96 well plates Thermo Fisher Search Results


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  • 99
    Thermo Fisher nunc edge 96 well plate
    Nunc Edge 96 Well Plate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher frozen thermo fisher custom made 96 well microtiter plate
    Frozen Thermo Fisher Custom Made 96 Well Microtiter Plate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher deep well 96 well plate
    Deep Well 96 Well Plate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher 96 well plates
    Proliferation of PBMC from macaques with collagen-induced arthritis (CIA). PBMC (2 × 10 5 cells in 100 μL per well) were seeded in <t>96-well</t> plates. Cells were cultured with or without CII (40 μg/mL) for 72 h, after which they were evaluated in a BrdU assay. The stimulation index value (mean optical density values of CII-stimulated cultures divided by the mean optical density values of medium-only cultures) was calculated for each treatment. (A) Proliferation of PBMC. (B) Proliferation of PBMC against CII. (C) Stimulation index. Data are expressed as box-and-whisker plots ( n = 3 or 4 per group); group means were compared by using Mann–Whitney U tests. *, Value significantly ( P
    96 Well Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1968 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher 96 well microtiter plate
    Binding of SP-D NCRD proteins to mycobacterial species. Bacilli (5 × 10 5 ) were dried down into each well of a <t>96-well</t> <t>microtiter</t> plate and incubated with the 5 μg/mL NCRD protein in the presence or absence of 100 mM maltose as
    96 Well Microtiter Plate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 737 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher 96 well microdialysis plate
    Binding of SP-D NCRD proteins to mycobacterial species. Bacilli (5 × 10 5 ) were dried down into each well of a <t>96-well</t> <t>microtiter</t> plate and incubated with the 5 μg/mL NCRD protein in the presence or absence of 100 mM maltose as
    96 Well Microdialysis Plate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher black 96 well immuno plates
    Binding of SP-D NCRD proteins to mycobacterial species. Bacilli (5 × 10 5 ) were dried down into each well of a <t>96-well</t> <t>microtiter</t> plate and incubated with the 5 μg/mL NCRD protein in the presence or absence of 100 mM maltose as
    Black 96 Well Immuno Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher 96 well assay plates
    Binding of SP-D NCRD proteins to mycobacterial species. Bacilli (5 × 10 5 ) were dried down into each well of a <t>96-well</t> <t>microtiter</t> plate and incubated with the 5 μg/mL NCRD protein in the presence or absence of 100 mM maltose as
    96 Well Assay Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 77 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher 96 well plate individual square well
    Binding of SP-D NCRD proteins to mycobacterial species. Bacilli (5 × 10 5 ) were dried down into each well of a <t>96-well</t> <t>microtiter</t> plate and incubated with the 5 μg/mL NCRD protein in the presence or absence of 100 mM maltose as
    96 Well Plate Individual Square Well, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher nunc fluoronunc luminunc 96 well plates
    Binding of SP-D NCRD proteins to mycobacterial species. Bacilli (5 × 10 5 ) were dried down into each well of a <t>96-well</t> <t>microtiter</t> plate and incubated with the 5 μg/mL NCRD protein in the presence or absence of 100 mM maltose as
    Nunc Fluoronunc Luminunc 96 Well Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher 96 well plastic plate
    Binding of SP-D NCRD proteins to mycobacterial species. Bacilli (5 × 10 5 ) were dried down into each well of a <t>96-well</t> <t>microtiter</t> plate and incubated with the 5 μg/mL NCRD protein in the presence or absence of 100 mM maltose as
    96 Well Plastic Plate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher nunc 96 well deep well plates
    Binding of SP-D NCRD proteins to mycobacterial species. Bacilli (5 × 10 5 ) were dried down into each well of a <t>96-well</t> <t>microtiter</t> plate and incubated with the 5 μg/mL NCRD protein in the presence or absence of 100 mM maltose as
    Nunc 96 Well Deep Well Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher 96 well polystyrene plates
    Roles of CLP proteins in bacterial aggregation. (A) Cells were grown in liquid LB medium for 72 h in <t>96-well</t> plates. The images were obtained by viewing from the top to the bottom. (B) Cells viewed from front to back after standing for 10 h following 24 h incubation in glass test tubes. (C) Cell sedimentation assy. WT, Δ clpA , Δ clpB , Δ clpC , and Δ clpD bacteria were grown until OD 600 = 0.7 and the bacterial precipitates were suspended by mixing, before the OD 600 values were measured at 1 h intervals.
    96 Well Polystyrene Plates, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 138 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher nunc microwell 96 well optical bottom plate
    Roles of CLP proteins in bacterial aggregation. (A) Cells were grown in liquid LB medium for 72 h in <t>96-well</t> plates. The images were obtained by viewing from the top to the bottom. (B) Cells viewed from front to back after standing for 10 h following 24 h incubation in glass test tubes. (C) Cell sedimentation assy. WT, Δ clpA , Δ clpB , Δ clpC , and Δ clpD bacteria were grown until OD 600 = 0.7 and the bacterial precipitates were suspended by mixing, before the OD 600 values were measured at 1 h intervals.
    Nunc Microwell 96 Well Optical Bottom Plate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Proliferation of PBMC from macaques with collagen-induced arthritis (CIA). PBMC (2 × 10 5 cells in 100 μL per well) were seeded in 96-well plates. Cells were cultured with or without CII (40 μg/mL) for 72 h, after which they were evaluated in a BrdU assay. The stimulation index value (mean optical density values of CII-stimulated cultures divided by the mean optical density values of medium-only cultures) was calculated for each treatment. (A) Proliferation of PBMC. (B) Proliferation of PBMC against CII. (C) Stimulation index. Data are expressed as box-and-whisker plots ( n = 3 or 4 per group); group means were compared by using Mann–Whitney U tests. *, Value significantly ( P

