bovine serum albumin bsa  (Millipore)


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    Bovine Serum Albumin
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    Millipore bovine serum albumin bsa
    Bovine Serum Albumin

    https://www.bioz.com/result/bovine serum albumin bsa/product/Millipore
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    bovine serum albumin bsa - by Bioz Stars, 2020-09
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    Images

    1) Product Images from "Immune exclusion by naturally acquired secretory IgA against pneumococcal pilus-1"

    Article Title: Immune exclusion by naturally acquired secretory IgA against pneumococcal pilus-1

    Journal: The Journal of Clinical Investigation

    doi: 10.1172/JCI132005

    Pilus-1 component RrgB mediates pneumococcal adherence and binding to sIgA. ( A ) Adherence of WT Spn and isogenic mutants deficient for 1 or 2 pilus-1 components to hNF was assessed in a solid-phase assay. Each bacteria (2 × 10 4 per 100 μL DMEM) were incubated with 10 μg hNF in the presence of 0.1% BSA for 2 hours at 30°C. Bound bacteria were determined by resuspension with 0.001% Triton X-100 following plating on TS agar plates supplemented with 200 μg/mL streptomycin. n = 5–18. ( B ) Flow cytometric analysis of sIgA binding by WT Spn and isogenic mutants in soluble hNF. Bacteria (5 × 10 6 CFU per 50 μL) were incubated with 50 μg/mL of hNF. Binding of surface-associated sIgA was analyzed using a FITC-labeled goat anti-human IgA1 antibody and is shown as the percentage binding. n = 6. ( A and B ) Results of at least 3 independent experiments are illustrated as mean values ± SD. * P
    Figure Legend Snippet: Pilus-1 component RrgB mediates pneumococcal adherence and binding to sIgA. ( A ) Adherence of WT Spn and isogenic mutants deficient for 1 or 2 pilus-1 components to hNF was assessed in a solid-phase assay. Each bacteria (2 × 10 4 per 100 μL DMEM) were incubated with 10 μg hNF in the presence of 0.1% BSA for 2 hours at 30°C. Bound bacteria were determined by resuspension with 0.001% Triton X-100 following plating on TS agar plates supplemented with 200 μg/mL streptomycin. n = 5–18. ( B ) Flow cytometric analysis of sIgA binding by WT Spn and isogenic mutants in soluble hNF. Bacteria (5 × 10 6 CFU per 50 μL) were incubated with 50 μg/mL of hNF. Binding of surface-associated sIgA was analyzed using a FITC-labeled goat anti-human IgA1 antibody and is shown as the percentage binding. n = 6. ( A and B ) Results of at least 3 independent experiments are illustrated as mean values ± SD. * P

    Techniques Used: Binding Assay, Incubation, Labeling

    Secretory IgA is necessary but not sufficient for pneumococcal adherence to hNF. ( A ) Adherence of Spn TIGR4 and isogenic pilus-1–deficient mutant to hNF from 6 individual donors was assessed in a solid-phase assay. Bacteria (2 × 10 4 per 100 μL DMEM) were incubated with 10 μg immobilized hNF in the presence of 0.1% BSA for 2 hours at 30°C. n = 6. ( B ) Anti-RrgB IgA was determined using an ELISA. Recombinant purified RrgB protein was immobilized in a microtiter plate (Immulon 2HB, Thermo Fisher Scientific) and, after blocking, incubated with 200 μg/mL hNF, or 25 μg/mL sIgA and serum IgA, respectively. Binding of RrgB-specific IgA was detected using a biotin-labeled anti-human IgA and peroxidase-coupled streptavidin. The values of control wells without hNF or sIgA were subtracted from each measured value. Results are illustrated as mean values ± SD of 2 independent experiments; n = 4. ( C ) Inhibition adherence assay using purified sIgA in increasing concentrations or purified serum IgA in a 2-fold molar ratio (compared with 50 μg/mL sIgA). Bacteria were pretreated with either sIgA or serum IgA for 30 minutes at 37°C before incubation with immobilized pooled hNF for 2 hours at 30°C. n = 6. ( D ) Binding of WT Spn to immobilized sIgA or BSA. Secretory IgA and BSA (each 10 μg) were immobilized overnight followed by blocking with 0.1% BSA and incubation with 2 × 10 4 per 100 μL bacteria for 2 hours at 30°C. n = 6. ( A – C ) Experiments were performed in duplicate, and mean values of 3 independent experiments are shown with error bars corresponding to SD. ** P
    Figure Legend Snippet: Secretory IgA is necessary but not sufficient for pneumococcal adherence to hNF. ( A ) Adherence of Spn TIGR4 and isogenic pilus-1–deficient mutant to hNF from 6 individual donors was assessed in a solid-phase assay. Bacteria (2 × 10 4 per 100 μL DMEM) were incubated with 10 μg immobilized hNF in the presence of 0.1% BSA for 2 hours at 30°C. n = 6. ( B ) Anti-RrgB IgA was determined using an ELISA. Recombinant purified RrgB protein was immobilized in a microtiter plate (Immulon 2HB, Thermo Fisher Scientific) and, after blocking, incubated with 200 μg/mL hNF, or 25 μg/mL sIgA and serum IgA, respectively. Binding of RrgB-specific IgA was detected using a biotin-labeled anti-human IgA and peroxidase-coupled streptavidin. The values of control wells without hNF or sIgA were subtracted from each measured value. Results are illustrated as mean values ± SD of 2 independent experiments; n = 4. ( C ) Inhibition adherence assay using purified sIgA in increasing concentrations or purified serum IgA in a 2-fold molar ratio (compared with 50 μg/mL sIgA). Bacteria were pretreated with either sIgA or serum IgA for 30 minutes at 37°C before incubation with immobilized pooled hNF for 2 hours at 30°C. n = 6. ( D ) Binding of WT Spn to immobilized sIgA or BSA. Secretory IgA and BSA (each 10 μg) were immobilized overnight followed by blocking with 0.1% BSA and incubation with 2 × 10 4 per 100 μL bacteria for 2 hours at 30°C. n = 6. ( A – C ) Experiments were performed in duplicate, and mean values of 3 independent experiments are shown with error bars corresponding to SD. ** P

    Techniques Used: Mutagenesis, Incubation, Enzyme-linked Immunosorbent Assay, Recombinant, Purification, Blocking Assay, Binding Assay, Labeling, Inhibition

    2) Product Images from "Dietary ω-6 polyunsaturated fatty acid arachidonic acid increases inflammation, but inhibits ECM protein expression in COPD"

    Article Title: Dietary ω-6 polyunsaturated fatty acid arachidonic acid increases inflammation, but inhibits ECM protein expression in COPD

    Journal: Respiratory Research

    doi: 10.1186/s12931-018-0919-4

    Dexamethasone suppresses AA-induced cytokine release in COPD and non-COPD. Pulmonary fibroblasts from COPD ( n = 3) and non-COPD ( n = 6) patients were pre-treated with dexamethasone (0.001 - 1 μM) for 60 min prior to challenge with AA (100 μM) in 0.1% BSA-DMEM for 48 h. Cell free supernatants were collected and CXCL8 ( a ) and IL-6 ( b ) release was measured using ELISA. All data are expressed as % of AA-induced cytokine release ± standard error of the mean. Two-way ANOVA with Bonferroni post-hoc testing was used to determine statistical significance. There were no statistical differences
    Figure Legend Snippet: Dexamethasone suppresses AA-induced cytokine release in COPD and non-COPD. Pulmonary fibroblasts from COPD ( n = 3) and non-COPD ( n = 6) patients were pre-treated with dexamethasone (0.001 - 1 μM) for 60 min prior to challenge with AA (100 μM) in 0.1% BSA-DMEM for 48 h. Cell free supernatants were collected and CXCL8 ( a ) and IL-6 ( b ) release was measured using ELISA. All data are expressed as % of AA-induced cytokine release ± standard error of the mean. Two-way ANOVA with Bonferroni post-hoc testing was used to determine statistical significance. There were no statistical differences

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reduced basal fibronectin, type I collagen, tenascin and perlecan deposition upon arachidonic acid challenge. Pulmonary fibroblasts from COPD ( n = 5–6 ) and non-COPD patients ( n = 4–5 ) were unstimulated (control) or challenged with the ω-6 PUFA arachidonic acid (AA) in 0.1% BSA-DMEM (100 μM) for 72 h. Deposition of fibronectin ( a ), type I collagen ( b ), tenascin ( c ) and perlecan ( d ) into the extracellular matrix (ECM) was measured by ECM ELISA. All data are expressed at fold change compared to control ± standard error of the mean. Challenge with AA is compared to control using a Two-way ANOVA with LSD fisher’s test. Significance is represented as * ( p
    Figure Legend Snippet: Reduced basal fibronectin, type I collagen, tenascin and perlecan deposition upon arachidonic acid challenge. Pulmonary fibroblasts from COPD ( n = 5–6 ) and non-COPD patients ( n = 4–5 ) were unstimulated (control) or challenged with the ω-6 PUFA arachidonic acid (AA) in 0.1% BSA-DMEM (100 μM) for 72 h. Deposition of fibronectin ( a ), type I collagen ( b ), tenascin ( c ) and perlecan ( d ) into the extracellular matrix (ECM) was measured by ECM ELISA. All data are expressed at fold change compared to control ± standard error of the mean. Challenge with AA is compared to control using a Two-way ANOVA with LSD fisher’s test. Significance is represented as * ( p

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reduced basal fibronectin and type I collagen expression upon arachidonic acid challenge. Pulmonary fibroblasts from COPD patients ( n = 5 ) and non-COPD ( n = 3–4 ) were unstimulated (control) or challenged with the ω-6 PUFA arachidonic acid (AA) in 0.1% BSA-DMEM (10 and 100 μM) for 48 h. Total RNA was collected and fibronectin ( a ), Type I collagen (1A2) ( b ) and tenascin ( c ) were detected using real time PCR array. The results are normalized to the endogenous control (18S rRNA), and presented as fold change from control ± standard error of the mean. Challenge with AA is compared to control using a Two-way ANOVA with LSD fisher’s test. Significance is represented as * ( p
    Figure Legend Snippet: Reduced basal fibronectin and type I collagen expression upon arachidonic acid challenge. Pulmonary fibroblasts from COPD patients ( n = 5 ) and non-COPD ( n = 3–4 ) were unstimulated (control) or challenged with the ω-6 PUFA arachidonic acid (AA) in 0.1% BSA-DMEM (10 and 100 μM) for 48 h. Total RNA was collected and fibronectin ( a ), Type I collagen (1A2) ( b ) and tenascin ( c ) were detected using real time PCR array. The results are normalized to the endogenous control (18S rRNA), and presented as fold change from control ± standard error of the mean. Challenge with AA is compared to control using a Two-way ANOVA with LSD fisher’s test. Significance is represented as * ( p

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    Reduced cytokine release upon arachidonic acid challenge in COPD versus non-COPD. Pulmonary fibroblasts from COPD ( n = 11–19) and non-COPD patients ( n = 12–36 ) were unstimulated (control) or challenged with ω-6 PUFA arachidonic acid (AA) in 0.1% BSA-DMEM (10 and 100 μM) for 48 h. Cell free supernatants were collected and CXCL8 ( a ), IL-6 ( b ) and PGE2 ( c ) release was measured using ELISA or enzyme immunoassay. Other cells from COPD ( n = 6–7) and non-COPD ( n = 6–7) patients were pre-treated with indomethacin (1 μM) ( d, e ) or celecoxib (0.01-1 μM) ( f, g ) for 60 min prior to challenge with AA (100 μM) in 0.1% BSA-DMEM for 48 h. Cell free supernatants were collected and CXCL8 ( d, f ) and IL-6 ( e, g ) release was measured using ELISA. Data are expressed as mean ± standard error of the mean ( a-c ) or as % of AA-induced cytokine release ± standard error of the mean ( d-g ). Two-way ANOVA with Bonferroni post-hoc testing was used to determine statistical significance. Significance is represented as *** ( p
    Figure Legend Snippet: Reduced cytokine release upon arachidonic acid challenge in COPD versus non-COPD. Pulmonary fibroblasts from COPD ( n = 11–19) and non-COPD patients ( n = 12–36 ) were unstimulated (control) or challenged with ω-6 PUFA arachidonic acid (AA) in 0.1% BSA-DMEM (10 and 100 μM) for 48 h. Cell free supernatants were collected and CXCL8 ( a ), IL-6 ( b ) and PGE2 ( c ) release was measured using ELISA or enzyme immunoassay. Other cells from COPD ( n = 6–7) and non-COPD ( n = 6–7) patients were pre-treated with indomethacin (1 μM) ( d, e ) or celecoxib (0.01-1 μM) ( f, g ) for 60 min prior to challenge with AA (100 μM) in 0.1% BSA-DMEM for 48 h. Cell free supernatants were collected and CXCL8 ( d, f ) and IL-6 ( e, g ) release was measured using ELISA. Data are expressed as mean ± standard error of the mean ( a-c ) or as % of AA-induced cytokine release ± standard error of the mean ( d-g ). Two-way ANOVA with Bonferroni post-hoc testing was used to determine statistical significance. Significance is represented as *** ( p

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Similar arachidonic acid-induced COX-2 mRNA expression in COPD and non-COPD. Pulmonary fibroblasts from COPD ( n = 5) and non-COPD patients ( n = 5 ) were unstimulated (control) or challenged with ω-6 PUFA arachidonic acid (AA) in 0.1% BSA-DMEM (100 μM) for 6 ( a ), 9 ( b ), 24 ( c ) or 48 ( d ) hours. Total RNA was extracted and cyclooxygenase (COX)-2 mRNA expression was measured using qPCR. The results are normalized to the endogenous control (18S rRNA), and presented as fold change from control ( t = 0 h) ± standard error of the mean. Unpaired t-test was used to determined statistical significance. There were no statistical differences
    Figure Legend Snippet: Similar arachidonic acid-induced COX-2 mRNA expression in COPD and non-COPD. Pulmonary fibroblasts from COPD ( n = 5) and non-COPD patients ( n = 5 ) were unstimulated (control) or challenged with ω-6 PUFA arachidonic acid (AA) in 0.1% BSA-DMEM (100 μM) for 6 ( a ), 9 ( b ), 24 ( c ) or 48 ( d ) hours. Total RNA was extracted and cyclooxygenase (COX)-2 mRNA expression was measured using qPCR. The results are normalized to the endogenous control (18S rRNA), and presented as fold change from control ( t = 0 h) ± standard error of the mean. Unpaired t-test was used to determined statistical significance. There were no statistical differences

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    Similar cytokine release upon TNFα challenge in COPD versus non-COPD. Pulmonary fibroblasts from COPD ( n = 15 ) and non-COPD patients ( n = 27 ) were unstimulated (control) or challenged with TNFα in 0.1% BSA-DMEM (1 ng/ml) for 48 h. Cell free supernatants were collected and CXCL8 ( a ) and IL-6 ( b ) release was measured using ELISA. All data are represented as mean ± standard error of the mean. Two-way ANOVA with Bonferroni post-hoc testing was used to determine statistical significance. There were no statistical differences
    Figure Legend Snippet: Similar cytokine release upon TNFα challenge in COPD versus non-COPD. Pulmonary fibroblasts from COPD ( n = 15 ) and non-COPD patients ( n = 27 ) were unstimulated (control) or challenged with TNFα in 0.1% BSA-DMEM (1 ng/ml) for 48 h. Cell free supernatants were collected and CXCL8 ( a ) and IL-6 ( b ) release was measured using ELISA. All data are represented as mean ± standard error of the mean. Two-way ANOVA with Bonferroni post-hoc testing was used to determine statistical significance. There were no statistical differences

