-injected mouse (Control). ( E ) ECG of a Control mice (upper panel) and a mouse treated with 20 μg of scFv (lower panel). The non-torsadogenic effect of the scDb was evalued considering no alterations were found either in the ECG trace and on ECG (Control mouse: QT interval = 34 ms, bpm = 380, QTc = 86. Treated mouse: QT interval = 36 ms; bpm = 372, QTc = 90 ms). No significant cardiac alterations were present. ( F ) Representative images of H E (Hematoxylin and eosin) staining performed on heart sections deriving from immunodeficient nude mice injected with scFv-hERG1-Cys-Alexa750 antibody showing no evident signs of citotoxicity. Left panels, Control. Right panels. Section derived from mice injected with scFv-hERG1-Cys-Alexa750. Scale bars, left panels, 100 μm. Scale bars, right panels, 50 μm.

    Techniques Used: In Vivo, Mouse Assay, Concentration Assay, Sandwich ELISA, Injection, In Vivo Imaging, Labeling, Fluorescence, Mass Spectrometry, Staining, Derivative Assay

    Biochemical characterization of scFv-hERG1 and scFv-hERG1-Cys antibodies ( A ) Amino acid sequence of the scFv-hERG1-encoding cassette. The CDRs of the heavy and light chain, identified according to the Kabat scheme through the ANARCI software, are highlighted in green; the glycine-serine linker region is in bold. The arrow indicates the F (Phenylalanine) amino acid in position 92 (red), which was replaced by a C (Cystein), as reported in the line above. SDS-PAGE and Coomassie Brilliant blue staining performed on different fractions (Fr.) obtained after AKTA purification of scFv-hERG1 ( B ) and scFv-hERG1-Cys ( C ). After dialysis using Slide-A-Lyzer™ Dialysis Cassettes (Thermo Fisher, Massachusetts, USA) against PBS, scFv protein absorbance was measured at 280 nm and the Lambert-Beer equation was applied for antibody quantification. Size-Exclusion Chromatography (SEC) of scFv-hERG1 ( D ) and scFv-hERG1-Cys ( E ). According to the column used (Superdex 75, Ge Healthcare), proteins with a molecular weight around 30 KDa, such as scFv, should have a retention time of roughly 24–25 min. For the scFV-hERG1, the first peak, arbitrarily labelled as 1, corresponds to a retention time of 15 min and represents the aggregated form of the antibody; the second peak, arbitrarily labelled as 2, corresponds to a retention time of 24 min, and represents the scFv antibody; the third peak, arbitrarily labelled as 3, corresponds to 30–35 min retention time, and represents the degraded form of the protein. For the scFv-hERG1-Cys, a single peak is visible with retention time of nearly 24 min, corresponding to what expected for a scFv molecule.
    Figure Legend Snippet: Biochemical characterization of scFv-hERG1 and scFv-hERG1-Cys antibodies ( A ) Amino acid sequence of the scFv-hERG1-encoding cassette. The CDRs of the heavy and light chain, identified according to the Kabat scheme through the ANARCI software, are highlighted in green; the glycine-serine linker region is in bold. The arrow indicates the F (Phenylalanine) amino acid in position 92 (red), which was replaced by a C (Cystein), as reported in the line above. SDS-PAGE and Coomassie Brilliant blue staining performed on different fractions (Fr.) obtained after AKTA purification of scFv-hERG1 ( B ) and scFv-hERG1-Cys ( C ). After dialysis using Slide-A-Lyzer™ Dialysis Cassettes (Thermo Fisher, Massachusetts, USA) against PBS, scFv protein absorbance was measured at 280 nm and the Lambert-Beer equation was applied for antibody quantification. Size-Exclusion Chromatography (SEC) of scFv-hERG1 ( D ) and scFv-hERG1-Cys ( E ). According to the column used (Superdex 75, Ge Healthcare), proteins with a molecular weight around 30 KDa, such as scFv, should have a retention time of roughly 24–25 min. For the scFV-hERG1, the first peak, arbitrarily labelled as 1, corresponds to a retention time of 15 min and represents the aggregated form of the antibody; the second peak, arbitrarily labelled as 2, corresponds to a retention time of 24 min, and represents the scFv antibody; the third peak, arbitrarily labelled as 3, corresponds to 30–35 min retention time, and represents the degraded form of the protein. For the scFv-hERG1-Cys, a single peak is visible with retention time of nearly 24 min, corresponding to what expected for a scFv molecule.