    Journal: Comparative Medicine

    Article Title: Relationships between Cytokine Levels and Disease Parameters during the Development of a Collagen-induced Arthritis Model in Cynomolgus Macaques (Macaca fascicularis)

    doi: 10.30802/AALAS-CM-18-000058

    Figure Lengend Snippet: Proliferation of PBMC from macaques with collagen-induced arthritis (CIA). PBMC (2 × 10 5 cells in 100 μL per well) were seeded in 96-well plates. Cells were cultured with or without CII (40 μg/mL) for 72 h, after which they were evaluated in a BrdU assay. The stimulation index value (mean optical density values of CII-stimulated cultures divided by the mean optical density values of medium-only cultures) was calculated for each treatment. (A) Proliferation of PBMC. (B) Proliferation of PBMC against CII. (C) Stimulation index. Data are expressed as box-and-whisker plots ( n = 3 or 4 per group); group means were compared by using Mann–Whitney U tests. *, Value significantly ( P

    Article Snippet: PBMC (2 × 105 cells/100 μL per well) were seeded in 96-well plates (Thermo Scientific, Waltham, MA).

    Techniques: Cell Culture, BrdU Staining, Whisker Assay

    EAEC 042 binds to ECM proteins. EAEC 042 was added to 96-well plates coated separately with 25 μg/ml of each ECM protein, and the binding was detected by ELISA using anti-O44 primary antibodies. The bars represent the means for three experiments,

    Journal:

    Article Title: The Major Pilin Subunit of the AAF/II Fimbriae from Enteroaggregative Escherichia coli Mediates Binding to Extracellular Matrix Proteins ▿

    doi: 10.1128/IAI.00439-08

    Figure Lengend Snippet: EAEC 042 binds to ECM proteins. EAEC 042 was added to 96-well plates coated separately with 25 μg/ml of each ECM protein, and the binding was detected by ELISA using anti-O44 primary antibodies. The bars represent the means for three experiments,

    Article Snippet: Optical densities were read at 450 nm with a 96-well plate reader (Thermo Labsystems).

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay

    Binding of AafA dsc to ECM proteins. (A) AafA dsc protein was added at 10 μg/ml to wells of 96-well plates coated separately with either 25 μg/ml or 50 μg/ml of each ECM protein, and the binding was determined by ELISA using anti-AafA

    Journal:

    Article Title: The Major Pilin Subunit of the AAF/II Fimbriae from Enteroaggregative Escherichia coli Mediates Binding to Extracellular Matrix Proteins ▿

    doi: 10.1128/IAI.00439-08

    Figure Lengend Snippet: Binding of AafA dsc to ECM proteins. (A) AafA dsc protein was added at 10 μg/ml to wells of 96-well plates coated separately with either 25 μg/ml or 50 μg/ml of each ECM protein, and the binding was determined by ELISA using anti-AafA

    Article Snippet: Optical densities were read at 450 nm with a 96-well plate reader (Thermo Labsystems).

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay

    The rPrP–LMWHep complex formed at pH 5.8 is resistant to conversion. For this assay, 98 μl of fresh RT-QuIC buffer (10 mM phosphate buffer, pH 7.4; 130 mM NaCl; 0.1 mg/ml rPrP  23–231 –LMWHep; 10 mM ThT; and 10 mM EDTA) was loaded into the wells of a black 96-well plate with a clear bottom. LMWHep, at a final concentration of 10 μM, was added to rPrP in 10 mM phosphate buffer containing 130 mM NaCl at pH 7.0 ( A ) or 5.8 ( B ). The reactions were seeded with 2 μl of a 10 −7  dilution of mouse BH. NBH, normal BH. The average ThT fluorescence from a set of quadruplicate wells is reported on the vertical axis.