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Arachidonic acid does not cause cytotoxicity in COPD and non-COPD fibroblasts. Pulmonary fibroblasts from COPD ( n = 7) and non-COPD patients ( n = 9 ) were unstimulated (control) or challenged with ω-6 PUFA arachidonic acid (AA) in 0.1% BSA-DMEM (100 μM) for 48 h. Cell free supernatants were collected and cell viability was estimated using lactate dehydrogenase (LDH) activity assay. Data is expressed as the absorbance (OD) at 490 nm ± standard error of the mean. Two-way ANOVA with Bonferroni post-hoc testing was used to determine statistical significance. There were no statistical differences
    Figure Legend Snippet: Arachidonic acid does not cause cytotoxicity in COPD and non-COPD fibroblasts. Pulmonary fibroblasts from COPD ( n = 7) and non-COPD patients ( n = 9 ) were unstimulated (control) or challenged with ω-6 PUFA arachidonic acid (AA) in 0.1% BSA-DMEM (100 μM) for 48 h. Cell free supernatants were collected and cell viability was estimated using lactate dehydrogenase (LDH) activity assay. Data is expressed as the absorbance (OD) at 490 nm ± standard error of the mean. Two-way ANOVA with Bonferroni post-hoc testing was used to determine statistical significance. There were no statistical differences

    Techniques Used: Activity Assay

    3) Product Images from "Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses"

    Article Title: Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses

    Journal: Scientific Reports

    doi: 10.1038/srep25080

    MisTTR antibody selectively binds monomeric, misfolded conformations of TTR. ( A ) Indirect ELISA using monomeric TTR (0.01 mg/mL TTR incubated at 25 °C , pH 3, 44 h), guanidine unfolded TTR (TTR in 6 M guanidine , incubated overnight at 25 °C), folded native TTR and BSA. ( B ) Competition ELISA using guanidine unfolded TTR as bound antigen, with monomeric and tetrameric TTR as competitors, and misTTR as the antibody. IC 50 = 63 ± 20 nM for monomeric TTR’s binding affinity for misTTR. ( C ) Native and SDS-PAGE analysis was performed on wild-type TTR purified from human plasma (purchased from Sigma-Aldrich). For native PAGE analysis, three pairs of sample lanes were run. The first lane consisted of molecular weight markers while the second lane consisted of 2 mg of wild-type TTR. The three pairs of lanes were excised from the gel. The first excised lane pair was stained with Coomassie Blue dye. The second pair was transferred to PDVF membrane and immunoblotted with misTTR antibody. The third pair was similarly transferred to PDVF membrane but immunoblotted with commercial anti-TTR antibody. The same procedure was repeated for an SDS-PAGE counterpart. In the native gels, misTTR did not recognize any species, while anti-TTR recognized putative dimers and higher molecular weight oligomers. In SDS gels misTTR only recognized monomers, while anti-TTR recognized monomers and putative dimers.
    Figure Legend Snippet: MisTTR antibody selectively binds monomeric, misfolded conformations of TTR. ( A ) Indirect ELISA using monomeric TTR (0.01 mg/mL TTR incubated at 25 °C , pH 3, 44 h), guanidine unfolded TTR (TTR in 6 M guanidine , incubated overnight at 25 °C), folded native TTR and BSA. ( B ) Competition ELISA using guanidine unfolded TTR as bound antigen, with monomeric and tetrameric TTR as competitors, and misTTR as the antibody. IC 50 = 63 ± 20 nM for monomeric TTR’s binding affinity for misTTR. ( C ) Native and SDS-PAGE analysis was performed on wild-type TTR purified from human plasma (purchased from Sigma-Aldrich). For native PAGE analysis, three pairs of sample lanes were run. The first lane consisted of molecular weight markers while the second lane consisted of 2 mg of wild-type TTR. The three pairs of lanes were excised from the gel. The first excised lane pair was stained with Coomassie Blue dye. The second pair was transferred to PDVF membrane and immunoblotted with misTTR antibody. The third pair was similarly transferred to PDVF membrane but immunoblotted with commercial anti-TTR antibody. The same procedure was repeated for an SDS-PAGE counterpart. In the native gels, misTTR did not recognize any species, while anti-TTR recognized putative dimers and higher molecular weight oligomers. In SDS gels misTTR only recognized monomers, while anti-TTR recognized monomers and putative dimers.

    Techniques Used: Indirect ELISA, Incubation, Enzyme-linked Immunosorbent Assay, Binding Assay, SDS Page, Purification, Clear Native PAGE, Molecular Weight, Staining

    4) Product Images from "Human Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P) regulates cytoplasmic lipid droplet abundance: A potential target for indirect-acting anti-dengue virus agents"

    Article Title: Human Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P) regulates cytoplasmic lipid droplet abundance: A potential target for indirect-acting anti-dengue virus agents

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0174483

    Extracellularly applied oleic acid, an inducer of lipid droplet formation, rescues intracellular DENV-2 RNA abundance in PF-429242-treated Huh-7.5.1 cells. (A–D) Huh-7.5.1 cells were treated either with 0.01% DMSO (control) or 10 μM PF-429242 for 24 hours. The inhibitor was removed and the cells were then infected with DENV-2 (MOI = 0.01) (A–B) or mock-infected (C–D) with or without addition of 0.6 mM oleic acid (with BSA in molar ratio 6:1) for 24 hours. (A) Total RNA was harvested and DENV-2 RNA levels, normalized to β-actin transcript levels, were relatively quantified in cell extracts using qRT-PCR. (B) Collected supernatant was cultured with naïve Huh-7.5.1 cells for 48 hours, and DENV-2 RNA levels were quantified. (C) Representative images of the effect of PF-429242 and oleic acid on lipid droplets are shown. Fixed cells were permeabilized with Triton X-100 and stained for cell nuclei using Hoechst dye and for lipid droplets using Nile red. Images were obtained using a Leica SP8 confocal microscope with a 100x objective. (D) Abundance of LDs was quantified by measuring the average LD-positive area (μm 2 )/cell and the average number of LDs/cell based on Nile red fluorescence in 0.01% DMSO-treated (control), PF-429242-treated (10 μM), OA/BSA-treated, and PF-429242 (10 μM) + OA/BSA-treated cells using Fiji software ( > 50 cells analyzed). Statistical significance was calculated with a two-way (A, D) and one-way (B) ANOVA with a Bonferroni’s post-test (*, p
    Figure Legend Snippet: Extracellularly applied oleic acid, an inducer of lipid droplet formation, rescues intracellular DENV-2 RNA abundance in PF-429242-treated Huh-7.5.1 cells. (A–D) Huh-7.5.1 cells were treated either with 0.01% DMSO (control) or 10 μM PF-429242 for 24 hours. The inhibitor was removed and the cells were then infected with DENV-2 (MOI = 0.01) (A–B) or mock-infected (C–D) with or without addition of 0.6 mM oleic acid (with BSA in molar ratio 6:1) for 24 hours. (A) Total RNA was harvested and DENV-2 RNA levels, normalized to β-actin transcript levels, were relatively quantified in cell extracts using qRT-PCR. (B) Collected supernatant was cultured with naïve Huh-7.5.1 cells for 48 hours, and DENV-2 RNA levels were quantified. (C) Representative images of the effect of PF-429242 and oleic acid on lipid droplets are shown. Fixed cells were permeabilized with Triton X-100 and stained for cell nuclei using Hoechst dye and for lipid droplets using Nile red. Images were obtained using a Leica SP8 confocal microscope with a 100x objective. (D) Abundance of LDs was quantified by measuring the average LD-positive area (μm 2 )/cell and the average number of LDs/cell based on Nile red fluorescence in 0.01% DMSO-treated (control), PF-429242-treated (10 μM), OA/BSA-treated, and PF-429242 (10 μM) + OA/BSA-treated cells using Fiji software ( > 50 cells analyzed). Statistical significance was calculated with a two-way (A, D) and one-way (B) ANOVA with a Bonferroni’s post-test (*, p

    Techniques Used: Infection, Quantitative RT-PCR, Cell Culture, Staining, Microscopy, Fluorescence, Software

    5) Product Images from "Reverse lectin ELISA for detecting fucosylated forms of α1-acid glycoprotein associated with hepatocellular carcinoma"

    Article Title: Reverse lectin ELISA for detecting fucosylated forms of α1-acid glycoprotein associated with hepatocellular carcinoma

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0173897

    A . Binding of different concentrations of purified AGP from patient samples to S2 in the reverse S2 lectin ELISA. AGP purified from a patient with HCC (black triangles), AGP purified from a cirrhosis patient (black squares) and AGP purified from a normal sample (black circles). B. Comparison of binding of different concentrations of purified AGP from a HCC patient sample diluted in 1% BSA in PBS (circles) and diluted in normal serum (black squares). C. Binding of different concentrations of dsAGP to S2 in the reverse S2 lectin ELISA assay.
    Figure Legend Snippet: A . Binding of different concentrations of purified AGP from patient samples to S2 in the reverse S2 lectin ELISA. AGP purified from a patient with HCC (black triangles), AGP purified from a cirrhosis patient (black squares) and AGP purified from a normal sample (black circles). B. Comparison of binding of different concentrations of purified AGP from a HCC patient sample diluted in 1% BSA in PBS (circles) and diluted in normal serum (black squares). C. Binding of different concentrations of dsAGP to S2 in the reverse S2 lectin ELISA assay.

    Techniques Used: Binding Assay, Purification, Enzyme-linked Immunosorbent Assay

    6) Product Images from "Formation of high molecular weight p62 by CORM-3"

    Article Title: Formation of high molecular weight p62 by CORM-3

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0210474

    Production of HMW-p62 by CORM-3 in vitro . Purified recombinant full-length human p62 (A), bovine plasma fibronectin (FN) (B), or bovine serum albumin (BSA) (C) was dissolved in PBS and treated with CORM-3 (1 mM), CORM-A1 (1 mM), or RuCl 3 (1 mM) for 0–60 min. p62, FN, and BSA were also treated with verteporfin (10 μM) for 0-60min. After SDS-PAGE, p62 and FN were visualized by immunoblot analysis while BSA was stained with CBB.
    Figure Legend Snippet: Production of HMW-p62 by CORM-3 in vitro . Purified recombinant full-length human p62 (A), bovine plasma fibronectin (FN) (B), or bovine serum albumin (BSA) (C) was dissolved in PBS and treated with CORM-3 (1 mM), CORM-A1 (1 mM), or RuCl 3 (1 mM) for 0–60 min. p62, FN, and BSA were also treated with verteporfin (10 μM) for 0-60min. After SDS-PAGE, p62 and FN were visualized by immunoblot analysis while BSA was stained with CBB.

    Techniques Used: In Vitro, Purification, Recombinant, SDS Page, Staining

    7) Product Images from "Albumin nanoparticles increase the anticancer efficacy of albendazole in ovarian cancer xenograft model"

    Article Title: Albumin nanoparticles increase the anticancer efficacy of albendazole in ovarian cancer xenograft model

    Journal: Journal of Nanobiotechnology

    doi: 10.1186/s12951-015-0082-8

    Release profile of albendazole from albumin nanoparticles. In-vitro release behaviour of ABZ from nanoparticle formulations BSA-ABZ 10 nm and Nab-ABZ 200 nm in PBS at pH 7.4. The nanoparticle dispersion was placed in an orbital shaker and shaken at 100 rpm at 37°C for 192 hours. The released ABZ concentration was measured by HPLC. Data are presented as mean ± SD (n = 2).
    Figure Legend Snippet: Release profile of albendazole from albumin nanoparticles. In-vitro release behaviour of ABZ from nanoparticle formulations BSA-ABZ 10 nm and Nab-ABZ 200 nm in PBS at pH 7.4. The nanoparticle dispersion was placed in an orbital shaker and shaken at 100 rpm at 37°C for 192 hours. The released ABZ concentration was measured by HPLC. Data are presented as mean ± SD (n = 2).

    Techniques Used: In Vitro, Concentration Assay, High Performance Liquid Chromatography

    Cytotoxicity of albendazole loaded albumin nanoparticles. Comparison of the cytotoxic effects of BSA-ABZ 10 nm, Nab-ABZ 200 nm and free ABZ in ovarian cancer cells, OVCAR3 (A) SKOV3 (B) and HOSE (C) at different concentration of ABZ (μM) for 72 hours. Each experiment was conducted three times with replicates of 4 to 8 for each drug concentration. Data are presented as mean ± SD (n = 3).
    Figure Legend Snippet: Cytotoxicity of albendazole loaded albumin nanoparticles. Comparison of the cytotoxic effects of BSA-ABZ 10 nm, Nab-ABZ 200 nm and free ABZ in ovarian cancer cells, OVCAR3 (A) SKOV3 (B) and HOSE (C) at different concentration of ABZ (μM) for 72 hours. Each experiment was conducted three times with replicates of 4 to 8 for each drug concentration. Data are presented as mean ± SD (n = 3).

    Techniques Used: Concentration Assay

    Synthesis and characterization of nab-ABZ. Schematic illustration of albendazole encapsulation by albumin nanoparticles (A) . TEM images of BSA-ABZ 10 nm (B) , the scale bar is 500 nm and TEM images of Nab-ABZ 200 nm (C) , and the scale bar is 0.2 μm. Size distribution (volume %) measured by DLS of BSA-ABZ 10 nm (D) and Nab-ABZ 200 nm (E) . Data are presented as the average of two measurements. TEM images confirmed the particle size of DLS.
    Figure Legend Snippet: Synthesis and characterization of nab-ABZ. Schematic illustration of albendazole encapsulation by albumin nanoparticles (A) . TEM images of BSA-ABZ 10 nm (B) , the scale bar is 500 nm and TEM images of Nab-ABZ 200 nm (C) , and the scale bar is 0.2 μm. Size distribution (volume %) measured by DLS of BSA-ABZ 10 nm (D) and Nab-ABZ 200 nm (E) . Data are presented as the average of two measurements. TEM images confirmed the particle size of DLS.

    Techniques Used: Transmission Electron Microscopy

    8) Product Images from "IL-1? enhances cell adhesion to degraded fibronectin"

    Article Title: IL-1? enhances cell adhesion to degraded fibronectin

    Journal: The FASEB Journal

    doi: 10.1096/fj.12-207381

    A ) HGFs plated on PLL-coated dishes were treated with vehicle or with IL-1β (20 ng/ml) for 30 min prior to incubation with BSA- or FN-coated fluorescent beads, and the percentage of cells with bound beads was analyzed by flow cytometry. B ) HGFs
    Figure Legend Snippet: A ) HGFs plated on PLL-coated dishes were treated with vehicle or with IL-1β (20 ng/ml) for 30 min prior to incubation with BSA- or FN-coated fluorescent beads, and the percentage of cells with bound beads was analyzed by flow cytometry. B ) HGFs

    Techniques Used: Incubation, Flow Cytometry, Cytometry

    9) Product Images from "Cost-effective and sensitive colorimetric immunosensing using an iron oxide-to-Prussian blue nanoparticles conversion strategy"

    Article Title: Cost-effective and sensitive colorimetric immunosensing using an iron oxide-to-Prussian blue nanoparticles conversion strategy

    Journal: The Analyst

    doi: 10.1039/c6an00254d

    Photographs (A) and UV-Vis spectra (B) of the immunosensing solutions at different PSA concentrations (5% BSA) before and after the nanoparticle conversion process. (C) Calibration plot of absorbance at 748 nm in UV-Vis spectra vs . logarithm of the PSA
    Figure Legend Snippet: Photographs (A) and UV-Vis spectra (B) of the immunosensing solutions at different PSA concentrations (5% BSA) before and after the nanoparticle conversion process. (C) Calibration plot of absorbance at 748 nm in UV-Vis spectra vs . logarithm of the PSA

    Techniques Used:

    10) Product Images from "Analysis of Surface Plasmon Resonance Curves with a Novel Sigmoid-Asymmetric Fitting Algorithm"

    Article Title: Analysis of Surface Plasmon Resonance Curves with a Novel Sigmoid-Asymmetric Fitting Algorithm

    Journal: Sensors (Basel, Switzerland)

    doi: 10.3390/s151025385

    Sensorgrams obtained by measuring θ RA (black solid line), θ CA (gray solid line), and θ SAA (pink solid line) in real time on binding, diluted BSA-glycerin mixture in PBS buffer solution on bare gold sensor chip.
    Figure Legend Snippet: Sensorgrams obtained by measuring θ RA (black solid line), θ CA (gray solid line), and θ SAA (pink solid line) in real time on binding, diluted BSA-glycerin mixture in PBS buffer solution on bare gold sensor chip.