    Techniques Used: Sequencing, Software, SDS Page, Staining, Purification, Size-exclusion Chromatography, Molecular Weight

    13) Product Images from "Simultaneous measurement of erythrocyte deformability and blood viscoelasticity using micropillars and co-flowing streams under pulsatile blood flows"

    Article Title: Simultaneous measurement of erythrocyte deformability and blood viscoelasticity using micropillars and co-flowing streams under pulsatile blood flows

    Journal: Biomicrofluidics

    doi: 10.1063/1.4973863

    Proposed method for quantification of the RBC deformability and blood viscoelasticity under pulsatile blood flows. (A) Schematic diagram of the proposed method including a disposable microfluidic device and two syringe pumps. (a) The microfluidic device has two inlets (A, B) and two outlets (A, B), two upper side channels, and two lower side channels connected to one bridge channel (BRG). To measure the deformability of RBC, the left-lower side channel has a deformability assessment chamber (DAC) with narrow-sized micropillars. Blood flow in the DAC is controlled by closing or opening a pinch valve connected to the end of outlet (A). To induce pulsatile blood flow in the microfluidic device, the blood is delivered into inlet (A) at a sinusoidal flow rate [ Q Blood = Q α + Q β sin (2πt/T)]. The PBS solution is supplied to inlet (B), at a constant flow-rate ( Q PBS = Q 0 ). (b) By opening the pinch valve (i.e., t
    Figure Legend Snippet: Proposed method for quantification of the RBC deformability and blood viscoelasticity under pulsatile blood flows. (A) Schematic diagram of the proposed method including a disposable microfluidic device and two syringe pumps. (a) The microfluidic device has two inlets (A, B) and two outlets (A, B), two upper side channels, and two lower side channels connected to one bridge channel (BRG). To measure the deformability of RBC, the left-lower side channel has a deformability assessment chamber (DAC) with narrow-sized micropillars. Blood flow in the DAC is controlled by closing or opening a pinch valve connected to the end of outlet (A). To induce pulsatile blood flow in the microfluidic device, the blood is delivered into inlet (A) at a sinusoidal flow rate [ Q Blood = Q α + Q β sin (2πt/T)]. The PBS solution is supplied to inlet (B), at a constant flow-rate ( Q PBS = Q 0 ). (b) By opening the pinch valve (i.e., t

    Techniques Used: Flow Cytometry

    14) Product Images from "Differential effects of extracellular ATP on chloride transport in cortical collecting duct cells"

    Article Title: Differential effects of extracellular ATP on chloride transport in cortical collecting duct cells

    Journal: American Journal of Physiology - Renal Physiology

    doi: 10.1152/ajprenal.00062.2012

    Arginine vasopressin (AVP) increases ATP concentration at the apical membrane of mpkCCD c14 cells. Media from the apical side of cell monolayers were replaced with PBS. Vehicle control or AVP (10 −9 M) was added to the basal side of cell monolayers.
    Figure Legend Snippet: Arginine vasopressin (AVP) increases ATP concentration at the apical membrane of mpkCCD c14 cells. Media from the apical side of cell monolayers were replaced with PBS. Vehicle control or AVP (10 −9 M) was added to the basal side of cell monolayers.