    Journal: The FASEB Journal

    Article Title: Heparin binding confers prion stability and impairs its aggregation

    doi: 10.1096/fj.13-246777

    Figure Lengend Snippet: The rPrP–LMWHep complex formed at pH 5.8 is resistant to conversion. For this assay, 98 μl of fresh RT-QuIC buffer (10 mM phosphate buffer, pH 7.4; 130 mM NaCl; 0.1 mg/ml rPrP 23–231 –LMWHep; 10 mM ThT; and 10 mM EDTA) was loaded into the wells of a black 96-well plate with a clear bottom. LMWHep, at a final concentration of 10 μM, was added to rPrP in 10 mM phosphate buffer containing 130 mM NaCl at pH 7.0 ( A ) or 5.8 ( B ). The reactions were seeded with 2 μl of a 10 −7 dilution of mouse BH. NBH, normal BH. The average ThT fluorescence from a set of quadruplicate wells is reported on the vertical axis.

    Article Snippet: Briefly, 98 μl of fresh RT-QuIC buffer (10 mM phosphate buffer, pH 7.4; 130 mM NaCl; 0.1 mg/ml rPrP; 10 mM ThT; and 10 mM EDTA) was loaded into the wells of a black 96-well plate with a clear bottom (Nalge Nunc International, Penfield, NY, USA).

    Techniques: Concentration Assay, Fluorescence

    Cleavage of ECE-1 quenched fluorescent substrate (QFS) by EAhy926 endothelial cells in culture. Panel A: Endothelial cells grown in 96-well microtiter plates were incubated with an ECE-1 QFS in the absence or presence of the NEP inhibitor thiorphan (10 or 50 μM) or the NEP/ECE inhibitor phosphoramidon (10 μM) within a thermostatted plate reader, and fluorescence continuously monitored. Shown are the results depicting the mean nmoles of QFS cleaved ( n = 3 per group, ± s.e.m.) for every fifth fluorescence determination. Panel B: Treatment with PMA increases cell-surface ECE-1 activity. Cells grown in 96-well plates were pre-incubated for 30 min with 10 μM thiorphan prior to addition of ECE-1 QFS. After a further 30 min, 10 μl vehicle or PMA (40 μM stock) was added to each well. Shown are the results depicting the mean nmoles of QFS cleaved ( n = 8 per group, ± s.e.m.) for every fifth fluorescence determination.

    Journal: International Journal of Peptide Research and Therapeutics

    Article Title: Protein Kinase C Regulates the Cell Surface Activity of Endothelin-Converting Enzyme-1

    doi: 10.1007/s10989-006-9034-3

    Figure Lengend Snippet: Cleavage of ECE-1 quenched fluorescent substrate (QFS) by EAhy926 endothelial cells in culture. Panel A: Endothelial cells grown in 96-well microtiter plates were incubated with an ECE-1 QFS in the absence or presence of the NEP inhibitor thiorphan (10 or 50 μM) or the NEP/ECE inhibitor phosphoramidon (10 μM) within a thermostatted plate reader, and fluorescence continuously monitored. Shown are the results depicting the mean nmoles of QFS cleaved ( n = 3 per group, ± s.e.m.) for every fifth fluorescence determination. Panel B: Treatment with PMA increases cell-surface ECE-1 activity. Cells grown in 96-well plates were pre-incubated for 30 min with 10 μM thiorphan prior to addition of ECE-1 QFS. After a further 30 min, 10 μl vehicle or PMA (40 μM stock) was added to each well. Shown are the results depicting the mean nmoles of QFS cleaved ( n = 8 per group, ± s.e.m.) for every fifth fluorescence determination.

    Article Snippet: Cell-based Quenched Fluorescent Substrate Assay EA.hy926 cells grown in 96-well microtiter plates were washed with Opti-MEM (Invitrogen Australia, Mt.

    Techniques: Incubation, Fluorescence, Activity Assay

    Nar enhances the chemosensitivity of human colorectal cancer cells to DNA-acting drugs. Human colorectal cancer cells SW1116 were plated (27 × 10 3 cells/well) into a 96-well plate at 37°C in a non-CO 2 incubator. At 18 h after starting the culture, the cells were treated for 24 h with Nar (1 mM) and various concentrations of camptothecin, CPT doxorubicin, DOX, 5-fluorouracil, 5FU cisplatin, CIP, etoposide, ETP ellipticine, ELP (1 × 10 −10 – 1 × 10 −3 M), carboplatin, CAP (1 × 10 −10 – 3.5 × 10 −4 M) and cyclophosphamide, CPA (1 × 10 −11 – 1 × 10 −5 M). Cell proliferation was monitored using an MTT assay.