    Techniques Used: Binding Assay, Chromatin Immunoprecipitation

    11) Product Images from "Label-free Detection of Cardiac Troponin I with a Photonic Crystal Biosensor"

    Article Title: Label-free Detection of Cardiac Troponin I with a Photonic Crystal Biosensor

    Journal: Biosensors & bioelectronics

    doi: 10.1016/j.bios.2014.02.057

    (a) Detection of cTnI spiked in PBS solutions. The blue bars show the results for the sensor without BSA blocking, while the red bars show the results with BSA blocking. (b) Detection of cTnI in human plasma using a functionalized PC-TIR sensor with BSA
    Figure Legend Snippet: (a) Detection of cTnI spiked in PBS solutions. The blue bars show the results for the sensor without BSA blocking, while the red bars show the results with BSA blocking. (b) Detection of cTnI in human plasma using a functionalized PC-TIR sensor with BSA

    Techniques Used: Blocking Assay

    12) Product Images from "A role of the sphingosine-1-phosphate (S1P)–S1P receptor 2 pathway in epithelial defense against cancer (EDAC)"

    Article Title: A role of the sphingosine-1-phosphate (S1P)–S1P receptor 2 pathway in epithelial defense against cancer (EDAC)

    Journal: Molecular Biology of the Cell

    doi: 10.1091/mbc.E15-03-0161

    The S1P–S1PR2 pathway acts upstream of Rho–Rho kinase in normal cells neighboring RasV12-transformed cells. (A) MDCK cells or S1PR2-knockdown MDCK cells were transfected with an expression vector for the FRET-based biosensor RaichuEV-RhoA. The cells were further transfected with an expression vector for mCherry alone or together with that for RasV12 and then seeded on the collagen gel. After 12 h, the sample was screened under a fluorescence microscope for a pair of adjacent cells, one of which expressed RaichuEV-RhoA and the other mCherry/RasV12. The Raichu-expressing cells were then monitored by dual-emission fluorescence microscopy. FRET/CFP ratio images were generated to represent FRET efficiency. Representative images at the indicated time points. The upper and lower limits of the ratio range are indicated at the bottom. Arrows indicate Raichu-expressing cells neighboring mCherry-expressing cells. Scale bar, 10 μm. (B, C) Traces for three-point moving average of the FRET/CFP emission ratio. (B) Quantification of A. p = 5.2 × 10 −5 between MDCK/control and MDCK/RasV12; p = 4.0 × 10 −8 between MDCK/RasV12 and S1PR2-shRNA1/RasV12; p = 2.0 × 10 −6 between MDCK/RasV12 and S1PR2-shRNA2/RasV12. n = 7, MDCK/control; n = 5, MDCK/RasV12; n = 8, S1PR2-shRNA1/RasV12; and n = 8, S1PR2-shRNA2/RasV12. (C) Effect of S1P on the Rho activity in normal cells. p = 1.7 × 10 −9 between MDCK/control and MDCK/RasV12. n = 6, control (fatty acid–free BSA); and n = 11, 200 nM S1P. Error bars indicate SEM. Time 0 min is set when the microscopic observations start (A, B) or S1P is added (C). (D) Effect of exogenously added S1P on the apical extrusion of RasV12 cells surrounded by normal MDCK cells or MDCK cells expressing the Rho kinase dominant-negative mutant. Data are mean ± SD from three (first, second, fifth, and sixth bars) or six (third and fourth bars) independent experiments. * p = 0.013, ** p = 0.00082, *** p = 0.0088. n.s., not significant.
    Figure Legend Snippet: The S1P–S1PR2 pathway acts upstream of Rho–Rho kinase in normal cells neighboring RasV12-transformed cells. (A) MDCK cells or S1PR2-knockdown MDCK cells were transfected with an expression vector for the FRET-based biosensor RaichuEV-RhoA. The cells were further transfected with an expression vector for mCherry alone or together with that for RasV12 and then seeded on the collagen gel. After 12 h, the sample was screened under a fluorescence microscope for a pair of adjacent cells, one of which expressed RaichuEV-RhoA and the other mCherry/RasV12. The Raichu-expressing cells were then monitored by dual-emission fluorescence microscopy. FRET/CFP ratio images were generated to represent FRET efficiency. Representative images at the indicated time points. The upper and lower limits of the ratio range are indicated at the bottom. Arrows indicate Raichu-expressing cells neighboring mCherry-expressing cells. Scale bar, 10 μm. (B, C) Traces for three-point moving average of the FRET/CFP emission ratio. (B) Quantification of A. p = 5.2 × 10 −5 between MDCK/control and MDCK/RasV12; p = 4.0 × 10 −8 between MDCK/RasV12 and S1PR2-shRNA1/RasV12; p = 2.0 × 10 −6 between MDCK/RasV12 and S1PR2-shRNA2/RasV12. n = 7, MDCK/control; n = 5, MDCK/RasV12; n = 8, S1PR2-shRNA1/RasV12; and n = 8, S1PR2-shRNA2/RasV12. (C) Effect of S1P on the Rho activity in normal cells. p = 1.7 × 10 −9 between MDCK/control and MDCK/RasV12. n = 6, control (fatty acid–free BSA); and n = 11, 200 nM S1P. Error bars indicate SEM. Time 0 min is set when the microscopic observations start (A, B) or S1P is added (C). (D) Effect of exogenously added S1P on the apical extrusion of RasV12 cells surrounded by normal MDCK cells or MDCK cells expressing the Rho kinase dominant-negative mutant. Data are mean ± SD from three (first, second, fifth, and sixth bars) or six (third and fourth bars) independent experiments. * p = 0.013, ** p = 0.00082, *** p = 0.0088. n.s., not significant.

    Techniques Used: Transformation Assay, Transfection, Expressing, Plasmid Preparation, Fluorescence, Microscopy, Generated, Activity Assay, Dominant Negative Mutation

    13) Product Images from "Chitosan Plus Compound 48/80: Formulation and Preliminary Evaluation as a Hepatitis B Vaccine Adjuvant"

    Article Title: Chitosan Plus Compound 48/80: Formulation and Preliminary Evaluation as a Hepatitis B Vaccine Adjuvant

    Journal: Pharmaceutics

    doi: 10.3390/pharmaceutics11020072

    Evaluation of uptake by macrophages. ( A ) Uptake of nanoparticles was assessed by incubating 4 h, 100 µg/mL RAW 264.7 cells with Chi-C48/80 NPs or Chi NPs prepared with fluorescein isothiocyanate (FITC)-labeled chitosan (green). ( B ) Uptake of the antigen loaded on nanoparticles was evaluated by incubating the cells with FITC-BSA loaded Chi-C48/80 NPs or Chi NPs. Cells were labeled with Alexa Fluor © 350 WGA (blue) to identify the membrane, and Lysotracker © Red identifies the acidic endosomes and lysosomes. Arrows in the merge image show co-localization.
    Figure Legend Snippet: Evaluation of uptake by macrophages. ( A ) Uptake of nanoparticles was assessed by incubating 4 h, 100 µg/mL RAW 264.7 cells with Chi-C48/80 NPs or Chi NPs prepared with fluorescein isothiocyanate (FITC)-labeled chitosan (green). ( B ) Uptake of the antigen loaded on nanoparticles was evaluated by incubating the cells with FITC-BSA loaded Chi-C48/80 NPs or Chi NPs. Cells were labeled with Alexa Fluor © 350 WGA (blue) to identify the membrane, and Lysotracker © Red identifies the acidic endosomes and lysosomes. Arrows in the merge image show co-localization.

    Techniques Used: Labeling, Whole Genome Amplification

    14) Product Images from "Spectral-domain optical coherence phase microscopy for label-free multiplexed protein microarray assay"

    Article Title: Spectral-domain optical coherence phase microscopy for label-free multiplexed protein microarray assay

    Journal: Biosensors & bioelectronics

    doi: 10.1016/j.bios.2009.06.028

    SD-OCPM protein assay on selective absorption of streptavidin to bBSA. The BSA and bBSA were spotted on the sensor surface. After incubation with streptavidin solution and rinsing with PBST, a ∼0.055 rad increase in phase delay was observed on
    Figure Legend Snippet: SD-OCPM protein assay on selective absorption of streptavidin to bBSA. The BSA and bBSA were spotted on the sensor surface. After incubation with streptavidin solution and rinsing with PBST, a ∼0.055 rad increase in phase delay was observed on

    Techniques Used: Incubation

    15) Product Images from "A Colorimetric Enzyme-Linked Immunosorbent Assay with CuO Nanoparticles as Signal Labels Based on the Growth of Gold Nanoparticles In Situ"

    Article Title: A Colorimetric Enzyme-Linked Immunosorbent Assay with CuO Nanoparticles as Signal Labels Based on the Growth of Gold Nanoparticles In Situ

    Journal: Nanomaterials

    doi: 10.3390/nano9010004

    The photographic images and absorption intensity for assays of various proteins (1, PSA; 2, BSA; 3, IgG; 4, albumin; 5, hemoglobin). The final concentration of PSA was 10 ng/mL and that of other proteins is 100 ng/mL.
    Figure Legend Snippet: The photographic images and absorption intensity for assays of various proteins (1, PSA; 2, BSA; 3, IgG; 4, albumin; 5, hemoglobin). The final concentration of PSA was 10 ng/mL and that of other proteins is 100 ng/mL.

    Techniques Used: Concentration Assay

    16) Product Images from "Interaction of C1q With Pentraxin 3 and IgM Revisited: Mutational Studies With Recombinant C1q Variants"

    Article Title: Interaction of C1q With Pentraxin 3 and IgM Revisited: Mutational Studies With Recombinant C1q Variants

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2019.00461

    Kinetic analyses of the interaction of PTX3 and IgM with immobilized C1q variants. Sixty microliter of PTX3 at the indicated concentrations were injected over (A) C1qWT (16,300 RU), (B) C1qLys C170 Glu (17,000 RU), (C) C1qTyr B175 Leu (12,200 RU), (D) C1qLys A200 Asp-Lys A201 Asp (18,400 RU), and (E) C1qArg B108 Asp-Arg B109 Glu (17,500 RU) in 50 mM Tris-HCl, 150 mM NaCl, 2 mM CaCl 2 , 0.005% surfactant P20, pH 7.4 at a flow rate of 20 μl/min. (F–J) IgM was injected over the immobilized C1q variants under the same conditions as in (A–E) . The binding signals shown were obtained by subtracting the signal over the BSA reference surface and further subtraction of buffer blanks. Fits are shown as red lines and were obtained by global fitting of the data using a 1:1 Langmuir binding model. Chi2 values were between 0.25 and 5.8. Each kinetic analysis shown is representative of two to five independent experiments performed on separate sensor chips.
    Figure Legend Snippet: Kinetic analyses of the interaction of PTX3 and IgM with immobilized C1q variants. Sixty microliter of PTX3 at the indicated concentrations were injected over (A) C1qWT (16,300 RU), (B) C1qLys C170 Glu (17,000 RU), (C) C1qTyr B175 Leu (12,200 RU), (D) C1qLys A200 Asp-Lys A201 Asp (18,400 RU), and (E) C1qArg B108 Asp-Arg B109 Glu (17,500 RU) in 50 mM Tris-HCl, 150 mM NaCl, 2 mM CaCl 2 , 0.005% surfactant P20, pH 7.4 at a flow rate of 20 μl/min. (F–J) IgM was injected over the immobilized C1q variants under the same conditions as in (A–E) . The binding signals shown were obtained by subtracting the signal over the BSA reference surface and further subtraction of buffer blanks. Fits are shown as red lines and were obtained by global fitting of the data using a 1:1 Langmuir binding model. Chi2 values were between 0.25 and 5.8. Each kinetic analysis shown is representative of two to five independent experiments performed on separate sensor chips.

    Techniques Used: Injection, Flow Cytometry, Binding Assay

    17) Product Images from "The Chlamydia trachomatis PmpD adhesin forms higher order structures through disulphide-mediated covalent interactions"

    Article Title: The Chlamydia trachomatis PmpD adhesin forms higher order structures through disulphide-mediated covalent interactions

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0198662

    Adhesion of rPmpD-coated beads to Hak cells is inhibited by soluble rPmpD and anti-rPmpD serum. ( A ) Carboxylate-modified beads were coated with oligomeric or monomeric rPmpD (50 μg/ml) and compared to control (naked or 200 μg/ml BSA-coated beads) at two different bead dilutions. The number of rPmpD-coated beads adhered to 50 cells within triplicate fields of view was counted. Significantly enhanced adhesive capacity compared to naked or BSA-coated beads was observed, although no significant difference in adhesion was observed between beads coated with oligomeric and monomeric rPmpD proteoforms ( B ) Titration of oligomeric rPmpD (50 μg/ml-0.25 μg/ml) prior to bead coating shows a pronounced concentration-dependent reduction in adhesion. Significance values are reported relative to BSA-coated beads. ( C ) Soluble rPmpD competitor protein significantly reduces adhesion of rPmpD-coated beads in a dose-dependent manner, likely indicating competitive binding of putative host cell receptor(s). Significance is measured relative to pre-incubation with BSA only. (D) Heat-inactivated anti-rPmpD serum obtained from rPmpD-immunized mice abrogates adhesion of rPmpD-coated beads. Bead coating concentration of rPmpD varied from 50 μg/ml-2.5 μg/ml. Significance is measured relative to a 1:50 dilution of heat-inactivated pre-immune serum. All data are representative of 3 separate experiments, and presented as mean ± standard deviation. For all experiments, statistical significance was determined using a two-tailed t-test with GraphPad Prism 6. * = p≤0.05, ** p≤0.01, ***p≤0.001.
    Figure Legend Snippet: Adhesion of rPmpD-coated beads to Hak cells is inhibited by soluble rPmpD and anti-rPmpD serum. ( A ) Carboxylate-modified beads were coated with oligomeric or monomeric rPmpD (50 μg/ml) and compared to control (naked or 200 μg/ml BSA-coated beads) at two different bead dilutions. The number of rPmpD-coated beads adhered to 50 cells within triplicate fields of view was counted. Significantly enhanced adhesive capacity compared to naked or BSA-coated beads was observed, although no significant difference in adhesion was observed between beads coated with oligomeric and monomeric rPmpD proteoforms ( B ) Titration of oligomeric rPmpD (50 μg/ml-0.25 μg/ml) prior to bead coating shows a pronounced concentration-dependent reduction in adhesion. Significance values are reported relative to BSA-coated beads. ( C ) Soluble rPmpD competitor protein significantly reduces adhesion of rPmpD-coated beads in a dose-dependent manner, likely indicating competitive binding of putative host cell receptor(s). Significance is measured relative to pre-incubation with BSA only. (D) Heat-inactivated anti-rPmpD serum obtained from rPmpD-immunized mice abrogates adhesion of rPmpD-coated beads. Bead coating concentration of rPmpD varied from 50 μg/ml-2.5 μg/ml. Significance is measured relative to a 1:50 dilution of heat-inactivated pre-immune serum. All data are representative of 3 separate experiments, and presented as mean ± standard deviation. For all experiments, statistical significance was determined using a two-tailed t-test with GraphPad Prism 6. * = p≤0.05, ** p≤0.01, ***p≤0.001.

    Techniques Used: Modification, Titration, Concentration Assay, Binding Assay, Incubation, Mouse Assay, Standard Deviation, Two Tailed Test

    rPmpD-coated beads form adhesion clusters on the surface of mammalian cell lines. Syrian hamster kidney (Hak) cell lines (Panels A-C ) or murine fibroblast (McCoy) cell lines (Panels D-F ) were incubated with naked ( A,D ), BSA-coated ( B,E ) or rPmpD-coated ( C,F ) beads. Large clusters of rPmpD-coated beads are observed on the surfaces of both Hak and McCoy cell lines (red arrows). BSA-coated and naked beads do not demonstrate this aggregative property on the cell surface. Images were acquired at 10x magnification (Scale bar = 20 μm).
    Figure Legend Snippet: rPmpD-coated beads form adhesion clusters on the surface of mammalian cell lines. Syrian hamster kidney (Hak) cell lines (Panels A-C ) or murine fibroblast (McCoy) cell lines (Panels D-F ) were incubated with naked ( A,D ), BSA-coated ( B,E ) or rPmpD-coated ( C,F ) beads. Large clusters of rPmpD-coated beads are observed on the surfaces of both Hak and McCoy cell lines (red arrows). BSA-coated and naked beads do not demonstrate this aggregative property on the cell surface. Images were acquired at 10x magnification (Scale bar = 20 μm).