    Techniques Used: Concentration Assay

    15) Product Images from "Microfluidic-Based Technique for Measuring RBC Aggregation and Blood Viscosity in a Continuous and Simultaneous Fashion"

    Article Title: Microfluidic-Based Technique for Measuring RBC Aggregation and Blood Viscosity in a Continuous and Simultaneous Fashion

    Journal: Micromachines

    doi: 10.3390/mi9090467

    Quantitative evaluations of RBC aggregation index and blood viscosity under pulsatile blood flow conditions (Q max = 0.5 mL/h, Q min = 0.2 mL/h, and period (T)). Blood and PBS solution were periodically supplied into the microfluidic device, at the same flow rate. ( A ) Quantitative evaluation of the effect of period (T) on RBC aggregation index and blood viscosity for blood (Hct = 50%). Blood (Hct = 50%) was prepared by adding normal RBCs into specific concentration of dextran solution (C dextran = 10 mg/mL). (a) Variations of
    Figure Legend Snippet: Quantitative evaluations of RBC aggregation index and blood viscosity under pulsatile blood flow conditions (Q max = 0.5 mL/h, Q min = 0.2 mL/h, and period (T)). Blood and PBS solution were periodically supplied into the microfluidic device, at the same flow rate. ( A ) Quantitative evaluation of the effect of period (T) on RBC aggregation index and blood viscosity for blood (Hct = 50%). Blood (Hct = 50%) was prepared by adding normal RBCs into specific concentration of dextran solution (C dextran = 10 mg/mL). (a) Variations of

    Techniques Used: Flow Cytometry, Concentration Assay

    Quantitative evaluations of RBC aggregation index (AI PM ) under constant blood flow. Blood (Hct = 50%) was prepared by adding normal RBCs into various concentrations of dextran solution (C dextran ) (C dextran = 0 mg/mL, 5 mg/mL, 10 mg/mL, and 15 mg/mL). Blood and PBS solution were delivered into the microfluidic device at the same flow rate (Q PBS = Q Blood = Q) (Q = 0.1 mL/h, 0.2 mL/h, 0.3 mL/h, 0.4 mL/h, and 0.5 mL/h). ( A ) Variations of RBC aggregation with respect to C dextran and Q. (a) Microscopic images for representing RBC aggregation of blood (RBCs suspended in dextran solution of C dextran = 5 mg/mL) with respect to Q. (b) Microscopic images for representing RBC aggregation of blood (RBCs suspended in dextran solution (C dextran = 15 mg/mL)) with respect to Q. (c) Variations of
    Figure Legend Snippet: Quantitative evaluations of RBC aggregation index (AI PM ) under constant blood flow. Blood (Hct = 50%) was prepared by adding normal RBCs into various concentrations of dextran solution (C dextran ) (C dextran = 0 mg/mL, 5 mg/mL, 10 mg/mL, and 15 mg/mL). Blood and PBS solution were delivered into the microfluidic device at the same flow rate (Q PBS = Q Blood = Q) (Q = 0.1 mL/h, 0.2 mL/h, 0.3 mL/h, 0.4 mL/h, and 0.5 mL/h). ( A ) Variations of RBC aggregation with respect to C dextran and Q. (a) Microscopic images for representing RBC aggregation of blood (RBCs suspended in dextran solution of C dextran = 5 mg/mL) with respect to Q. (b) Microscopic images for representing RBC aggregation of blood (RBCs suspended in dextran solution (C dextran = 15 mg/mL)) with respect to Q. (c) Variations of

    Techniques Used: Flow Cytometry

    16) Product Images from "Generation and characterization of novel recombinant anti-hERG1 scFv antibodies for cancer molecular imaging"

    Article Title: Generation and characterization of novel recombinant anti-hERG1 scFv antibodies for cancer molecular imaging