    Journal: Cancer Cell International

    Article Title: Growth inhibitory and chemo-sensitization effects of naringenin, a natural flavanone purified from Thymus vulgaris, on human breast and colorectal cancer

    doi: 10.1186/s12935-015-0194-0

    Figure Lengend Snippet: Nar enhances the chemosensitivity of human colorectal cancer cells to DNA-acting drugs. Human colorectal cancer cells SW1116 were plated (27 × 10 3 cells/well) into a 96-well plate at 37°C in a non-CO 2 incubator. At 18 h after starting the culture, the cells were treated for 24 h with Nar (1 mM) and various concentrations of camptothecin, CPT doxorubicin, DOX, 5-fluorouracil, 5FU cisplatin, CIP, etoposide, ETP ellipticine, ELP (1 × 10 −10 – 1 × 10 −3 M), carboplatin, CAP (1 × 10 −10 – 3.5 × 10 −4 M) and cyclophosphamide, CPA (1 × 10 −11 – 1 × 10 −5 M). Cell proliferation was monitored using an MTT assay.

    Article Snippet: For each sample, 2.5 μl of cDNA and 12.5 μl of Taqman Universal Master Mix (2×) were used, and the final volume was adjusted to 25 μl with nuclease-free water on an optical 96-well reaction plate (Applied Biosystems).

    Techniques: Cycling Probe Technology, MTT Assay

    Nar enhances the chemosensitivity of human breast cancer cells to DNA-acting drugs. Human breast cancer cells HTB26 were plated (27 × 10 3 cells/well) into a 96-well plate at 37°C in a non-CO 2 incubator. At 18 h after starting the culture, the cells were treated for 24 h with Nar (1 mM) and various concentrations of camptothecin, CPT, doxorubicin, DOX, 5-fluorouracil, 5FU, cisplatin, CIP, etoposide, ETP, ellipticine, ELP (1 × 10 −10 – 1 × 10 −3 M), carboplatin, CAP (1 × 10 −10 – 3.5 × 10 −4 M) and cyclophosphamide, CPA (1 × 10 −11 – 1 × 10 −5 M). Cell proliferation was monitored using an MTT assay.

    Journal: Cancer Cell International

    Article Title: Growth inhibitory and chemo-sensitization effects of naringenin, a natural flavanone purified from Thymus vulgaris, on human breast and colorectal cancer

    doi: 10.1186/s12935-015-0194-0

    Figure Lengend Snippet: Nar enhances the chemosensitivity of human breast cancer cells to DNA-acting drugs. Human breast cancer cells HTB26 were plated (27 × 10 3 cells/well) into a 96-well plate at 37°C in a non-CO 2 incubator. At 18 h after starting the culture, the cells were treated for 24 h with Nar (1 mM) and various concentrations of camptothecin, CPT, doxorubicin, DOX, 5-fluorouracil, 5FU, cisplatin, CIP, etoposide, ETP, ellipticine, ELP (1 × 10 −10 – 1 × 10 −3 M), carboplatin, CAP (1 × 10 −10 – 3.5 × 10 −4 M) and cyclophosphamide, CPA (1 × 10 −11 – 1 × 10 −5 M). Cell proliferation was monitored using an MTT assay.

    Article Snippet: For each sample, 2.5 μl of cDNA and 12.5 μl of Taqman Universal Master Mix (2×) were used, and the final volume was adjusted to 25 μl with nuclease-free water on an optical 96-well reaction plate (Applied Biosystems).

    Techniques: Cycling Probe Technology, MTT Assay

    Time and dose-dependent anti-proliferative effects and inhibition of colony formation of Nar on human colorectal and breast cancer cell lines. Human colorectal cancer cells (SW1116, SW837) (A a- e) , human breast cancer cells (HTB 26, HTB132) (B a- e) and normal human fibroblast cells (CRL1554) (A, B a- e) were plated (27 × 10 3 cells/well) in 96-well plates in CO 2 and non-CO 2 incubators, depending on type of media and cells, at 37°C for 18 h. The cells were then treated with various concentrations of Nar (0.05 – 4.0 mM) for 3–24 h. Cell growth was monitored using an MTT assay. Untreated and Nar-treated colorectal cancer cells SW1116 (Ca) , SW837 (Cb) and Nar-treated breast cancer cells HTB26 (Cc) , HTB132 (Cd) were trypsinized, counted and plated (500 cells /well) in 6-well plates. Following 10–14 days of incubation in non-CO 2 incubator at 37°C, the colonies were fixed and stained with crystal violet. The stained colonies were counted and compared with the untreated control.