    Techniques Used: Incubation

    18) Product Images from "Protective Efficacy of a Novel Alpha Hemolysin Subunit Vaccine (AT62) against Staphylococcus aureus Skin and Soft Tissue Infections"

    Article Title: Protective Efficacy of a Novel Alpha Hemolysin Subunit Vaccine (AT62) against Staphylococcus aureus Skin and Soft Tissue Infections

    Journal: Vaccine

    doi: 10.1016/j.vaccine.2016.09.061

    Immunogenicity and protective efficacy of AT62 in a murine surgical wound infection model. (A) Mice were immunized on days 0, 14, and 28 with 20 μg AT62 or BSA + MPL. Serum samples were diluted 1:100, and antibody levels to native Hla were measured by ELISA. (B) Mice actively immunized with AT62 or BSA had surgical site wounds inoculated with 3 μl containing 176 to 300 CFU S. aureus LAC. Three days after bacterial challenge, quantitative cultures were performed on homogenized tissues to determine the bacterial burden. The data are pooled from two independent experiments. (C) Mice were passively immunized by the IP route with 1 mg of rabbit AT62 IgG or naïve IgG and challenged 24 h later with 43 to 92 CFU S. aureus LAC. Quantitative cultures were performed after 3 d on homogenized tissues to determine the bacterial burden. Horizontal lines represent group medians, and dashed lines represent lower limit of detection by culture. *, P
    Figure Legend Snippet: Immunogenicity and protective efficacy of AT62 in a murine surgical wound infection model. (A) Mice were immunized on days 0, 14, and 28 with 20 μg AT62 or BSA + MPL. Serum samples were diluted 1:100, and antibody levels to native Hla were measured by ELISA. (B) Mice actively immunized with AT62 or BSA had surgical site wounds inoculated with 3 μl containing 176 to 300 CFU S. aureus LAC. Three days after bacterial challenge, quantitative cultures were performed on homogenized tissues to determine the bacterial burden. The data are pooled from two independent experiments. (C) Mice were passively immunized by the IP route with 1 mg of rabbit AT62 IgG or naïve IgG and challenged 24 h later with 43 to 92 CFU S. aureus LAC. Quantitative cultures were performed after 3 d on homogenized tissues to determine the bacterial burden. Horizontal lines represent group medians, and dashed lines represent lower limit of detection by culture. *, P

    Techniques Used: Infection, Mouse Assay, Enzyme-linked Immunosorbent Assay

    Protective efficacy of AT62 in a necrotic lesion model of SSTI. Mice were actively immunized with 20 μg AT62 or BSA before challenge with 10 7 CFU of S. aureus LAC. Lesion size (A) and weight loss (B) were measured over 14 days. The data are representative of two independent experiments and were analyzed by two-way ANOVA with multiple comparisons corrected for repeated measures. **, P
    Figure Legend Snippet: Protective efficacy of AT62 in a necrotic lesion model of SSTI. Mice were actively immunized with 20 μg AT62 or BSA before challenge with 10 7 CFU of S. aureus LAC. Lesion size (A) and weight loss (B) were measured over 14 days. The data are representative of two independent experiments and were analyzed by two-way ANOVA with multiple comparisons corrected for repeated measures. **, P

    Techniques Used: Mouse Assay

    19) Product Images from "Endogenous glucocorticoids modulate neutrophil function in a murine model of haemolytic uraemic syndrome"

    Article Title: Endogenous glucocorticoids modulate neutrophil function in a murine model of haemolytic uraemic syndrome

    Journal: Clinical and Experimental Immunology

    doi: 10.1111/j.1365-2249.2005.02659.x

    Effect of Stx2 and Ru486 on PMN adhesion 72 h post treatment. PMN (1·5 × 10 5 ) were incubated with saline solution (BASAL) (□) or PMA (10 ng/ml) 60 min at 37°C (▪) and seeded on plates coated with (a) FGN (b) BSA and (c) CTI. Adhesion was revealed by crystal violet staining. The results are expressed as percentage of increase with respect to BASAL saline and each value represents the mean ± SEM from 4 to 6 separate experiments performed with a pool of 3 mice/group. (a) * P
    Figure Legend Snippet: Effect of Stx2 and Ru486 on PMN adhesion 72 h post treatment. PMN (1·5 × 10 5 ) were incubated with saline solution (BASAL) (□) or PMA (10 ng/ml) 60 min at 37°C (▪) and seeded on plates coated with (a) FGN (b) BSA and (c) CTI. Adhesion was revealed by crystal violet staining. The results are expressed as percentage of increase with respect to BASAL saline and each value represents the mean ± SEM from 4 to 6 separate experiments performed with a pool of 3 mice/group. (a) * P

    Techniques Used: Incubation, Staining, Mouse Assay

    20) Product Images from "Effect of Plasma Protein Binding on the Anti-Hepatitis B Virus Activity and Pharmacokinetic Properties of NVR 3-778"

    Article Title: Effect of Plasma Protein Binding on the Anti-Hepatitis B Virus Activity and Pharmacokinetic Properties of NVR 3-778

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.01497-18

    Pharmacokinetic properties of NVR 3-778 in PHHs cultured in different HCM. PHHs that were cultured for 5 days in either HCM without BSA/hA1GP (●) or in HCM spiked with 4.3% BSA–0.07% hA1GP (■) or with 8% BSA–0.07% hA1GP (▲) were incubated with 1 μM NVR 3-778 for 4 days, and both cells and supernatant were harvested at 1, 24, 48, and 72 h postincubation. The parent drug was quantified by LC/MS-MS at the indicated time points. (A) Quantification of the parent drug in the cell culture supernatant of PHHs. (B) Cellular concentration normalized for the hepatocyte volume of NVR 3-778 in PHHs. (C) Predicted liver-to-medium ratio of NVR 3-778 at the indicated time points calculated based on the medium and hepatocyte concentrations of NVR 3-778 in PHHs. Hepatocyte concentrations were normalized for the hepatocellularity to predict the corresponding liver concentrations. All data represent the means of three replicates ± SEM.
    Figure Legend Snippet: Pharmacokinetic properties of NVR 3-778 in PHHs cultured in different HCM. PHHs that were cultured for 5 days in either HCM without BSA/hA1GP (●) or in HCM spiked with 4.3% BSA–0.07% hA1GP (■) or with 8% BSA–0.07% hA1GP (▲) were incubated with 1 μM NVR 3-778 for 4 days, and both cells and supernatant were harvested at 1, 24, 48, and 72 h postincubation. The parent drug was quantified by LC/MS-MS at the indicated time points. (A) Quantification of the parent drug in the cell culture supernatant of PHHs. (B) Cellular concentration normalized for the hepatocyte volume of NVR 3-778 in PHHs. (C) Predicted liver-to-medium ratio of NVR 3-778 at the indicated time points calculated based on the medium and hepatocyte concentrations of NVR 3-778 in PHHs. Hepatocyte concentrations were normalized for the hepatocellularity to predict the corresponding liver concentrations. All data represent the means of three replicates ± SEM.

    Techniques Used: Cell Culture, Incubation, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Concentration Assay

    Effect of plasma proteins on cell viability of HBV-infected PHHs. Cell viability was assessed by measurement of the ATP content after 8 and 12 days postinfection, as indicated. PHHs were HBV infected and cultured in medium without BSA/hA1GP or in medium spiked with either 4.3% BSA or 8% BSA together with 0.07% hA1GP for 8 and 12 days. Cell viability in HCM without BSA/hA1GP was set to be 100%. All data represent the means of three or more independent experiments ± SEM. **, P
    Figure Legend Snippet: Effect of plasma proteins on cell viability of HBV-infected PHHs. Cell viability was assessed by measurement of the ATP content after 8 and 12 days postinfection, as indicated. PHHs were HBV infected and cultured in medium without BSA/hA1GP or in medium spiked with either 4.3% BSA or 8% BSA together with 0.07% hA1GP for 8 and 12 days. Cell viability in HCM without BSA/hA1GP was set to be 100%. All data represent the means of three or more independent experiments ± SEM. **, P

    Techniques Used: Infection, Cell Culture

    21) Product Images from "Long Polar Fimbriae of Enterohemorrhagic Escherichia coli O157:H7 Bind to Extracellular Matrix Proteins ▿"

    Article Title: Long Polar Fimbriae of Enterohemorrhagic Escherichia coli O157:H7 Bind to Extracellular Matrix Proteins ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.05317-11

    ECM proteins promote EHEC adherence to T84 cells. Numbers of adherent EHEC EDL933-infecting T84 cells preincubated with 5 μg/ml of fibronectin (T84+Fn), laminin (T84+Lm), collagen IV (T84+IVC), or BSA (T84+BSA) prior to infection. *, P
    Figure Legend Snippet: ECM proteins promote EHEC adherence to T84 cells. Numbers of adherent EHEC EDL933-infecting T84 cells preincubated with 5 μg/ml of fibronectin (T84+Fn), laminin (T84+Lm), collagen IV (T84+IVC), or BSA (T84+BSA) prior to infection. *, P

    Techniques Used: Infection

    22) Product Images from "Investigating the effect of proteoglycan 4 on hyaluronan solution properties using confocal fluorescence recovery after photobleaching"

    Article Title: Investigating the effect of proteoglycan 4 on hyaluronan solution properties using confocal fluorescence recovery after photobleaching

    Journal: BMC Musculoskeletal Disorders

    doi: 10.1186/s12891-019-2469-4

    Apparent mesh size distribution (ξ) of 1500 kDa HA ± 450 μg/mL BSA (∆ for HA + BSA, ● for HA) ( a ), 500 kDa HA ± 450 μ g/mL BSA ( b ); 1500 kDa HA ± 45 μg/mL BSA ( c ), 500 kDa HA ± 45 μ g/mL BSA ( d ). The empirical constants from the scaling equations were used to calculate the average distribution of apparent mesh sizes, ξ, using the correlation length relation (dashed lines = HA + PRG4, solid lines = HA)
    Figure Legend Snippet: Apparent mesh size distribution (ξ) of 1500 kDa HA ± 450 μg/mL BSA (∆ for HA + BSA, ● for HA) ( a ), 500 kDa HA ± 450 μ g/mL BSA ( b ); 1500 kDa HA ± 45 μg/mL BSA ( c ), 500 kDa HA ± 45 μ g/mL BSA ( d ). The empirical constants from the scaling equations were used to calculate the average distribution of apparent mesh sizes, ξ, using the correlation length relation (dashed lines = HA + PRG4, solid lines = HA)

    Techniques Used:

    Tracer diffusion coefficients of FITC-dextran (2000 kDa) through 1500 kDa HA solutions ±450 μg/ml BSA (∆ for HA + BSA, ● for HA) ( a ), 500 kDa HA solutions ±450 μg/ml BSA ( b ); 1500 kDa HA solutions ±45 μg/ml BSA ( c ), 500 kDa HA solutions ±45 μg/ml BSA ( d ). Data points are fit to the universal scaling equation (dashed lines = HA + BSA, solid lines = HA). At 450 μg/ml BSA, in both 1500 and 500 kDa HA ( a , b ) the diffusion of the tracer was significantly affected by HA concentration (both p
    Figure Legend Snippet: Tracer diffusion coefficients of FITC-dextran (2000 kDa) through 1500 kDa HA solutions ±450 μg/ml BSA (∆ for HA + BSA, ● for HA) ( a ), 500 kDa HA solutions ±450 μg/ml BSA ( b ); 1500 kDa HA solutions ±45 μg/ml BSA ( c ), 500 kDa HA solutions ±45 μg/ml BSA ( d ). Data points are fit to the universal scaling equation (dashed lines = HA + BSA, solid lines = HA). At 450 μg/ml BSA, in both 1500 and 500 kDa HA ( a , b ) the diffusion of the tracer was significantly affected by HA concentration (both p

    Techniques Used: Diffusion-based Assay, Concentration Assay

    23) Product Images from "Akt Inhibition Promotes ABCA1-Mediated Cholesterol Efflux to ApoA-I through Suppressing mTORC1"

    Article Title: Akt Inhibition Promotes ABCA1-Mediated Cholesterol Efflux to ApoA-I through Suppressing mTORC1

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0113789

    Akt inhibition by LY294002 or Akt1/2 also enhances cholesterol efflux to apoA-I from ABCA1-expressing BHK cells. A ) BHK cells were induced as in Fig. 1 and then incubated with LY294002 (200 µM) for 2 h. Cells were then lysed and analysed for ABCA1, phosphorylated Akt (p-Akt) and total Akt by Western-blotting. Hsp70 was also blotted as loading control. B C ) BHK cells were labeled with [ 3 H] cholesterol and induced with 10 nM mifepristone overnight. Cholesterol efflux was measured after 2 h incubation with BSA (1 mg/ml) or BSA plus apoA-I (5 µg/ml). Some of cells were also incubated with indicated doses of LY294002 ( B ) or Akt1/2 ( C ), in addition to apoA-I, during 2 h efflux period. Results are presented as the average of triplicate wells with standard deviation and representative of more than three independent experiments. *** P
    Figure Legend Snippet: Akt inhibition by LY294002 or Akt1/2 also enhances cholesterol efflux to apoA-I from ABCA1-expressing BHK cells. A ) BHK cells were induced as in Fig. 1 and then incubated with LY294002 (200 µM) for 2 h. Cells were then lysed and analysed for ABCA1, phosphorylated Akt (p-Akt) and total Akt by Western-blotting. Hsp70 was also blotted as loading control. B C ) BHK cells were labeled with [ 3 H] cholesterol and induced with 10 nM mifepristone overnight. Cholesterol efflux was measured after 2 h incubation with BSA (1 mg/ml) or BSA plus apoA-I (5 µg/ml). Some of cells were also incubated with indicated doses of LY294002 ( B ) or Akt1/2 ( C ), in addition to apoA-I, during 2 h efflux period. Results are presented as the average of triplicate wells with standard deviation and representative of more than three independent experiments. *** P

    Techniques Used: Inhibition, Expressing, Incubation, Western Blot, Labeling, Standard Deviation

    Akt inhibition by DEBC enhances cholesterol efflux to apoA-I specifically from ABCA1-expressing BHK cells. A ) BHK-ABCA1 cells were induced with mifepristone (10 nM) overnight and then incubated with indicated doses of DEBC for 2 h. Cells were then lysed and Western-blotted for ABCA1, phosphorylated Akt (p-Akt) and total Akt. Hsp70 was also blotted as loading control. B ) BHK-ABCA1 cells were labeled with [ 3 H] cholesterol and induced overnight as above. After 2 h incubation with BSA (1 mg/ml) or BSA plus apoA-I (5 µg/ml), cholesterol efflux was measured as described in the Methods section. Some of the cells were also incubated with indicated doses of DEBC, in addition to apoA-I, during 2 h efflux period. C ) BHK-ABCA1 and BHK-A937V cells were induced with mifepristone (10 nM) overnight. 2 h Cholesterol efflux was measured as above either with or without DEBC (25 µM). Results are presented as the average of triplicate wells with standard deviation and representative of more than three independent experiments. *** P
    Figure Legend Snippet: Akt inhibition by DEBC enhances cholesterol efflux to apoA-I specifically from ABCA1-expressing BHK cells. A ) BHK-ABCA1 cells were induced with mifepristone (10 nM) overnight and then incubated with indicated doses of DEBC for 2 h. Cells were then lysed and Western-blotted for ABCA1, phosphorylated Akt (p-Akt) and total Akt. Hsp70 was also blotted as loading control. B ) BHK-ABCA1 cells were labeled with [ 3 H] cholesterol and induced overnight as above. After 2 h incubation with BSA (1 mg/ml) or BSA plus apoA-I (5 µg/ml), cholesterol efflux was measured as described in the Methods section. Some of the cells were also incubated with indicated doses of DEBC, in addition to apoA-I, during 2 h efflux period. C ) BHK-ABCA1 and BHK-A937V cells were induced with mifepristone (10 nM) overnight. 2 h Cholesterol efflux was measured as above either with or without DEBC (25 µM). Results are presented as the average of triplicate wells with standard deviation and representative of more than three independent experiments. *** P

    Techniques Used: Inhibition, Expressing, Incubation, Western Blot, Labeling, Standard Deviation

    24) Product Images from "Starch-poly-?-caprolactone Microparticles Reduce the Needed Amount of BMP-2"

    Article Title: Starch-poly-?-caprolactone Microparticles Reduce the Needed Amount of BMP-2

    Journal: Clinical Orthopaedics and Related Research

    doi: 10.1007/s11999-009-0954-z

    A graph shows ALP activity in C2C12 cells, as determined using pNP assay. Controls include unloaded SPCL microparticles (SPCL MP), BSA/BMP-2 (2 mg/100 ng per mL), and BMP-2 (100 ng/mL) or DEX (10 −8 mol/L) solution. Samples include BMP-2- and DEX-loaded microparticles incubated directly with the cells (1–10 mg/mL). The graph suggests bioactivity is maintained and there is a difference in osteogenetic potential between DEX and BMP-2. Values are mean ± standard deviation (n = 3). Each pair of values compared is indicated when compared to unloaded SPCL microparticles, to negative control (DMEM) (**), and between a pair of controls or samples (horizontal bars).
    Figure Legend Snippet: A graph shows ALP activity in C2C12 cells, as determined using pNP assay. Controls include unloaded SPCL microparticles (SPCL MP), BSA/BMP-2 (2 mg/100 ng per mL), and BMP-2 (100 ng/mL) or DEX (10 −8 mol/L) solution. Samples include BMP-2- and DEX-loaded microparticles incubated directly with the cells (1–10 mg/mL). The graph suggests bioactivity is maintained and there is a difference in osteogenetic potential between DEX and BMP-2. Values are mean ± standard deviation (n = 3). Each pair of values compared is indicated when compared to unloaded SPCL microparticles, to negative control (DMEM) (**), and between a pair of controls or samples (horizontal bars).