    Journal: Oncotarget

    doi: 10.18632/oncotarget.26200

    Biochemical characterization of scFv-hERG1 and scFv-hERG1-Cys antibodies ( A ) Amino acid sequence of the scFv-hERG1-encoding cassette. The CDRs of the heavy and light chain, identified according to the Kabat scheme through the ANARCI software, are highlighted in green; the glycine-serine linker region is in bold. The arrow indicates the F (Phenylalanine) amino acid in position 92 (red), which was replaced by a C (Cystein), as reported in the line above. SDS-PAGE and Coomassie Brilliant blue staining performed on different fractions (Fr.) obtained after AKTA purification of scFv-hERG1 ( B ) and scFv-hERG1-Cys ( C ). After dialysis using Slide-A-Lyzer™ Dialysis Cassettes (Thermo Fisher, Massachusetts, USA) against PBS, scFv protein absorbance was measured at 280 nm and the Lambert-Beer equation was applied for antibody quantification. Size-Exclusion Chromatography (SEC) of scFv-hERG1 ( D ) and scFv-hERG1-Cys ( E ). According to the column used (Superdex 75, Ge Healthcare), proteins with a molecular weight around 30 KDa, such as scFv, should have a retention time of roughly 24–25 min. For the scFV-hERG1, the first peak, arbitrarily labelled as 1, corresponds to a retention time of 15 min and represents the aggregated form of the antibody; the second peak, arbitrarily labelled as 2, corresponds to a retention time of 24 min, and represents the scFv antibody; the third peak, arbitrarily labelled as 3, corresponds to 30–35 min retention time, and represents the degraded form of the protein. For the scFv-hERG1-Cys, a single peak is visible with retention time of nearly 24 min, corresponding to what expected for a scFv molecule.
    Figure Legend Snippet: Biochemical characterization of scFv-hERG1 and scFv-hERG1-Cys antibodies ( A ) Amino acid sequence of the scFv-hERG1-encoding cassette. The CDRs of the heavy and light chain, identified according to the Kabat scheme through the ANARCI software, are highlighted in green; the glycine-serine linker region is in bold. The arrow indicates the F (Phenylalanine) amino acid in position 92 (red), which was replaced by a C (Cystein), as reported in the line above. SDS-PAGE and Coomassie Brilliant blue staining performed on different fractions (Fr.) obtained after AKTA purification of scFv-hERG1 ( B ) and scFv-hERG1-Cys ( C ). After dialysis using Slide-A-Lyzer™ Dialysis Cassettes (Thermo Fisher, Massachusetts, USA) against PBS, scFv protein absorbance was measured at 280 nm and the Lambert-Beer equation was applied for antibody quantification. Size-Exclusion Chromatography (SEC) of scFv-hERG1 ( D ) and scFv-hERG1-Cys ( E ). According to the column used (Superdex 75, Ge Healthcare), proteins with a molecular weight around 30 KDa, such as scFv, should have a retention time of roughly 24–25 min. For the scFV-hERG1, the first peak, arbitrarily labelled as 1, corresponds to a retention time of 15 min and represents the aggregated form of the antibody; the second peak, arbitrarily labelled as 2, corresponds to a retention time of 24 min, and represents the scFv antibody; the third peak, arbitrarily labelled as 3, corresponds to 30–35 min retention time, and represents the degraded form of the protein. For the scFv-hERG1-Cys, a single peak is visible with retention time of nearly 24 min, corresponding to what expected for a scFv molecule.

    Techniques Used: Sequencing, Software, SDS Page, Staining, Purification, Size-exclusion Chromatography, Molecular Weight

    Related Articles

    Immunocytochemistry:

    Article Title: Adenosine A1 receptor-mediated presynaptic inhibition at the calyx of Held of immature rats
    Article Snippet: .. The sections were then processed for immunocytochemistry as follows: (i) blocking in 0.1 m sodium phosphate buffer containing 4 % skimmed milk and 0.4 % Triton X-100 overnight at 4 °C, (ii) application of primary antibodies in 20 m m sodium phosphate buffer solution containing 300 m m NaCl, 1 % bovine serum albumin and 0.02 % Triton X-100 for 2 days at 4 °C, (iii) application of secondary antibodies in phosphate-buffer saline solution (PBS) for 2 days at 4 °C, (iv) mounting with ProLong antifade kit (Molecular Probes). .. Adenosine receptors were visualized with rabbit anti-adenosine A1 receptor antibodies (Affinity bioreagents, Golden, CO, USA, diluted 1:100).