    Journal: Cancer Cell International

    Article Title: Growth inhibitory and chemo-sensitization effects of naringenin, a natural flavanone purified from Thymus vulgaris, on human breast and colorectal cancer

    doi: 10.1186/s12935-015-0194-0

    Figure Lengend Snippet: Time and dose-dependent anti-proliferative effects and inhibition of colony formation of Nar on human colorectal and breast cancer cell lines. Human colorectal cancer cells (SW1116, SW837) (A a- e) , human breast cancer cells (HTB 26, HTB132) (B a- e) and normal human fibroblast cells (CRL1554) (A, B a- e) were plated (27 × 10 3 cells/well) in 96-well plates in CO 2 and non-CO 2 incubators, depending on type of media and cells, at 37°C for 18 h. The cells were then treated with various concentrations of Nar (0.05 – 4.0 mM) for 3–24 h. Cell growth was monitored using an MTT assay. Untreated and Nar-treated colorectal cancer cells SW1116 (Ca) , SW837 (Cb) and Nar-treated breast cancer cells HTB26 (Cc) , HTB132 (Cd) were trypsinized, counted and plated (500 cells /well) in 6-well plates. Following 10–14 days of incubation in non-CO 2 incubator at 37°C, the colonies were fixed and stained with crystal violet. The stained colonies were counted and compared with the untreated control.

    Article Snippet: For each sample, 2.5 μl of cDNA and 12.5 μl of Taqman Universal Master Mix (2×) were used, and the final volume was adjusted to 25 μl with nuclease-free water on an optical 96-well reaction plate (Applied Biosystems).

    Techniques: Inhibition, MTT Assay, Incubation, Staining

    Detection of Nb474H immuno-affinity captured glycosomal aldolase. (A) Nb474H immuno-affinity captured glycosomal aldolase ( Tco ALD) detected by SDS-PAGE under reducing conditions. Panel ( top left ): Native Tco ALD was captured from the soluble proteome (s.p.) or infected sera on a 96-well ELISA coated with Nb474H, eluted from the plate and analysed on a 10% SDS-PAGE developed with silver staining. Lane M, protein ladder; lane 1, pure Nb474H; lane 2, pure Nb474B; lane 3, eluted protein captured from s.p. (6 μg); lane 4, eluted protein captured from infected sera (8 μg). Panel ( top right ): Native Tco ALD was captured from secretome on nickel beads linked to Nb474H, eluted and analysed on a 10% SDS-PAGE developed with coomassie blue. Lane M, protein ladder; lane 1, Nb474H; lane 2, flow through; lane 3, wash; lane 4, eluted protein. Native Tco ALD protein migrated at ±40 kDa (arrows, top) and the Nb474 migrated at ±15kDa (arrows, bottom). (B) Nb474H immuno-affinity captured Tco ALD from T . congolense TC13 s.p. detected by Anti- T . brucei aldolase MAb (Anti- Tb ALD MAb) in ELISA. Bar ( left ): OD450nm levels in wells filled with coating buffer followed by addition of T . congolense TC13 s.p. and then Anti-TbALD MAb; bar ( middle ): OD450nm in wells coated with the Nb followed by addition of Anti- Tb ALD MAb; and bar ( right ): OD450nm in wells coated with the Nb followed by addition of T . congolense TC13 s.p. and then Anti- Tb ALD MAb. In the last step goat anti-mouse IgG conjugated to Horse radish peroxidase (HRP) was added to all the wells and then developed with 1-Step ultra 3,3′,5,5′-tetramethylbenzidine (TMB) substrate. The OD450nm shown on the graph represent the average value of duplicate wells. *** p

    Journal: PLoS Neglected Tropical Diseases

    Article Title: An Anti-proteome Nanobody Library Approach Yields a Specific Immunoassay for Trypanosoma congolense Diagnosis Targeting Glycosomal Aldolase

    doi: 10.1371/journal.pntd.0004420

    Figure Lengend Snippet: Detection of Nb474H immuno-affinity captured glycosomal aldolase. (A) Nb474H immuno-affinity captured glycosomal aldolase ( Tco ALD) detected by SDS-PAGE under reducing conditions. Panel ( top left ): Native Tco ALD was captured from the soluble proteome (s.p.) or infected sera on a 96-well ELISA coated with Nb474H, eluted from the plate and analysed on a 10% SDS-PAGE developed with silver staining. Lane M, protein ladder; lane 1, pure Nb474H; lane 2, pure Nb474B; lane 3, eluted protein captured from s.p. (6 μg); lane 4, eluted protein captured from infected sera (8 μg). Panel ( top right ): Native Tco ALD was captured from secretome on nickel beads linked to Nb474H, eluted and analysed on a 10% SDS-PAGE developed with coomassie blue. Lane M, protein ladder; lane 1, Nb474H; lane 2, flow through; lane 3, wash; lane 4, eluted protein. Native Tco ALD protein migrated at ±40 kDa (arrows, top) and the Nb474 migrated at ±15kDa (arrows, bottom). (B) Nb474H immuno-affinity captured Tco ALD from T . congolense TC13 s.p. detected by Anti- T . brucei aldolase MAb (Anti- Tb ALD MAb) in ELISA. Bar ( left ): OD450nm levels in wells filled with coating buffer followed by addition of T . congolense TC13 s.p. and then Anti-TbALD MAb; bar ( middle ): OD450nm in wells coated with the Nb followed by addition of Anti- Tb ALD MAb; and bar ( right ): OD450nm in wells coated with the Nb followed by addition of T . congolense TC13 s.p. and then Anti- Tb ALD MAb. In the last step goat anti-mouse IgG conjugated to Horse radish peroxidase (HRP) was added to all the wells and then developed with 1-Step ultra 3,3′,5,5′-tetramethylbenzidine (TMB) substrate. The OD450nm shown on the graph represent the average value of duplicate wells. *** p