    Techniques Used: ALP Assay, Activity Assay, Incubation, Standard Deviation, Negative Control

    Graphs show OCN promoter activity, as determined by luciferase activity, in C2C12 cells after administration of ( A ) BMP-2 or ( B ) DEX. The luciferase gene in the transfected vector is driven by the OCN promoter. Luciferase activity is measured after administration of luciferin by photon emission intensity. Controls include culture medium only (DMEM), BSA/BMP-2 (2 mg/100 ng per mL), BMP-2 (100 ng/mL), or DEX (10 −8 mol/L) solutions. Samples include supernatants from the in vitro release of BMP-2 and DEX after 1, 5, and 10 days in PBS and BMP-2- and DEX-loaded microparticles incubated directly with the cells (5 and 10 mg/mL). In addition, Transwell ® experiments using DEX-loaded microparticles (10 mg/mL) are presented for comparison, representing the released fraction without direct contact. These graphs show bioactivity of the drugs is maintained. Values are mean ± standard deviation. * Indicates the comparison to the negative control (DMEM), ** indicates the comparison to the positive control (BMP-2 or DEX solutions). Comparisons with p values between the tested samples are indicated by horizontal bars and vertical ticks.
    Figure Legend Snippet: Graphs show OCN promoter activity, as determined by luciferase activity, in C2C12 cells after administration of ( A ) BMP-2 or ( B ) DEX. The luciferase gene in the transfected vector is driven by the OCN promoter. Luciferase activity is measured after administration of luciferin by photon emission intensity. Controls include culture medium only (DMEM), BSA/BMP-2 (2 mg/100 ng per mL), BMP-2 (100 ng/mL), or DEX (10 −8 mol/L) solutions. Samples include supernatants from the in vitro release of BMP-2 and DEX after 1, 5, and 10 days in PBS and BMP-2- and DEX-loaded microparticles incubated directly with the cells (5 and 10 mg/mL). In addition, Transwell ® experiments using DEX-loaded microparticles (10 mg/mL) are presented for comparison, representing the released fraction without direct contact. These graphs show bioactivity of the drugs is maintained. Values are mean ± standard deviation. * Indicates the comparison to the negative control (DMEM), ** indicates the comparison to the positive control (BMP-2 or DEX solutions). Comparisons with p values between the tested samples are indicated by horizontal bars and vertical ticks.

    Techniques Used: Activity Assay, Luciferase, Transfection, Plasmid Preparation, In Vitro, Incubation, Standard Deviation, Negative Control, Positive Control

    25) Product Images from "Development of novel HDL-mimicking α-tocopherol-coated nanoparticles to encapsulate nerve growth factor and evaluation of biodistribution"

    Article Title: Development of novel HDL-mimicking α-tocopherol-coated nanoparticles to encapsulate nerve growth factor and evaluation of biodistribution

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

    doi: 10.1016/j.ejpb.2016.08.005

    In vitro release profiles of free NGF and NGF NPs in 5% BSA-PBS solution (pH 7). Data are presented as the mean ± SD (n=4).
    Figure Legend Snippet: In vitro release profiles of free NGF and NGF NPs in 5% BSA-PBS solution (pH 7). Data are presented as the mean ± SD (n=4).

    Techniques Used: In Vitro

    26) Product Images from "A Rapid Approach for Fabricating Boronic Acid-Functionalized Plates for On-Probe Detection of Glycoprotein and Glycopeptide"

    Article Title: A Rapid Approach for Fabricating Boronic Acid-Functionalized Plates for On-Probe Detection of Glycoprotein and Glycopeptide

    Journal: Mass Spectrometry

    doi: 10.5702/massspectrometry.S0063

    Fig. 4. MALDI-TOF analysis of (a) a mixture of 100 ng BSA /100 ng HRP and (b) a mixture of 1 μg BSA /100 ng HRP. Upper panel: before BP-plate enrichment. Lower panel: after BP-plate enrichment.
    Figure Legend Snippet: Fig. 4. MALDI-TOF analysis of (a) a mixture of 100 ng BSA /100 ng HRP and (b) a mixture of 1 μg BSA /100 ng HRP. Upper panel: before BP-plate enrichment. Lower panel: after BP-plate enrichment.

    Techniques Used:

    27) Product Images from "In vivo function of airway epithelial TLR2 in host defense against bacterial infection"

    Article Title: In vivo function of airway epithelial TLR2 in host defense against bacterial infection

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    doi: 10.1152/ajplung.00336.2010

    Human LTF protein dose-dependently reduces lung bacterial load in Mp-infected TLR2 −/− mice. TLR2 −/− mice were intranasally inoculated with purified LTF protein from human milk or bovine serum albumin (BSA) 30 min after
    Figure Legend Snippet: Human LTF protein dose-dependently reduces lung bacterial load in Mp-infected TLR2 −/− mice. TLR2 −/− mice were intranasally inoculated with purified LTF protein from human milk or bovine serum albumin (BSA) 30 min after

    Techniques Used: Infection, Mouse Assay, Purification

    Human LTF protein directly inhibits Mp growth in vitro. Mp was incubated with purified human LTF protein from milk at various concentrations or BSA in a 96-well tissue culture plate for 2 h. Mp levels in the supernatants were quantified by culture. Values
    Figure Legend Snippet: Human LTF protein directly inhibits Mp growth in vitro. Mp was incubated with purified human LTF protein from milk at various concentrations or BSA in a 96-well tissue culture plate for 2 h. Mp levels in the supernatants were quantified by culture. Values

    Techniques Used: In Vitro, Incubation, Purification

    28) Product Images from "Screening for Oxidative Stress Elicited by Engineered Nanomaterials: Evaluation of Acellular DCFH Assay"

    Article Title: Screening for Oxidative Stress Elicited by Engineered Nanomaterials: Evaluation of Acellular DCFH Assay

    Journal: Dose-Response

    doi: 10.2203/dose-response.10-036.Pal

    DCFH ROS generation of 19 ENMs in 1wt.%BSA/0.9wt. % NaCl aq dispersed by cup sonication. Only 4 of the 19 ENMs were positive (95% confidence interval above blank value denoted with the red line), 13 were negative and two were inconclusive (MWCNT_L, nano
    Figure Legend Snippet: DCFH ROS generation of 19 ENMs in 1wt.%BSA/0.9wt. % NaCl aq dispersed by cup sonication. Only 4 of the 19 ENMs were positive (95% confidence interval above blank value denoted with the red line), 13 were negative and two were inconclusive (MWCNT_L, nano

    Techniques Used: Sonication

    DCFH ROS generation of 19 ENMs in 1wt.%BSA/0.9wt.% NaCl dispersed by probe sonication. Only 3 of the 19 ENMs were positive (95% confidence interval above blank value denoted with the red line), 12 were negative and four were inconclusive (MWCNT_L, MWCNT_S,
    Figure Legend Snippet: DCFH ROS generation of 19 ENMs in 1wt.%BSA/0.9wt.% NaCl dispersed by probe sonication. Only 3 of the 19 ENMs were positive (95% confidence interval above blank value denoted with the red line), 12 were negative and four were inconclusive (MWCNT_L, MWCNT_S,

    Techniques Used: Sonication

    29) Product Images from "Receptor-Binding Properties of a Soluble Form of Human Cytomegalovirus Glycoprotein B"

    Article Title: Receptor-Binding Properties of a Soluble Form of Human Cytomegalovirus Glycoprotein B

    Journal: Journal of Virology

    doi:

    HCMV infection is decreased in the presence of gB-S. IF monolayers cultured on glass coverslips in a 12-well plate were chilled to 4°C. Increasing concentrations of nonradiolabeled gB-S (□), BSA (⧫), or 10 μg of heparin per ml were allowed to incubate with the cells for 60 min at 4°C. Virus was added to the cells (MOI = 0.1) and allowed to absorb for 90 min at 4°C. After a 30-min temperature shift to 37°C, a low-pH citrate buffer was added to inactivate any extracellular virus. At 24 h postinfection, immunofluorescence staining was performed with a rabbit anti-IE antibody followed by the secondary goat anti-rabbit–fluorescein conjugate in combination with Hoechst dye. Experiments for all data points were performed in duplicate, and a minimum of 500 cells per coverslip were scored. Bars represent standard deviations.
    Figure Legend Snippet: HCMV infection is decreased in the presence of gB-S. IF monolayers cultured on glass coverslips in a 12-well plate were chilled to 4°C. Increasing concentrations of nonradiolabeled gB-S (□), BSA (⧫), or 10 μg of heparin per ml were allowed to incubate with the cells for 60 min at 4°C. Virus was added to the cells (MOI = 0.1) and allowed to absorb for 90 min at 4°C. After a 30-min temperature shift to 37°C, a low-pH citrate buffer was added to inactivate any extracellular virus. At 24 h postinfection, immunofluorescence staining was performed with a rabbit anti-IE antibody followed by the secondary goat anti-rabbit–fluorescein conjugate in combination with Hoechst dye. Experiments for all data points were performed in duplicate, and a minimum of 500 cells per coverslip were scored. Bars represent standard deviations.

    Techniques Used: Infection, Cell Culture, Immunofluorescence, Staining

    30) Product Images from "An efficient method for FITC labelling of proteins using tandem affinity purification"

    Article Title: An efficient method for FITC labelling of proteins using tandem affinity purification

    Journal: Bioscience Reports

    doi: 10.1042/BSR20181764

    Protease assay with trypsin using FITC Pea15 as a substrate Increase in fluorescence of unquenched FITC was recorded at 485 nm excitation and 535 nm emission wavelengths. BSA has been used as negative control.
    Figure Legend Snippet: Protease assay with trypsin using FITC Pea15 as a substrate Increase in fluorescence of unquenched FITC was recorded at 485 nm excitation and 535 nm emission wavelengths. BSA has been used as negative control.

    Techniques Used: Protease Assay, Fluorescence, Negative Control

    31) Product Images from "Scavenging of reactive oxygen species induced by hyperthermia in biological fluid"

    Article Title: Scavenging of reactive oxygen species induced by hyperthermia in biological fluid

    Journal: Journal of Clinical Biochemistry and Nutrition

    doi: 10.3164/jcbn.13-61

    Reduction profile of TEMPOL in reaction mixture containing biological concentration of ascorbic acid and BSA. A reaction mixture containing 0.1 mM TEMPOL, 1 mM GSH, 4% BSA, and various concentrations of ascorbic acid (gray squares: 0.03 mM, black squares: 0.04 mM) was prepared with 100 mM phosphate buffer (pH 7). Experiments were performed at 44°C.
    Figure Legend Snippet: Reduction profile of TEMPOL in reaction mixture containing biological concentration of ascorbic acid and BSA. A reaction mixture containing 0.1 mM TEMPOL, 1 mM GSH, 4% BSA, and various concentrations of ascorbic acid (gray squares: 0.03 mM, black squares: 0.04 mM) was prepared with 100 mM phosphate buffer (pH 7). Experiments were performed at 44°C.

    Techniques Used: Concentration Assay

    Suppression of temperature- and GSH-dependent reduction of TEMPOL by bovine serum albumin (BSA). A reaction mixture containing 0.1 mM TEMPOL, 1 mM GSH, and various concentrations of BSA was prepared with 100 mM phosphate buffer (pH 7). The reaction mixture was incubated at (A) 37°C or (B) 44°C. Reduction of TEMPOL in the reaction mixture containing BSA was suppressed concentration dependently. 0.5% BSA was sufficient to suppress the reduction of TEMPOL at 37°C but not at 44°C.
    Figure Legend Snippet: Suppression of temperature- and GSH-dependent reduction of TEMPOL by bovine serum albumin (BSA). A reaction mixture containing 0.1 mM TEMPOL, 1 mM GSH, and various concentrations of BSA was prepared with 100 mM phosphate buffer (pH 7). The reaction mixture was incubated at (A) 37°C or (B) 44°C. Reduction of TEMPOL in the reaction mixture containing BSA was suppressed concentration dependently. 0.5% BSA was sufficient to suppress the reduction of TEMPOL at 37°C but not at 44°C.

    Techniques Used: Incubation, Concentration Assay

    32) Product Images from "Amplified voltammetric detection of glycoproteins using 4-mercaptophenylboronic acid/biotin-modified multifunctional gold nanoparticles as labels"

    Article Title: Amplified voltammetric detection of glycoproteins using 4-mercaptophenylboronic acid/biotin-modified multifunctional gold nanoparticles as labels

    Journal: International Journal of Nanomedicine

    doi: 10.2147/IJN.S62343

    ( A ) Electrochemical impedance spectroscopy of Au (curve a), Au/aptamers (curve b), Au/aptamers/MCH/BSA (curve c), Au/aptamers/MCH/BSA/rHuEPO (curve d), and Au/aptamers/MCH/BSA/rHuEPO/MBA-biotin-AuNPs (curve e) electrodes in [Fe(CN) 6 ] 3−/4− . ( B ) Cyclic voltammograms of the aptamer-covered electrode with (black curve) and without (red curve) the capture of rHuEPO, followed by the attachment of MBA-biotin-AuNPs as well as SA-ALP for the generation of p-AP. Blue curve corresponds to that after the capture of rHuEPO and the treatment with biotin-AuNPs in place of MBA-biotin-AuNPs. The concentration of rHuEPO was 10 pmol L −1 . The arrow indicates the scan direction. Abbreviations: biotin-AuNP, biotin-modified gold nanoparticle; BSA, bovine serum albumin; MBA-biotin-AuNP, 4-mercaptophenylboronic acid/biotin-modified gold nanoparticle; MCH, 6-mercapto-1-hexanol; p-AP, p-aminophenol; Q, a constant phase element; Ret, electron-transfer resistance; rHuEPO, recombinant human erythropoietin; Rs, resistance between working and reference electrodes; SA-ALP, streptavidin-conjugated alkaline phosphatase; Zw, Warburg impedance.
    Figure Legend Snippet: ( A ) Electrochemical impedance spectroscopy of Au (curve a), Au/aptamers (curve b), Au/aptamers/MCH/BSA (curve c), Au/aptamers/MCH/BSA/rHuEPO (curve d), and Au/aptamers/MCH/BSA/rHuEPO/MBA-biotin-AuNPs (curve e) electrodes in [Fe(CN) 6 ] 3−/4− . ( B ) Cyclic voltammograms of the aptamer-covered electrode with (black curve) and without (red curve) the capture of rHuEPO, followed by the attachment of MBA-biotin-AuNPs as well as SA-ALP for the generation of p-AP. Blue curve corresponds to that after the capture of rHuEPO and the treatment with biotin-AuNPs in place of MBA-biotin-AuNPs. The concentration of rHuEPO was 10 pmol L −1 . The arrow indicates the scan direction. Abbreviations: biotin-AuNP, biotin-modified gold nanoparticle; BSA, bovine serum albumin; MBA-biotin-AuNP, 4-mercaptophenylboronic acid/biotin-modified gold nanoparticle; MCH, 6-mercapto-1-hexanol; p-AP, p-aminophenol; Q, a constant phase element; Ret, electron-transfer resistance; rHuEPO, recombinant human erythropoietin; Rs, resistance between working and reference electrodes; SA-ALP, streptavidin-conjugated alkaline phosphatase; Zw, Warburg impedance.