    Blocking Assay:

    Article Title: Adenosine A1 receptor-mediated presynaptic inhibition at the calyx of Held of immature rats
    Article Snippet: .. The sections were then processed for immunocytochemistry as follows: (i) blocking in 0.1 m sodium phosphate buffer containing 4 % skimmed milk and 0.4 % Triton X-100 overnight at 4 °C, (ii) application of primary antibodies in 20 m m sodium phosphate buffer solution containing 300 m m NaCl, 1 % bovine serum albumin and 0.02 % Triton X-100 for 2 days at 4 °C, (iii) application of secondary antibodies in phosphate-buffer saline solution (PBS) for 2 days at 4 °C, (iv) mounting with ProLong antifade kit (Molecular Probes). .. Adenosine receptors were visualized with rabbit anti-adenosine A1 receptor antibodies (Affinity bioreagents, Golden, CO, USA, diluted 1:100).

    Concentration Assay:

    Article Title: Fast characterisation of cell-derived extracellular vesicles by nanoparticles tracking analysis, cryo-electron microscopy, and Raman tweezers microspectroscopy
    Article Snippet: .. EVs, present in the 12,000×g pellet, are resuspended in a phosphate-buffered solution (PBS) [pH 7.4 without calcium and magnesium (Gibco)], with a 20 to 100 volume concentration factor (X), relative to the volume of the 2,000×g supernatant. .. The 700×g and 2,000×g centrifugations are performed in single-use 15 ml tubes on an Eppendorf 5804R centrifuge.

    Article Title: The Inorganic Side of NGF: Copper(II) and Zinc(II) Affect the NGF Mimicking Signaling of the N-Terminus Peptides Encompassing the Recognition Domain of TrkA Receptor
    Article Snippet: .. After that, cells were rinsed (2 × 1mL) with phosphate buffer saline solution (PBS, 10 mM, pH = 7.4 at 25°C) and stained by 15 min incubation with CS1 intracellular monovalent copper probe (final concentration of 2 μM from 1 mM stock solution in DMSO) and the cell-permeant nuclear counterstain Hoechst 33342 (NucBlue® Live ReadyProbes® Reagent, Life Technologies), followed by buffer rinsing (2 × 1 mL). .. In two parallel experiments, before the treatments with the peptide NGF(1–14) and Ac-NGF(1–14), cells were pre-incubated in the medium supplemented with 50 μM of copper chelator BCS (bathocuproine disulfonic acid disodium salt, purchased from Sigma Aldrich, from a 10 mM stock solution in DMSO) for 3 h or 100 μM of CuSO4 for 1 h. A 0.5% (v/v) DMSO was added in all conditions as control.

    Incubation:

    Article Title: The Inorganic Side of NGF: Copper(II) and Zinc(II) Affect the NGF Mimicking Signaling of the N-Terminus Peptides Encompassing the Recognition Domain of TrkA Receptor
    Article Snippet: .. After that, cells were rinsed (2 × 1mL) with phosphate buffer saline solution (PBS, 10 mM, pH = 7.4 at 25°C) and stained by 15 min incubation with CS1 intracellular monovalent copper probe (final concentration of 2 μM from 1 mM stock solution in DMSO) and the cell-permeant nuclear counterstain Hoechst 33342 (NucBlue® Live ReadyProbes® Reagent, Life Technologies), followed by buffer rinsing (2 × 1 mL). .. In two parallel experiments, before the treatments with the peptide NGF(1–14) and Ac-NGF(1–14), cells were pre-incubated in the medium supplemented with 50 μM of copper chelator BCS (bathocuproine disulfonic acid disodium salt, purchased from Sigma Aldrich, from a 10 mM stock solution in DMSO) for 3 h or 100 μM of CuSO4 for 1 h. A 0.5% (v/v) DMSO was added in all conditions as control.