    Article Snippet: Then 1011 of display phages were adsorbed on a 96-well Nunc plate (Thermo scientific) coated in parallel with soluble proteome (25 μg/well) of four different T . congolense strains (STIB68, TRT17, TC13 or MF3cl2).

    Techniques: SDS Page, Infection, Enzyme-linked Immunosorbent Assay, Silver Staining, Flow Cytometry

    COMP associates with ADAMTS-7 both in vitro and in vivo. A ) GST pulldown assay. Purified GST (lane 2) or GST-TS7-CT fusion protein (lane 3 and 4) immobilized on GSH-Sepharose beads were incubated with purified hCOMP in the presence (lane 4) or absence (lane 3) of 5 mM Ca 2+ . Proteins trapped by C terminal of ADAMTS-7 fused to GST were examined by immunoblotting with anti-COMP antibodies. Purified COMP (lane 1) was used as a positive control. Arrow indicates full-length COMP band. B ) Solid-phase assay. Various amounts of recombinant His tagged C-terminal 4 TSP motifs of ADAMTS7 (His-TS7C4TSP) were immobilized on solid-phase 96-well microtiter plates. After being blocked, COMP was added to each well, followed by the addition of 10 mM CaCl 2 . Samples were then allowed to bind overnight at 4°C. Bound protein from liquid phase was detected using monoclonal antibodies to the bound COMP. C ) Characterization of anti-ADAMTS-7 Ab. Cell lysates prepared from Sf9 insect cells infected with control (lane 1) or ADAMTS-7 bacluovirus (lane 2), from HEK293 cells stably transfected with a COMP expression construct (lane 3), and from MG-63 osteoblastic cells (lane 4) were subjected to SDS-PAGE and immunoblotted with affinity-purified anti-ADAMTS-7 antibodies. D ) CO-IP assay. Cartilage extracts were incubated with either anti-COMP (lane 2) antiserum or control IgG (lane 3), followed by protein A/G agarose. Immunoprecipitated protein complex and cartilage extracts (lane 1, which provides a positive control) were examined by Western blotting with an anti-ADAMTS-7 Ab.

    Journal: The FASEB journal : official publication of the Federation of American Societies for Experimental Biology

    Article Title: ADAMTS-7: a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein

    doi: 10.1096/fj.05-3877fje

    Figure Lengend Snippet: COMP associates with ADAMTS-7 both in vitro and in vivo. A ) GST pulldown assay. Purified GST (lane 2) or GST-TS7-CT fusion protein (lane 3 and 4) immobilized on GSH-Sepharose beads were incubated with purified hCOMP in the presence (lane 4) or absence (lane 3) of 5 mM Ca 2+ . Proteins trapped by C terminal of ADAMTS-7 fused to GST were examined by immunoblotting with anti-COMP antibodies. Purified COMP (lane 1) was used as a positive control. Arrow indicates full-length COMP band. B ) Solid-phase assay. Various amounts of recombinant His tagged C-terminal 4 TSP motifs of ADAMTS7 (His-TS7C4TSP) were immobilized on solid-phase 96-well microtiter plates. After being blocked, COMP was added to each well, followed by the addition of 10 mM CaCl 2 . Samples were then allowed to bind overnight at 4°C. Bound protein from liquid phase was detected using monoclonal antibodies to the bound COMP. C ) Characterization of anti-ADAMTS-7 Ab. Cell lysates prepared from Sf9 insect cells infected with control (lane 1) or ADAMTS-7 bacluovirus (lane 2), from HEK293 cells stably transfected with a COMP expression construct (lane 3), and from MG-63 osteoblastic cells (lane 4) were subjected to SDS-PAGE and immunoblotted with affinity-purified anti-ADAMTS-7 antibodies. D ) CO-IP assay. Cartilage extracts were incubated with either anti-COMP (lane 2) antiserum or control IgG (lane 3), followed by protein A/G agarose. Immunoprecipitated protein complex and cartilage extracts (lane 1, which provides a positive control) were examined by Western blotting with an anti-ADAMTS-7 Ab.