    Techniques Used: Impedance Spectroscopy, ALP Assay, Concentration Assay, Modification, Recombinant

    Schematic illustration of the method for rHuEOP detection by MBA-biotin-AuNPs as labels. Abbreviations: BSA, bovine serum albumin; MBA-biotin-AuNP, 4-mercaptophenylboronic acid/biotin-modified gold nanoparticle; MCH, 6-mercapto-1-hexanol; p-AP, p-aminophenol; p-APP, p-aminophenyl phosphate; rHUEPO, recombinant human erythropoietin; SA-ALP, streptavidin-conjugated alkaline phosphatase.
    Figure Legend Snippet: Schematic illustration of the method for rHuEOP detection by MBA-biotin-AuNPs as labels. Abbreviations: BSA, bovine serum albumin; MBA-biotin-AuNP, 4-mercaptophenylboronic acid/biotin-modified gold nanoparticle; MCH, 6-mercapto-1-hexanol; p-AP, p-aminophenol; p-APP, p-aminophenyl phosphate; rHUEPO, recombinant human erythropoietin; SA-ALP, streptavidin-conjugated alkaline phosphatase.

    Techniques Used: Modification, Recombinant, ALP Assay

    33) Product Images from "Synthesis of Water-Dispersed Ferrecene/Phenylboronic Acid-Modified Bifunctional Gold Nanoparticles and the Application in Biosensing"

    Article Title: Synthesis of Water-Dispersed Ferrecene/Phenylboronic Acid-Modified Bifunctional Gold Nanoparticles and the Application in Biosensing

    Journal: Materials

    doi: 10.3390/ma7085554

    ( A ) The fits with the Randles equivalent circuit; ( B ) electrochemical impedance spectroscopy (EIS) of bare (black curve), biotin-covered (red curve), biotin/MCH/BSA-covered (blue curve), and biotin/MCH/BSA/avidin-covered (olive curve) gold electrode; ( C ) CVs of the biotin/MCH/BSA/avidin-covered electrode before (black curve) and after (red curve) incubation with FBA solution; ( D ) CVs of the biotin/MCH/BSA-covered electrode with (black curve) and without (red curve) the capture of avidin, followed by the attachment of Fc–MBA–AuNPs. The blue curve in panel D corresponds to that with streptavidin in place of avidin. The concentration of avidin was 157 pM, and the arrow indicates the scan direction.
    Figure Legend Snippet: ( A ) The fits with the Randles equivalent circuit; ( B ) electrochemical impedance spectroscopy (EIS) of bare (black curve), biotin-covered (red curve), biotin/MCH/BSA-covered (blue curve), and biotin/MCH/BSA/avidin-covered (olive curve) gold electrode; ( C ) CVs of the biotin/MCH/BSA/avidin-covered electrode before (black curve) and after (red curve) incubation with FBA solution; ( D ) CVs of the biotin/MCH/BSA-covered electrode with (black curve) and without (red curve) the capture of avidin, followed by the attachment of Fc–MBA–AuNPs. The blue curve in panel D corresponds to that with streptavidin in place of avidin. The concentration of avidin was 157 pM, and the arrow indicates the scan direction.

    Techniques Used: Impedance Spectroscopy, Avidin-Biotin Assay, Incubation, Concentration Assay

    34) Product Images from "Misoprostol Inhibits Equine Neutrophil Adhesion, Migration, and Respiratory Burst in an In Vitro Model of Inflammation"

    Article Title: Misoprostol Inhibits Equine Neutrophil Adhesion, Migration, and Respiratory Burst in an In Vitro Model of Inflammation

    Journal: Frontiers in Veterinary Science

    doi: 10.3389/fvets.2017.00159

    Misoprostol pretreatment inhibits LTB 4 - but not immune complex (IC)- or PMA-induced equine neutrophil adhesion. Calcein AM-labeled equine neutrophils were pretreated with varying concentrations of misoprostol, dibutyryl cyclic-AMP (db-cAMP), or the vehicle control (VC) for each inhibitor (Hank’s balanced salt solution). Preincubation with known inhibitors of neutrophil adhesion—wortmannin (for IC) or staurosporine (for LTB 4 and PMA)—were utilized as a positive control for inhibition. Neutrophils were stimulated with the following stimulants or vehicles: (A) 10 nM LTB 4 (or EtOH vehicle), (B) 100 ng/ml PMA (or DMSO vehicle), (C) 5 µg immobilized IC (or 5% BSA vehicle). Cells were stimulated with LTB 4 for 75 s, or PMA and IC for 30 min. Initial fluorescence readings were taken prior to removal of non-adherent neutrophils via multiple washing steps including two washes for LTB 4 , and three washes for IC and PMA. Percent adhesion was calculated as the final fluorescence reading versus the initial fluorescence reading in each well. Data are expressed as mean% adhesion ± SEM. ** p
    Figure Legend Snippet: Misoprostol pretreatment inhibits LTB 4 - but not immune complex (IC)- or PMA-induced equine neutrophil adhesion. Calcein AM-labeled equine neutrophils were pretreated with varying concentrations of misoprostol, dibutyryl cyclic-AMP (db-cAMP), or the vehicle control (VC) for each inhibitor (Hank’s balanced salt solution). Preincubation with known inhibitors of neutrophil adhesion—wortmannin (for IC) or staurosporine (for LTB 4 and PMA)—were utilized as a positive control for inhibition. Neutrophils were stimulated with the following stimulants or vehicles: (A) 10 nM LTB 4 (or EtOH vehicle), (B) 100 ng/ml PMA (or DMSO vehicle), (C) 5 µg immobilized IC (or 5% BSA vehicle). Cells were stimulated with LTB 4 for 75 s, or PMA and IC for 30 min. Initial fluorescence readings were taken prior to removal of non-adherent neutrophils via multiple washing steps including two washes for LTB 4 , and three washes for IC and PMA. Percent adhesion was calculated as the final fluorescence reading versus the initial fluorescence reading in each well. Data are expressed as mean% adhesion ± SEM. ** p

    Techniques Used: Labeling, Positive Control, Inhibition, Fluorescence

    35) Product Images from "Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction"

    Article Title: Design and biological activities of novel inhibitory peptides for SARS-CoV spike protein and angiotensin-converting enzyme 2 interaction

    Journal: Antiviral Research

    doi: 10.1016/j.antiviral.2005.10.005

    Inhibitory effects of peptides on the SARS-CoV S protein and ACE2 interaction by competitive biotinylated ELISA. Biotin-labeled S protein (1 nmol) was mixed with 10 nmol of synthetic peptides or BSA and incubated at 37 °C with shaking. After a 2-h incubation, the mixtures were added to wells, which were coated with 1 ng of ACE2 and incubated at 37 °C for 1 h. Following three washes, peroxidase-conjugated avidin and chromatic substrate were sequentially added. The absorbance was read at 405 nm in an ELISA plate reader. The results are expressed as inhibition described in Section 2 . Values are mean ± standard error of six independent assays. ** p
    Figure Legend Snippet: Inhibitory effects of peptides on the SARS-CoV S protein and ACE2 interaction by competitive biotinylated ELISA. Biotin-labeled S protein (1 nmol) was mixed with 10 nmol of synthetic peptides or BSA and incubated at 37 °C with shaking. After a 2-h incubation, the mixtures were added to wells, which were coated with 1 ng of ACE2 and incubated at 37 °C for 1 h. Following three washes, peroxidase-conjugated avidin and chromatic substrate were sequentially added. The absorbance was read at 405 nm in an ELISA plate reader. The results are expressed as inhibition described in Section 2 . Values are mean ± standard error of six independent assays. ** p

    Techniques Used: Enzyme-linked Immunosorbent Assay, Labeling, Incubation, Avidin-Biotin Assay, Inhibition

    Analysis of SARS-CoV S protein and ACE2 interaction by biotinylated ELISA. The wells were coated with 1 ng of ACE2 and challenged with various amounts of biotin-labeled S protein (●), biotin-labeled BSA (○) or biotin (▴). Following three washes, peroxidase-conjugated avidin and chromatic substrate were sequentially added. The absorbance was read at 405 nm in an ELISA plate reader. Values are mean ± standard error of four independent assays.
    Figure Legend Snippet: Analysis of SARS-CoV S protein and ACE2 interaction by biotinylated ELISA. The wells were coated with 1 ng of ACE2 and challenged with various amounts of biotin-labeled S protein (●), biotin-labeled BSA (○) or biotin (▴). Following three washes, peroxidase-conjugated avidin and chromatic substrate were sequentially added. The absorbance was read at 405 nm in an ELISA plate reader. Values are mean ± standard error of four independent assays.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Labeling, Avidin-Biotin Assay

    36) Product Images from "An Enzyme- and Label-Free Fluorescence Aptasensor for Detection of Thrombin Based on Graphene Oxide and G-Quadruplex"

    Article Title: An Enzyme- and Label-Free Fluorescence Aptasensor for Detection of Thrombin Based on Graphene Oxide and G-Quadruplex

    Journal: Sensors (Basel, Switzerland)

    doi: 10.3390/s19204424

    Selectivity evaluation of the biosensor for the detection of thrombin against other proteins of Lysozyme, Trypsase, lgG, BSA, and HSA. The concentration of the thrombin was 0.2 µM. However, the concentration of Lysozyme, Trypsase, lgG, BSA, and HSA was 2 µM. No thrombin or other proteins were used in the blank group. Inset: the changes in fluorescence intensity (F/F 0 ), F and F 0 , are the fluorescence intensities in the presence and absence of protein, respectively. The error bar was calculated in three independent experiments.
    Figure Legend Snippet: Selectivity evaluation of the biosensor for the detection of thrombin against other proteins of Lysozyme, Trypsase, lgG, BSA, and HSA. The concentration of the thrombin was 0.2 µM. However, the concentration of Lysozyme, Trypsase, lgG, BSA, and HSA was 2 µM. No thrombin or other proteins were used in the blank group. Inset: the changes in fluorescence intensity (F/F 0 ), F and F 0 , are the fluorescence intensities in the presence and absence of protein, respectively. The error bar was calculated in three independent experiments.

    Techniques Used: Concentration Assay, Fluorescence

    37) Product Images from "Development of Robust and Standardized Cantilever Sensors Based on Biotin/Neutravidin Coupling for Antibody Detection"

    Article Title: Development of Robust and Standardized Cantilever Sensors Based on Biotin/Neutravidin Coupling for Antibody Detection

    Journal: Sensors (Basel, Switzerland)

    doi: 10.3390/s130405273

    Specificity test of the biotinylated BSA layer on cantilevers to m-IgG. ( a ) The average absolute bending responses of different protein coated cantilevers upon injecting of m-IgG (red hatched area) displaying different binding affinity. ( b ) The average differential bending signal of BSA to m-IgG is evaluated by subtracting of the bending signal of bMBP to IgG.
    Figure Legend Snippet: Specificity test of the biotinylated BSA layer on cantilevers to m-IgG. ( a ) The average absolute bending responses of different protein coated cantilevers upon injecting of m-IgG (red hatched area) displaying different binding affinity. ( b ) The average differential bending signal of BSA to m-IgG is evaluated by subtracting of the bending signal of bMBP to IgG.

    Techniques Used: Binding Assay

    Schematics of cantilever functionalization: ( a ) gold-coated cantilevers were functionalized with a self-assembled monolayer of SH-C 11 -(PEG) 3 -biotin as a sensor to detect NeutrAvidin. Other cantilevers were coated with SH-C 11 -(PEG) 4 inert to NeutrAvidin serving as reference. ( b ) Subsequent functionalization with NeutrAvidin. ( c ) Adsorption of biotinylated BSA forms a multilayer for capturing antibodies. ( d ) Scheme depicting how antibodies are captured by the multilayer cantilever biosensor.
    Figure Legend Snippet: Schematics of cantilever functionalization: ( a ) gold-coated cantilevers were functionalized with a self-assembled monolayer of SH-C 11 -(PEG) 3 -biotin as a sensor to detect NeutrAvidin. Other cantilevers were coated with SH-C 11 -(PEG) 4 inert to NeutrAvidin serving as reference. ( b ) Subsequent functionalization with NeutrAvidin. ( c ) Adsorption of biotinylated BSA forms a multilayer for capturing antibodies. ( d ) Scheme depicting how antibodies are captured by the multilayer cantilever biosensor.

    Techniques Used: Adsorption

    38) Product Images from "Wound healing monitoring using near infrared fluorescent fibrinogen"

    Article Title: Wound healing monitoring using near infrared fluorescent fibrinogen

    Journal: Biomedical Optics Express

    doi: 10.1364/boe.1.000285

    (a) Plot of fluorescence intensity vs. time. The intensities were integrated from the wound individually. 8-12 wounds were inspected. The error bars describe the standard deviations of the intensity distribution. Solid lines represent the fluorescence changes for administration of the labels 1 hr after wound creation. Dashed lines are for administration of the labels 24 hrs after wound creation. Black and red: hFg. Blue and green: BSA. (b) and (c) are “Day 1” image (24 hrs after label administration) of the wound, for which the labels were injected into rat 24 hrs after wound creation. (b) is for hFg label. (c) is for BSA label.
    Figure Legend Snippet: (a) Plot of fluorescence intensity vs. time. The intensities were integrated from the wound individually. 8-12 wounds were inspected. The error bars describe the standard deviations of the intensity distribution. Solid lines represent the fluorescence changes for administration of the labels 1 hr after wound creation. Dashed lines are for administration of the labels 24 hrs after wound creation. Black and red: hFg. Blue and green: BSA. (b) and (c) are “Day 1” image (24 hrs after label administration) of the wound, for which the labels were injected into rat 24 hrs after wound creation. (b) is for hFg label. (c) is for BSA label.

    Techniques Used: Fluorescence, Injection

    SDS-PAGE gel images showing Coomassie blue staining (left panel) and NIR fluorescence (right panel) for the same gel. Lanes 1 and 6 are protein MW standards. Lane 2 is unlabeled hFg only. Three major bands (from top to bottom) represent α (63.5 kDa), β (56 kDa), and γ (47 kDa) chains, respectively. Lanes 3–5 and 7–9 are protein with NIR labels (3–5: hFG and 7–9: BSA) Lanes 3 and 7 have no TG2. Lanes 4 and 8 are incubated with TG2. Lanes 5 and 9 are incubated with both TG2 and EDTA. EDTA inhibits the cross-linking reaction of TG2.
    Figure Legend Snippet: SDS-PAGE gel images showing Coomassie blue staining (left panel) and NIR fluorescence (right panel) for the same gel. Lanes 1 and 6 are protein MW standards. Lane 2 is unlabeled hFg only. Three major bands (from top to bottom) represent α (63.5 kDa), β (56 kDa), and γ (47 kDa) chains, respectively. Lanes 3–5 and 7–9 are protein with NIR labels (3–5: hFG and 7–9: BSA) Lanes 3 and 7 have no TG2. Lanes 4 and 8 are incubated with TG2. Lanes 5 and 9 are incubated with both TG2 and EDTA. EDTA inhibits the cross-linking reaction of TG2.