    Infection:

    Article Title: Detection and characterization of a novel marine birnavirus isolated from Asian seabass in Singapore
    Article Snippet: .. Two days after infection, infected cells were pelleted in 1X phosphate buffered solution (PBS) (Invitrogen, USA) and fixed with 4% paraformaldehyde. ..

    Staining:

    Article Title: The Inorganic Side of NGF: Copper(II) and Zinc(II) Affect the NGF Mimicking Signaling of the N-Terminus Peptides Encompassing the Recognition Domain of TrkA Receptor
    Article Snippet: .. After that, cells were rinsed (2 × 1mL) with phosphate buffer saline solution (PBS, 10 mM, pH = 7.4 at 25°C) and stained by 15 min incubation with CS1 intracellular monovalent copper probe (final concentration of 2 μM from 1 mM stock solution in DMSO) and the cell-permeant nuclear counterstain Hoechst 33342 (NucBlue® Live ReadyProbes® Reagent, Life Technologies), followed by buffer rinsing (2 × 1 mL). .. In two parallel experiments, before the treatments with the peptide NGF(1–14) and Ac-NGF(1–14), cells were pre-incubated in the medium supplemented with 50 μM of copper chelator BCS (bathocuproine disulfonic acid disodium salt, purchased from Sigma Aldrich, from a 10 mM stock solution in DMSO) for 3 h or 100 μM of CuSO4 for 1 h. A 0.5% (v/v) DMSO was added in all conditions as control.

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93
    Thermo Fisher pbs casein solution
    Humoral and cellular immune responses of the mice from the prophylactic bioassay utilizing the oral cancer orthotopic model consisting of C3H/He mice challenged with the AT-84 E7 Luc cell line. Groups of five female C3H/He mice were immunized with one of the following treatments: 100 μ g of KLH or FLH, 50 μ g of KLH or FLH plus 10 μ g of QS-21, and 10 μ g of QS-21 or 100 μ l of <t>PBS.</t> At 10 and 25 days, serum samples were taken to determine the titers of <t>IgG</t> subclasses by indirect ELISA. DTH determination was performed on day 15 of the bioassay. (a) Total anti-hemocyanin IgG titers in mouse sera. Data are shown as means ± SEM. Anti-hemocyanin IgG titers for each hemocyanin alone were compared by one-way ANOVA with the same hemocyanin in combination with QS-21 at day 10 and at day 21. ∗∗∗∗ P
    Pbs Casein Solution, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pbs casein solution/product/Thermo Fisher
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pbs casein solution - by Bioz Stars, 2020-08
    93/100 stars
      Buy from Supplier

    94
    Thermo Fisher pbs solution
    Confocal micrographs showing the uptake by MCs of C6-LP ( A ), 6%-TRX-C6-LP ( B ), 11%-TRX-C6-LP ( C ), and 14%-TRX-C6-LP ( D ) after 24 h incubation (C6: green). Notes: MCs were incubated with C6-LP (control) or TRX-C6-LPs at a lipid concentration of 0.8 mg/mL for 2 h in serum-free RPMI 1640 at <t>37°C</t> and then washed with <t>PBS</t> to terminate the uptake process. After fixation in 10% neutral buffer formalin, the cells were counterstained with DAPI (blue) for observation under a laser confocal microscope. Magnification ×400. Abbreviations: C6, Coumarin-6; C6-LP, Coumarin-6-loaded liposomes; DAPI, dihydrochloride; MCs, mesangial cells; PBS, phosphate-buffered saline; TRX-C6-LP, TRX-20-modified Coumarin-6-loaded liposomes.
    Pbs Solution, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 369 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pbs solution/product/Thermo Fisher
    Average 94 stars, based on 369 article reviews
    Price from $9.99 to $1999.99
    pbs solution - by Bioz Stars, 2020-08
    94/100 stars
      Buy from Supplier