    Article Snippet: PCR reactions for all samples were performed in duplicate in 96-well optical plates with 5 ng of cDNA (1 ng of cDNA for the 18S rRNA), 100 nM probe, 200 nM each primer, and 10.0 μl of TaqMan Universal 2× PCR Master Mix (PE-Applied Biosystems, St. Louis, MO) in a 20 μl reaction vol.

    Techniques: In Vitro, In Vivo, GST Pulldown Assay, Purification, Incubation, Positive Control, Recombinant, Infection, Stable Transfection, Transfection, Expressing, Construct, SDS Page, Affinity Purification, Co-Immunoprecipitation Assay, Immunoprecipitation, Western Blot

    Cell-to-cell infection occurs through the extracellular medium. (A and B) Monolayers of HLC-A549 were inoculated with Ad2-dE3B-GFP expressing eGFP. Two h later, the inoculum was replaced with liquid or gel-forming (semisolid) medium (0.6% ultralow-melting-point agarose mass). This agarose is liquid at 37°C, gels at room temperature, and remains gelled at 37°C. PQs exhibit comet-like shapes in liquid medium and circular shapes in semisolid medium. The micrographs are composites of stitched images taken from multiple sites in 96-well plates at 113.5 hpi. (C) Neutralizing antiserum against HAdV in the culture medium inhibits viral spreading. HLC-A549 cells grown in monolayers in 96-well plates were inoculated with 0.1 ml of medium containing 10 −7 mg/ml Ad2-dE3B-GFP for 24 h, supplemented with antiserum containing medium, and then imaged at the indicated time points. Scale bar, 1 mm. See also Fig. S2 and S3 and Movies S2 and S3 in the supplemental material.

    Journal: Journal of Virology

    Article Title: Cell-Free Transmission of Human Adenovirus by Passive Mass Transfer in Cell Culture Simulated in a Computer Model

    doi: 10.1128/JVI.01102-12

    Figure Lengend Snippet: Cell-to-cell infection occurs through the extracellular medium. (A and B) Monolayers of HLC-A549 were inoculated with Ad2-dE3B-GFP expressing eGFP. Two h later, the inoculum was replaced with liquid or gel-forming (semisolid) medium (0.6% ultralow-melting-point agarose mass). This agarose is liquid at 37°C, gels at room temperature, and remains gelled at 37°C. PQs exhibit comet-like shapes in liquid medium and circular shapes in semisolid medium. The micrographs are composites of stitched images taken from multiple sites in 96-well plates at 113.5 hpi. (C) Neutralizing antiserum against HAdV in the culture medium inhibits viral spreading. HLC-A549 cells grown in monolayers in 96-well plates were inoculated with 0.1 ml of medium containing 10 −7 mg/ml Ad2-dE3B-GFP for 24 h, supplemented with antiserum containing medium, and then imaged at the indicated time points. Scale bar, 1 mm. See also Fig. S2 and S3 and Movies S2 and S3 in the supplemental material.

    Article Snippet: All live imaging experiments were performed in 96-well black plates (Matrix; Thermo Fisher Scientific, Lausanne, Switzerland).

    Techniques: Infection, Expressing

    Frequency distributions for quantification of soy 305423. Comparative overview over 20 exemplary frequency distributions resulting from a single experimental 96-well plate for the quantification of soy event 305423 (compare Additional file 3 : Figure S3). Effects of different baseline/threshold settings (Table 1 ) are shown from left to right, increasing replicate numbers from top to bottom, respectively. The grey diamond marks the nominal GMO content of the reference material.

    Journal: BMC Bioinformatics

    Article Title: A statistical approach to quantification of genetically modified organisms (GMO) using frequency distributions

    doi: 10.1186/s12859-014-0407-x

    Figure Lengend Snippet: Frequency distributions for quantification of soy 305423. Comparative overview over 20 exemplary frequency distributions resulting from a single experimental 96-well plate for the quantification of soy event 305423 (compare Additional file 3 : Figure S3). Effects of different baseline/threshold settings (Table 1 ) are shown from left to right, increasing replicate numbers from top to bottom, respectively. The grey diamond marks the nominal GMO content of the reference material.

    Article Snippet: After manual setup, 20 μL of this mixture and subsequently 5 μL sample DNA were distributed automatically into the wells of 96-well reaction plates (MicroAmp, Life Technologies) using a pipetting robot (epMotion 5070, Eppendorf, Hamburg, Germany, or Piro, Dornier-LTF, Lindau, Germany) at constant cooling to 4°C.

    Techniques:

    Frequency distributions for quantification of maize NK603. Comparative overview over 20 exemplary frequency distributions resulting from a single experimental 96-well plate for the quantification of maize event NK603 (compare Figure 2 ). Effects of different baseline/threshold settings (Table 1 ) are shown from left to right, increasing replicate numbers from top to bottom, respectively. The grey diamond marks the nominal GMO content of the reference material.