    Techniques Used: SDS Page, Staining, Fluorescence, Incubation

    Wound images. (a) Typical “white light” and NIR fluorescence images. The images in (b) and (c) are the expanded time-lapse images of wound sites, showing hFg label and BSA label respectively. The Day 0 image was taken within 5 min of contrast injection. Day 1 was taken 24 hrs after injection, Day 2, 48 hours after injection, and so forth.
    Figure Legend Snippet: Wound images. (a) Typical “white light” and NIR fluorescence images. The images in (b) and (c) are the expanded time-lapse images of wound sites, showing hFg label and BSA label respectively. The Day 0 image was taken within 5 min of contrast injection. Day 1 was taken 24 hrs after injection, Day 2, 48 hours after injection, and so forth.

    Techniques Used: Fluorescence, Injection

    39) Product Images from "Ceramide 1-phosphate stimulates proliferation of C2C12 myoblasts"

    Article Title: Ceramide 1-phosphate stimulates proliferation of C2C12 myoblasts

    Journal: Biochimie

    doi: 10.1016/j.biochi.2011.09.009

    Effect of C1P on C2C12 myoblast differentiation (A) and apoptosis (B). A) Confluent C2C12 myoblasts were incubated in medium supplemented with 0.1% BSA for the indicated period of time in the absence (−) or in the presence (+) of 15 μM C1P. Upper panel: Western blot analysis of myogenic marker expression. The content of myogenin, myosin heavy chain (MHC), and caveolin-3 (cav-3) was analyzed in cell lysates (30 μg) by Western Blot analysis. Equally loaded protein was checked by expression of the nonmuscle-specific β isoform of actin. A blot representative of four independent experiments with analogous results is shown. The histograms represent band intensity of MHC, myogenin, and cav-3 normalized to β-actin and reported as mean ± SEM of four independent experiments, fold change over control (time 24 h, no addition) set as 1. The effect of C1P was statistically significant by Student’s t test (* P
    Figure Legend Snippet: Effect of C1P on C2C12 myoblast differentiation (A) and apoptosis (B). A) Confluent C2C12 myoblasts were incubated in medium supplemented with 0.1% BSA for the indicated period of time in the absence (−) or in the presence (+) of 15 μM C1P. Upper panel: Western blot analysis of myogenic marker expression. The content of myogenin, myosin heavy chain (MHC), and caveolin-3 (cav-3) was analyzed in cell lysates (30 μg) by Western Blot analysis. Equally loaded protein was checked by expression of the nonmuscle-specific β isoform of actin. A blot representative of four independent experiments with analogous results is shown. The histograms represent band intensity of MHC, myogenin, and cav-3 normalized to β-actin and reported as mean ± SEM of four independent experiments, fold change over control (time 24 h, no addition) set as 1. The effect of C1P was statistically significant by Student’s t test (* P

    Techniques Used: Incubation, Western Blot, Marker, Expressing

    40) Product Images from "Anandamide Induces Sperm Release from Oviductal Epithelia through Nitric Oxide Pathway in Bovines"

    Article Title: Anandamide Induces Sperm Release from Oviductal Epithelia through Nitric Oxide Pathway in Bovines

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0030671

    Participation of CB1 and TRPV1 in NO production during bull sperm capacitation by AEA. Sperm samples were incubated for 60 min at 38.5°C in 0.3% BSA sp-TALP containing 0.1 mM L-Arginine and 5 µM of DAF-FM diacetate and untreated (control) or treated with MetAEA (1.4 nM) and/or SR141716A (SR1: CB1 antagonist (0.1 nM)) or Capsazepine (CZP: TRPV1 antagonist (10 nM)). Spermatozoa were fixed and the fluorescent complex was measured by flow cytometry. Fluorescence data are expressed as mean fluorescence (percentage of control at 45 min incubation, control adjusted to 100%). Data are expressed as mean ± SEM (n = 5). a≠b, p
    Figure Legend Snippet: Participation of CB1 and TRPV1 in NO production during bull sperm capacitation by AEA. Sperm samples were incubated for 60 min at 38.5°C in 0.3% BSA sp-TALP containing 0.1 mM L-Arginine and 5 µM of DAF-FM diacetate and untreated (control) or treated with MetAEA (1.4 nM) and/or SR141716A (SR1: CB1 antagonist (0.1 nM)) or Capsazepine (CZP: TRPV1 antagonist (10 nM)). Spermatozoa were fixed and the fluorescent complex was measured by flow cytometry. Fluorescence data are expressed as mean fluorescence (percentage of control at 45 min incubation, control adjusted to 100%). Data are expressed as mean ± SEM (n = 5). a≠b, p

    Techniques Used: Incubation, Flow Cytometry, Cytometry, Fluorescence

    Determination of NO levels in bull spermatozoa. Sperm samples were incubated for 60 min at 38.5°C in 0.3% BSA sp-TALP containing 0.1 mM L-Arginine and 5 µM of DAF-FM diacetate and untreated (control) or treated with MetAEA (1.4 nM), MetAEA+L-NAME (1 µM). Spermatozoa were fixed and the fluorescent complex was measured by flow cytometry. A) A representative photograph showing fluorescence in spermatozoa, indicating the content of intracellular NO (Magnification, ×600); B) Fluorescence data are expressed as mean fluorescence (percentage of control at 45 min incubation, control adjusted to 100%). Data are expressed as mean ± SEM (n = 8). a≠b, p
    Figure Legend Snippet: Determination of NO levels in bull spermatozoa. Sperm samples were incubated for 60 min at 38.5°C in 0.3% BSA sp-TALP containing 0.1 mM L-Arginine and 5 µM of DAF-FM diacetate and untreated (control) or treated with MetAEA (1.4 nM), MetAEA+L-NAME (1 µM). Spermatozoa were fixed and the fluorescent complex was measured by flow cytometry. A) A representative photograph showing fluorescence in spermatozoa, indicating the content of intracellular NO (Magnification, ×600); B) Fluorescence data are expressed as mean fluorescence (percentage of control at 45 min incubation, control adjusted to 100%). Data are expressed as mean ± SEM (n = 8). a≠b, p

    Techniques Used: Incubation, Flow Cytometry, Cytometry, Fluorescence

    Assessment of participation of the nitrergic system on sperm release induced by anandamide. Sperm cells and BOEC were co-cultured and then incubated for 15 min with BSA-free sp-TALP alone (control), AEA (1 nM) or MetAEA (1.4 nM) and L-NAME (1 µM; NO synthase inhibitor) or Hemoglobin (Hb) (30 µg/ml; NO scavenger). Bars indicate the number of spermatozoa that remained attached to the monolayers and represent the mean ± S.E.M. of bound spermatozoa/0.11 mm 2 monolayer (n = 6), a≠b p
    Figure Legend Snippet: Assessment of participation of the nitrergic system on sperm release induced by anandamide. Sperm cells and BOEC were co-cultured and then incubated for 15 min with BSA-free sp-TALP alone (control), AEA (1 nM) or MetAEA (1.4 nM) and L-NAME (1 µM; NO synthase inhibitor) or Hemoglobin (Hb) (30 µg/ml; NO scavenger). Bars indicate the number of spermatozoa that remained attached to the monolayers and represent the mean ± S.E.M. of bound spermatozoa/0.11 mm 2 monolayer (n = 6), a≠b p

    Techniques Used: Cell Culture, Incubation

    Effect of L-NAME or Hemoglobin on bull sperm capacitation induced by AEA. Spermatozoa were incubated for 45 min at 38.5°C in 0.3% BSA sp-TALP medium with AEA (1 nM) and L-NAME (1 µM) or Hb (30 µg/ml). Bars indicate the percentage of capacitated spermatozoa (A: % pattern B of CTC; B: % acrosome reacted spermatozoa). A: Assessment of sperm capacitation by CTC; T0 and T45: 0.3% BSA sp-TALP at 0 and 45 min (control) incubation respectively (n = 6). B: Assessment of sperm capacitation by LPC-induced acrosome reaction (AR)-PSA-FITC. T45: 0.3% BSA sp-TALP (control). After capacitation, spermatozoa were incubated for 15 min either with or without LPC to induce AR. Bars show percentage of spermatozoa that underwent LPC-induced AR minus the percentage of spermatozoa that underwent spontaneous AR (n = 6). Data are expressed as mean ± SEM. a≠b, p
    Figure Legend Snippet: Effect of L-NAME or Hemoglobin on bull sperm capacitation induced by AEA. Spermatozoa were incubated for 45 min at 38.5°C in 0.3% BSA sp-TALP medium with AEA (1 nM) and L-NAME (1 µM) or Hb (30 µg/ml). Bars indicate the percentage of capacitated spermatozoa (A: % pattern B of CTC; B: % acrosome reacted spermatozoa). A: Assessment of sperm capacitation by CTC; T0 and T45: 0.3% BSA sp-TALP at 0 and 45 min (control) incubation respectively (n = 6). B: Assessment of sperm capacitation by LPC-induced acrosome reaction (AR)-PSA-FITC. T45: 0.3% BSA sp-TALP (control). After capacitation, spermatozoa were incubated for 15 min either with or without LPC to induce AR. Bars show percentage of spermatozoa that underwent LPC-induced AR minus the percentage of spermatozoa that underwent spontaneous AR (n = 6). Data are expressed as mean ± SEM. a≠b, p

    Techniques Used: Incubation

    Effect of L-NAME or Hemoglobin on bull sperm capacitation induced by MetAEA. Spermatozoa were incubated for 45 min at 38.5°C in 0.3% BSA sp-TALP medium with MetAEA (1.4 nM) and L-NAME (1 µM) or Hb (30 µg/ml). Bars indicate the percentage of capacitated spermatozoa (A: % pattern B of CTC; B: % acrosome reacted spermatozoa). A: Assessment of sperm capacitation by CTC; T0 and T45: 0.3% BSA sp-TALP at 0 and 45 min (control) incubation respectively (n = 6). B: Assessment of sperm capacitation by LPC-induced acrosome reaction (AR)-PSA-FITC. T45: 0.3% BSA sp-TALP (control). After capacitation, spermatozoa were incubated for 15 min either with or without LPC to induce AR. Bars show percentage of spermatozoa that underwent LPC-induced AR minus the percentage of spermatozoa that underwent spontaneous AR (n = 6). Data are expressed as mean ± SEM. a≠b, p
    Figure Legend Snippet: Effect of L-NAME or Hemoglobin on bull sperm capacitation induced by MetAEA. Spermatozoa were incubated for 45 min at 38.5°C in 0.3% BSA sp-TALP medium with MetAEA (1.4 nM) and L-NAME (1 µM) or Hb (30 µg/ml). Bars indicate the percentage of capacitated spermatozoa (A: % pattern B of CTC; B: % acrosome reacted spermatozoa). A: Assessment of sperm capacitation by CTC; T0 and T45: 0.3% BSA sp-TALP at 0 and 45 min (control) incubation respectively (n = 6). B: Assessment of sperm capacitation by LPC-induced acrosome reaction (AR)-PSA-FITC. T45: 0.3% BSA sp-TALP (control). After capacitation, spermatozoa were incubated for 15 min either with or without LPC to induce AR. Bars show percentage of spermatozoa that underwent LPC-induced AR minus the percentage of spermatozoa that underwent spontaneous AR (n = 6). Data are expressed as mean ± SEM. a≠b, p

    Techniques Used: Incubation

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  • 99
    Millipore fibronectin bovine plasma
    Lateral movement of actin bundles in fibroblasts on homogeneous substrates vs. disk-like patches. (A) Micrograph of a cell membrane-stained (DiI) fibroblast in the late spreading phase on a homogeneous <t>fibronectin</t> coated glass coverslip using TIRF microscopy (scale bar: 15 μm). (B) Time-lapse sequence of the red dashed region of interest in (A) (scale bar: 2 μm). (C) Phase contrast micrograph of a disk-shaped fibroblast (scale bar: 20 μm). Blue circle indicates the fibronectin patch on which the cell adhere. (D) Time-lapse sequence of the red solid region of interest in (C) . An actin bundle, which moves under angle α perpendicular to the cell membrane is highlighted by red arrows (scale bar: 5 μm). Blue arrowhead indicates an actin fold with their width b and distance from the cell membrane d .
    Fibronectin Bovine Plasma, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore bovine derived exosomes
    Pancreatic cancer-derived <t>exosomes</t> induce inflammation and fibrotic microenvironment formation in the liver IHC analysis and histopathological examination of macrophages (F4/80), hStCs (α-SMA), and neutrophils in liver metastatic niches of naïve mice and mice treated with PBS, Panc02 EXOs, or Panc02-H7 EXOs at 30d post-SOI (arrow shows neutrophils in liver) (A) . Representative histogram shows quantification of F4/80 + macrophages, α-SMA + hStCs, and neutrophils (B) . Identification of FN, S100A8, and S100A9 as inflammatory mediators, and collagen deposition in the liver metastatic niche (C) . Representative histogram shows FN and MTS quantification (D) . Representative histogram shows S100A8 and S100A9 quantification (E) . n=6/group.**P
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    92
    Millipore btx 1 bsa
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    Image Search Results


    Lateral movement of actin bundles in fibroblasts on homogeneous substrates vs. disk-like patches. (A) Micrograph of a cell membrane-stained (DiI) fibroblast in the late spreading phase on a homogeneous fibronectin coated glass coverslip using TIRF microscopy (scale bar: 15 μm). (B) Time-lapse sequence of the red dashed region of interest in (A) (scale bar: 2 μm). (C) Phase contrast micrograph of a disk-shaped fibroblast (scale bar: 20 μm). Blue circle indicates the fibronectin patch on which the cell adhere. (D) Time-lapse sequence of the red solid region of interest in (C) . An actin bundle, which moves under angle α perpendicular to the cell membrane is highlighted by red arrows (scale bar: 5 μm). Blue arrowhead indicates an actin fold with their width b and distance from the cell membrane d .

    Journal: Frontiers in Cell and Developmental Biology

    Article Title: Biomechanical Aspects of Actin Bundle Dynamics

    doi: 10.3389/fcell.2020.00422

    Figure Lengend Snippet: Lateral movement of actin bundles in fibroblasts on homogeneous substrates vs. disk-like patches. (A) Micrograph of a cell membrane-stained (DiI) fibroblast in the late spreading phase on a homogeneous fibronectin coated glass coverslip using TIRF microscopy (scale bar: 15 μm). (B) Time-lapse sequence of the red dashed region of interest in (A) (scale bar: 2 μm). (C) Phase contrast micrograph of a disk-shaped fibroblast (scale bar: 20 μm). Blue circle indicates the fibronectin patch on which the cell adhere. (D) Time-lapse sequence of the red solid region of interest in (C) . An actin bundle, which moves under angle α perpendicular to the cell membrane is highlighted by red arrows (scale bar: 5 μm). Blue arrowhead indicates an actin fold with their width b and distance from the cell membrane d .

    Article Snippet: We detected the time at which the effect of myosin X knock-down was maximal in cells on overall fibronectin-coated glass coverslips.