    Image Search Results


    Humoral and cellular immune responses of the mice from the prophylactic bioassay utilizing the oral cancer orthotopic model consisting of C3H/He mice challenged with the AT-84 E7 Luc cell line. Groups of five female C3H/He mice were immunized with one of the following treatments: 100 μ g of KLH or FLH, 50 μ g of KLH or FLH plus 10 μ g of QS-21, and 10 μ g of QS-21 or 100 μ l of PBS. At 10 and 25 days, serum samples were taken to determine the titers of IgG subclasses by indirect ELISA. DTH determination was performed on day 15 of the bioassay. (a) Total anti-hemocyanin IgG titers in mouse sera. Data are shown as means ± SEM. Anti-hemocyanin IgG titers for each hemocyanin alone were compared by one-way ANOVA with the same hemocyanin in combination with QS-21 at day 10 and at day 21. ∗∗∗∗ P

    Journal: Journal of Immunology Research

    Article Title: Immunotherapeutic Potential of Mollusk Hemocyanins in Combination with Human Vaccine Adjuvants in Murine Models of Oral Cancer

    doi: 10.1155/2019/7076942

    Figure Lengend Snippet: Humoral and cellular immune responses of the mice from the prophylactic bioassay utilizing the oral cancer orthotopic model consisting of C3H/He mice challenged with the AT-84 E7 Luc cell line. Groups of five female C3H/He mice were immunized with one of the following treatments: 100 μ g of KLH or FLH, 50 μ g of KLH or FLH plus 10 μ g of QS-21, and 10 μ g of QS-21 or 100 μ l of PBS. At 10 and 25 days, serum samples were taken to determine the titers of IgG subclasses by indirect ELISA. DTH determination was performed on day 15 of the bioassay. (a) Total anti-hemocyanin IgG titers in mouse sera. Data are shown as means ± SEM. Anti-hemocyanin IgG titers for each hemocyanin alone were compared by one-way ANOVA with the same hemocyanin in combination with QS-21 at day 10 and at day 21. ∗∗∗∗ P

    Article Snippet: Subsequently, 100 μ l of a 1% PBS-casein solution containing goat anti-mouse IgG (H + L) serum labeled with alkaline phosphatase (ALP; Thermo Scientific) was added at a 1 : 2500 dilution and incubated for 30 minutes at 37°C.

    Techniques: Mouse Assay, Indirect ELISA

    Specific humoral and cellular immune responses in C57BL/6 mice immunized with hemocyanins in combination with adjuvants. Groups of three female C57BL/6 mice were immunized subcutaneously on days 1 and 16 with one of the following treatments: 50 μ g of KLH, CCH, or FLH alone or in combination with 100 μ g of alum or 10 μ g of QS-21 in a 1 : 1 (vol/vol) ratio with AddaVax, all in a total volume of 100 μ l of PBS (vehicle). A serum sample was taken from each animal on day 37 after the second immunization for analysis by indirect ELISA. (a) Total anti-hemocyanin IgG titers in mouse sera. Values are presented as means ± SEM. The anti-hemocyanin IgG titers for each hemocyanin alone were compared by one-way ANOVA with the same hemocyanin in combination with an adjuvant. ∗∗∗∗ P

    Journal: Journal of Immunology Research

    Article Title: Immunotherapeutic Potential of Mollusk Hemocyanins in Combination with Human Vaccine Adjuvants in Murine Models of Oral Cancer

    doi: 10.1155/2019/7076942

    Figure Lengend Snippet: Specific humoral and cellular immune responses in C57BL/6 mice immunized with hemocyanins in combination with adjuvants. Groups of three female C57BL/6 mice were immunized subcutaneously on days 1 and 16 with one of the following treatments: 50 μ g of KLH, CCH, or FLH alone or in combination with 100 μ g of alum or 10 μ g of QS-21 in a 1 : 1 (vol/vol) ratio with AddaVax, all in a total volume of 100 μ l of PBS (vehicle). A serum sample was taken from each animal on day 37 after the second immunization for analysis by indirect ELISA. (a) Total anti-hemocyanin IgG titers in mouse sera. Values are presented as means ± SEM. The anti-hemocyanin IgG titers for each hemocyanin alone were compared by one-way ANOVA with the same hemocyanin in combination with an adjuvant. ∗∗∗∗ P

    Article Snippet: Subsequently, 100 μ l of a 1% PBS-casein solution containing goat anti-mouse IgG (H + L) serum labeled with alkaline phosphatase (ALP; Thermo Scientific) was added at a 1 : 2500 dilution and incubated for 30 minutes at 37°C.

    Techniques: Mouse Assay, Indirect ELISA

    Confocal micrographs showing the uptake by MCs of C6-LP ( A ), 6%-TRX-C6-LP ( B ), 11%-TRX-C6-LP ( C ), and 14%-TRX-C6-LP ( D ) after 24 h incubation (C6: green). Notes: MCs were incubated with C6-LP (control) or TRX-C6-LPs at a lipid concentration of 0.8 mg/mL for 2 h in serum-free RPMI 1640 at 37°C and then washed with PBS to terminate the uptake process. After fixation in 10% neutral buffer formalin, the cells were counterstained with DAPI (blue) for observation under a laser confocal microscope. Magnification ×400. Abbreviations: C6, Coumarin-6; C6-LP, Coumarin-6-loaded liposomes; DAPI, dihydrochloride; MCs, mesangial cells; PBS, phosphate-buffered saline; TRX-C6-LP, TRX-20-modified Coumarin-6-loaded liposomes.

    Journal: International Journal of Nanomedicine

    Article Title: Renal-targeted delivery of triptolide by entrapment in pegylated TRX-20-modified liposomes

    doi: 10.2147/IJN.S141095

    Figure Lengend Snippet: Confocal micrographs showing the uptake by MCs of C6-LP ( A ), 6%-TRX-C6-LP ( B ), 11%-TRX-C6-LP ( C ), and 14%-TRX-C6-LP ( D ) after 24 h incubation (C6: green). Notes: MCs were incubated with C6-LP (control) or TRX-C6-LPs at a lipid concentration of 0.8 mg/mL for 2 h in serum-free RPMI 1640 at 37°C and then washed with PBS to terminate the uptake process. After fixation in 10% neutral buffer formalin, the cells were counterstained with DAPI (blue) for observation under a laser confocal microscope. Magnification ×400. Abbreviations: C6, Coumarin-6; C6-LP, Coumarin-6-loaded liposomes; DAPI, dihydrochloride; MCs, mesangial cells; PBS, phosphate-buffered saline; TRX-C6-LP, TRX-20-modified Coumarin-6-loaded liposomes.

    Article Snippet: After enzymatic digestions with collagenase IV (0.1% w/v) at 37°C in PBS solution for 20–45 min, the MC suspensions were obtained and cultured in RPMI 1640 medium containing 20% heat-inactivated fetal bovine serum, 2 μg/mL insulin, 300 μg/L transferrin, 100 U/mL penicillin, and 100 U/mL streptomycin at 37°C in a humidified 5% (v/v) CO2 incubator (Thermo Scientific, Marietta, OH, USA).

    Techniques: Incubation, Concentration Assay, Microscopy, Modification

    A. Live animal imaging after intravaginal instillation of CL 40 DMPC 60 liposomes encapsulating Dylight 649 (20 mg/mL) or PBS (middle animal in each image) at various time points . B. Quantification of radiant efficiency at each time point around the region of interest. Data are means ± SD with n = 8 in each group

    Journal: Biomaterials

    Article Title: Liposomes for HIV prophylaxis

    doi: 10.1016/j.biomaterials.2011.07.068

    Figure Lengend Snippet: A. Live animal imaging after intravaginal instillation of CL 40 DMPC 60 liposomes encapsulating Dylight 649 (20 mg/mL) or PBS (middle animal in each image) at various time points . B. Quantification of radiant efficiency at each time point around the region of interest. Data are means ± SD with n = 8 in each group

    Article Snippet: The PBS solution contained non-reactive DyLight 649 free acid dye (ThermoFisher, Rockford, IL) that has an excitation of 682 nm and emission of 712 nm.

    Techniques: Imaging