    Techniques: Staining, Microscopy, Sequencing

    Pancreatic cancer-derived exosomes induce inflammation and fibrotic microenvironment formation in the liver IHC analysis and histopathological examination of macrophages (F4/80), hStCs (α-SMA), and neutrophils in liver metastatic niches of naïve mice and mice treated with PBS, Panc02 EXOs, or Panc02-H7 EXOs at 30d post-SOI (arrow shows neutrophils in liver) (A) . Representative histogram shows quantification of F4/80 + macrophages, α-SMA + hStCs, and neutrophils (B) . Identification of FN, S100A8, and S100A9 as inflammatory mediators, and collagen deposition in the liver metastatic niche (C) . Representative histogram shows FN and MTS quantification (D) . Representative histogram shows S100A8 and S100A9 quantification (E) . n=6/group.**P

    Journal: Oncotarget

    Article Title: Pancreatic cancer-derived exosomes promote tumor metastasis and liver pre-metastatic niche formation

    doi: 10.18632/oncotarget.18831

    Figure Lengend Snippet: Pancreatic cancer-derived exosomes induce inflammation and fibrotic microenvironment formation in the liver IHC analysis and histopathological examination of macrophages (F4/80), hStCs (α-SMA), and neutrophils in liver metastatic niches of naïve mice and mice treated with PBS, Panc02 EXOs, or Panc02-H7 EXOs at 30d post-SOI (arrow shows neutrophils in liver) (A) . Representative histogram shows quantification of F4/80 + macrophages, α-SMA + hStCs, and neutrophils (B) . Identification of FN, S100A8, and S100A9 as inflammatory mediators, and collagen deposition in the liver metastatic niche (C) . Representative histogram shows FN and MTS quantification (D) . Representative histogram shows S100A8 and S100A9 quantification (E) . n=6/group.**P

    Article Snippet: Exosome isolation and purification Panc02 and Panc02-H7cells were cultured to 70% confluence in 75 cm2 flasks in RPMI-1640medium supplemented with 10% exosome-free FBS, which had been depleted of bovine-derived exosomes by ultracentrifugation for 70 min at 100,000 g, followed by filtration through a 0.2-μm filter from Millipore (MA, USA).

    Techniques: Derivative Assay, Immunohistochemistry, Mouse Assay

    iTRAQ labeling experimental design schematic Panc02 and Panc02-H7 cell-derived exosomes (EXO) were labeled with iTRAQ tags, 116 and 114, respectively, and another pair of biological replicates of the same sample was labeled with iTRAQ tags, 118 and 119, respectively.

    Journal: Oncotarget

    Article Title: Pancreatic cancer-derived exosomes promote tumor metastasis and liver pre-metastatic niche formation

    doi: 10.18632/oncotarget.18831

    Figure Lengend Snippet: iTRAQ labeling experimental design schematic Panc02 and Panc02-H7 cell-derived exosomes (EXO) were labeled with iTRAQ tags, 116 and 114, respectively, and another pair of biological replicates of the same sample was labeled with iTRAQ tags, 118 and 119, respectively.

    Article Snippet: Exosome isolation and purification Panc02 and Panc02-H7cells were cultured to 70% confluence in 75 cm2 flasks in RPMI-1640medium supplemented with 10% exosome-free FBS, which had been depleted of bovine-derived exosomes by ultracentrifugation for 70 min at 100,000 g, followed by filtration through a 0.2-μm filter from Millipore (MA, USA).

    Techniques: Labeling, Derivative Assay

    Panc02-H7-derived exosomes promote metastatis-related characteristics in vitro Panc02 cells tookup PKH67-labeled Panc02-H7EXOs. Numerous green fluorescently-labeled exosomes were observed inside cells after 5 h (400× magnification). (A) The MTT cell adhesion assay indicated that Panc02-H7 EXOs decrease Panc02 cell adhesion. (B) Wound-healing assays indicated that Panc02-H7 EXOs enhanced Panc02 cell migration (200×magnification). (C) Transwell chamber invasion assays showed that Panc02-H7 EXOs increased Panc02 cell invasion (200×magnification). (D) Western blotting indicated that Panc02-H7 EXOs increased Panc02 cell migration and invasion via CXCR4 and MMP-9 signaling. (E) n=3/group.*P

    Journal: Oncotarget

    Article Title: Pancreatic cancer-derived exosomes promote tumor metastasis and liver pre-metastatic niche formation

    doi: 10.18632/oncotarget.18831

    Figure Lengend Snippet: Panc02-H7-derived exosomes promote metastatis-related characteristics in vitro Panc02 cells tookup PKH67-labeled Panc02-H7EXOs. Numerous green fluorescently-labeled exosomes were observed inside cells after 5 h (400× magnification). (A) The MTT cell adhesion assay indicated that Panc02-H7 EXOs decrease Panc02 cell adhesion. (B) Wound-healing assays indicated that Panc02-H7 EXOs enhanced Panc02 cell migration (200×magnification). (C) Transwell chamber invasion assays showed that Panc02-H7 EXOs increased Panc02 cell invasion (200×magnification). (D) Western blotting indicated that Panc02-H7 EXOs increased Panc02 cell migration and invasion via CXCR4 and MMP-9 signaling. (E) n=3/group.*P

    Article Snippet: Exosome isolation and purification Panc02 and Panc02-H7cells were cultured to 70% confluence in 75 cm2 flasks in RPMI-1640medium supplemented with 10% exosome-free FBS, which had been depleted of bovine-derived exosomes by ultracentrifugation for 70 min at 100,000 g, followed by filtration through a 0.2-μm filter from Millipore (MA, USA).

    Techniques: Derivative Assay, In Vitro, Labeling, MTT Assay, Cell Adhesion Assay, Migration, Western Blot

    Pancreatic cancer-derived exosomes mediate liver pre-metastatic niche formation Confocal microscopy (lung, liver, spleen, brain) of PKH67-labeled Panc02 EXO and Panc02-H7 EXO tissue distribution (green) 24 hpi. (A) PKH-67-labeled liposomes served as controls (scale bar=100 μm). Histogram shows exosome tissue distribution quantification (n=5/group). CD45, p-Stat3, and CD11b IF staining in liver sections from controls (left) and mice treated with Panc02 EXOs(middle) or Panc02-H7 EXOs (right) for 12 d without tumor challenge. (B) Histogram shows infiltrating CD45 + cell quantification. FN and α-SMA IF staining in liver sections from controls (top) and mice treated with Panc02 EXOs(middle) or Panc02-H7 EXOs (bottom) for 12 d without tumor challenge. (C) Histogram shows infiltrating α-SMA + hStCs and FN expression quantification(400× magnification; n=5/group). Western blotting analysis showed upregulated S100A8 and S100A9 in livers treated with Panc02-H7-derived exosomes. Histogram shows expression of the three proteins in three groupsas determined by densitometric analysis (n=3/group). (D) Pancreatic cancer-derived exosomes induce MDSC accumulation in peripheral blood. (E) Representative flow cytometric plots (left) and quantification (right) of CD11b + GR1 + MDSCs (n=5/group). *P

    Journal: Oncotarget

    Article Title: Pancreatic cancer-derived exosomes promote tumor metastasis and liver pre-metastatic niche formation

    doi: 10.18632/oncotarget.18831

    Figure Lengend Snippet: Pancreatic cancer-derived exosomes mediate liver pre-metastatic niche formation Confocal microscopy (lung, liver, spleen, brain) of PKH67-labeled Panc02 EXO and Panc02-H7 EXO tissue distribution (green) 24 hpi. (A) PKH-67-labeled liposomes served as controls (scale bar=100 μm). Histogram shows exosome tissue distribution quantification (n=5/group). CD45, p-Stat3, and CD11b IF staining in liver sections from controls (left) and mice treated with Panc02 EXOs(middle) or Panc02-H7 EXOs (right) for 12 d without tumor challenge. (B) Histogram shows infiltrating CD45 + cell quantification. FN and α-SMA IF staining in liver sections from controls (top) and mice treated with Panc02 EXOs(middle) or Panc02-H7 EXOs (bottom) for 12 d without tumor challenge. (C) Histogram shows infiltrating α-SMA + hStCs and FN expression quantification(400× magnification; n=5/group). Western blotting analysis showed upregulated S100A8 and S100A9 in livers treated with Panc02-H7-derived exosomes. Histogram shows expression of the three proteins in three groupsas determined by densitometric analysis (n=3/group). (D) Pancreatic cancer-derived exosomes induce MDSC accumulation in peripheral blood. (E) Representative flow cytometric plots (left) and quantification (right) of CD11b + GR1 + MDSCs (n=5/group). *P

    Article Snippet: Exosome isolation and purification Panc02 and Panc02-H7cells were cultured to 70% confluence in 75 cm2 flasks in RPMI-1640medium supplemented with 10% exosome-free FBS, which had been depleted of bovine-derived exosomes by ultracentrifugation for 70 min at 100,000 g, followed by filtration through a 0.2-μm filter from Millipore (MA, USA).

    Techniques: Derivative Assay, Confocal Microscopy, Labeling, Staining, Mouse Assay, Expressing, Western Blot, Flow Cytometry

    Pancreatic cancer-derived exosomes promote tumor growth and metastasis Representative macro-anatomy and H E-stained images of Panc02-H7 EXO-treated mice 30 d post-SOI. (A) A yellow star marks primary tumor locations; arrows indicate metastatic sites in the peritoneal cavity (Aa) . Arrows showing lung micrometastasis (Ab) , pleura metastasis (Ac) , tumor invasion of the diaphragm (Ad) , metastasis to spleen (Ae) , tumor invasion of the adrenal gland (Af) , metastasis to the kidney (Ag) , tumor invasion of the small intestine (Ah) , micrometastasis of the liver(lower right shows enlarged image) (Ai) , and metastasis to lymph nodes (Aj) (magnification, 100×). Primary tumor volume in mice treated with PBS, Panc02 EXOs, orPanc02-H7 EXOs at 15 and 30 d post-SOI (B) . Number of micrometastases in mice treated with PBS, Panc02 EXOs, or Panc02-H7 EXOsat 15d post-SOI (n=6/group) (C) . *P

    Journal: Oncotarget

    Article Title: Pancreatic cancer-derived exosomes promote tumor metastasis and liver pre-metastatic niche formation

    doi: 10.18632/oncotarget.18831

    Figure Lengend Snippet: Pancreatic cancer-derived exosomes promote tumor growth and metastasis Representative macro-anatomy and H E-stained images of Panc02-H7 EXO-treated mice 30 d post-SOI. (A) A yellow star marks primary tumor locations; arrows indicate metastatic sites in the peritoneal cavity (Aa) . Arrows showing lung micrometastasis (Ab) , pleura metastasis (Ac) , tumor invasion of the diaphragm (Ad) , metastasis to spleen (Ae) , tumor invasion of the adrenal gland (Af) , metastasis to the kidney (Ag) , tumor invasion of the small intestine (Ah) , micrometastasis of the liver(lower right shows enlarged image) (Ai) , and metastasis to lymph nodes (Aj) (magnification, 100×). Primary tumor volume in mice treated with PBS, Panc02 EXOs, orPanc02-H7 EXOs at 15 and 30 d post-SOI (B) . Number of micrometastases in mice treated with PBS, Panc02 EXOs, or Panc02-H7 EXOsat 15d post-SOI (n=6/group) (C) . *P

    Article Snippet: Exosome isolation and purification Panc02 and Panc02-H7cells were cultured to 70% confluence in 75 cm2 flasks in RPMI-1640medium supplemented with 10% exosome-free FBS, which had been depleted of bovine-derived exosomes by ultracentrifugation for 70 min at 100,000 g, followed by filtration through a 0.2-μm filter from Millipore (MA, USA).

    Techniques: Derivative Assay, Staining, Mouse Assay

    Characterization of Panc02- and Panc02-H7-derived exosomes Exosome isolation and purification schematic. (A) Common exosome markers, including TSG101, CD9, and MHC-I, were detected in two exosomes. (B) Cytochrome c was detectable in two whole-cell lysates, but not in exosomes. Panc02 EXOs and Panc02-H7 EXOs were negatively stained with 3%phosphotungstic acid and viewed by TEM (scale bar=200 nm). (C) Total protein per million cells in two exosomes. (D) Panc02-H7EXOs expressed more total protein than Panc02 EXOs.(*P

    Journal: Oncotarget

    Article Title: Pancreatic cancer-derived exosomes promote tumor metastasis and liver pre-metastatic niche formation

    doi: 10.18632/oncotarget.18831

    Figure Lengend Snippet: Characterization of Panc02- and Panc02-H7-derived exosomes Exosome isolation and purification schematic. (A) Common exosome markers, including TSG101, CD9, and MHC-I, were detected in two exosomes. (B) Cytochrome c was detectable in two whole-cell lysates, but not in exosomes. Panc02 EXOs and Panc02-H7 EXOs were negatively stained with 3%phosphotungstic acid and viewed by TEM (scale bar=200 nm). (C) Total protein per million cells in two exosomes. (D) Panc02-H7EXOs expressed more total protein than Panc02 EXOs.(*P

    Article Snippet: Exosome isolation and purification Panc02 and Panc02-H7cells were cultured to 70% confluence in 75 cm2 flasks in RPMI-1640medium supplemented with 10% exosome-free FBS, which had been depleted of bovine-derived exosomes by ultracentrifugation for 70 min at 100,000 g, followed by filtration through a 0.2-μm filter from Millipore (MA, USA).

    Techniques: Derivative Assay, Isolation, Purification, Staining, Transmission Electron Microscopy

    Construction and characterization of colloidal gold strip test; ( A ) the description of strip test results. In the absence of BTX-1 in the sample solution, both two line exits on the control and test zone, indicating negative. Only one control line stands positive for enough toxin binding to the anti-BTX-1-BSA McAb. If no lines, or only the test line was red, it indicated invalid results; ( B ) cross-reactivity of the test strip with other toxins, such as OA, DA, BTX-2, BTX-3, TTX, CTX, STX; ( C ) the detection limit of colloidal gold strip test for BTX-1; ( D ) the real sample solution detection of colloidal gold strip for BTX-1.

    Journal: Toxins

    Article Title: Preparation of Monoclonal Antibody for Brevetoxin 1 and Development of Ic-ELISA and Colloidal Gold Strip to Detect Brevetoxin 1

    doi: 10.3390/toxins10020075

    Figure Lengend Snippet: Construction and characterization of colloidal gold strip test; ( A ) the description of strip test results. In the absence of BTX-1 in the sample solution, both two line exits on the control and test zone, indicating negative. Only one control line stands positive for enough toxin binding to the anti-BTX-1-BSA McAb. If no lines, or only the test line was red, it indicated invalid results; ( B ) cross-reactivity of the test strip with other toxins, such as OA, DA, BTX-2, BTX-3, TTX, CTX, STX; ( C ) the detection limit of colloidal gold strip test for BTX-1; ( D ) the real sample solution detection of colloidal gold strip for BTX-1.

    Article Snippet: The reason was that BTX-1 will bind with antibody-gold nanoparticle conjugates, so it makes the antibody-gold nanoparticle conjugates fail to bind with the BTX-1-BSA that was coated onto the Millipore 135 NC membrane (Jieyi biotech Co., shanghai, china).

    Techniques: Stripping Membranes, Binding Assay

    Identification of the conjugates and anti-serum titer. ( A , B ) Analysis of conjugates and carrier protein by non-denaturing agarose electrophoris. ( A ) Lane 1: BTX-1-BSA conjugates sample, Lane 2: BSA; ( B ) Lane 1: BTX-1-OVA conjugates sample, Lane 2: OVA. ( C ) Titer of mice anti-serum measured by indirect ELISA. Mouse 1 and 2 were immunized with BTX-1-OVA conjugate, and the control was immunized with only adjuvant and PBS.

    Journal: Toxins

    Article Title: Preparation of Monoclonal Antibody for Brevetoxin 1 and Development of Ic-ELISA and Colloidal Gold Strip to Detect Brevetoxin 1

    doi: 10.3390/toxins10020075

    Figure Lengend Snippet: Identification of the conjugates and anti-serum titer. ( A , B ) Analysis of conjugates and carrier protein by non-denaturing agarose electrophoris. ( A ) Lane 1: BTX-1-BSA conjugates sample, Lane 2: BSA; ( B ) Lane 1: BTX-1-OVA conjugates sample, Lane 2: OVA. ( C ) Titer of mice anti-serum measured by indirect ELISA. Mouse 1 and 2 were immunized with BTX-1-OVA conjugate, and the control was immunized with only adjuvant and PBS.

    Article Snippet: The reason was that BTX-1 will bind with antibody-gold nanoparticle conjugates, so it makes the antibody-gold nanoparticle conjugates fail to bind with the BTX-1-BSA that was coated onto the Millipore 135 NC membrane (Jieyi biotech Co., shanghai, china).

    Techniques: Mouse Assay, Indirect ELISA