    Journal: BMC Bioinformatics

    Article Title: A statistical approach to quantification of genetically modified organisms (GMO) using frequency distributions

    doi: 10.1186/s12859-014-0407-x

    Figure Lengend Snippet: Frequency distributions for quantification of maize NK603. Comparative overview over 20 exemplary frequency distributions resulting from a single experimental 96-well plate for the quantification of maize event NK603 (compare Figure 2 ). Effects of different baseline/threshold settings (Table 1 ) are shown from left to right, increasing replicate numbers from top to bottom, respectively. The grey diamond marks the nominal GMO content of the reference material.

    Article Snippet: After manual setup, 20 μL of this mixture and subsequently 5 μL sample DNA were distributed automatically into the wells of 96-well reaction plates (MicroAmp, Life Technologies) using a pipetting robot (epMotion 5070, Eppendorf, Hamburg, Germany, or Piro, Dornier-LTF, Lindau, Germany) at constant cooling to 4°C.

    Techniques:

    Effect of number of replicates on relative standard deviation. Each partial figure shows the effect of different numbers of combined replicates (abscissa) on the relative standard deviation of the population (ordinate). Values for five different settings of baseline/threshold (1–5; Table 1 ) are depicted. The green diamond marks the number of replicates with which a maximum of 15% relative standard deviation is achieved (for all settings). The titles state the name of the event and the nominal value of the measured reference material. Each partial figure is based on experimental data from a single 96-well plate. Dashed frames indicate experiments with plasmidic standard curves (plasmids were linearized before use).

    Journal: BMC Bioinformatics

    Article Title: A statistical approach to quantification of genetically modified organisms (GMO) using frequency distributions

    doi: 10.1186/s12859-014-0407-x

    Figure Lengend Snippet: Effect of number of replicates on relative standard deviation. Each partial figure shows the effect of different numbers of combined replicates (abscissa) on the relative standard deviation of the population (ordinate). Values for five different settings of baseline/threshold (1–5; Table 1 ) are depicted. The green diamond marks the number of replicates with which a maximum of 15% relative standard deviation is achieved (for all settings). The titles state the name of the event and the nominal value of the measured reference material. Each partial figure is based on experimental data from a single 96-well plate. Dashed frames indicate experiments with plasmidic standard curves (plasmids were linearized before use).

    Article Snippet: After manual setup, 20 μL of this mixture and subsequently 5 μL sample DNA were distributed automatically into the wells of 96-well reaction plates (MicroAmp, Life Technologies) using a pipetting robot (epMotion 5070, Eppendorf, Hamburg, Germany, or Piro, Dornier-LTF, Lindau, Germany) at constant cooling to 4°C.

    Techniques: Standard Deviation

    Flowchart for generation of frequency distributions. Illustrated flowchart for the generation of several frequency distributions starting from a single experimental 96-well plate. Transgene (red) and reference gene (blue) are analysed via real-time PCR in separate wells. The light coloured wells contain reactions for 32 replicates of the sample DNA to be measured. Transgene and reference gene copy numbers are extrapolated from corresponding standard curves (dark colours). The white well depicts negative control. For each number of possible transgene or reference gene replicates (considered in two isolations each, i.e. 2× 2, 2× 3, 2× 4, 2× 5,…, 2× 16), copy numbers are arranged in 5000 combinations by chance. The resulting 5000 GMO percentages are divided into frequency classes and depicted. For each number of replicates, a corresponding frequency distribution with its statistical parameters can be visualised. Effects of different baseline/threshold settings are shown from left to right, increasing replicate numbers from top to bottom, respectively.

    Journal: BMC Bioinformatics

    Article Title: A statistical approach to quantification of genetically modified organisms (GMO) using frequency distributions

    doi: 10.1186/s12859-014-0407-x

    Figure Lengend Snippet: Flowchart for generation of frequency distributions. Illustrated flowchart for the generation of several frequency distributions starting from a single experimental 96-well plate. Transgene (red) and reference gene (blue) are analysed via real-time PCR in separate wells. The light coloured wells contain reactions for 32 replicates of the sample DNA to be measured. Transgene and reference gene copy numbers are extrapolated from corresponding standard curves (dark colours). The white well depicts negative control. For each number of possible transgene or reference gene replicates (considered in two isolations each, i.e. 2× 2, 2× 3, 2× 4, 2× 5,…, 2× 16), copy numbers are arranged in 5000 combinations by chance. The resulting 5000 GMO percentages are divided into frequency classes and depicted. For each number of replicates, a corresponding frequency distribution with its statistical parameters can be visualised. Effects of different baseline/threshold settings are shown from left to right, increasing replicate numbers from top to bottom, respectively.

    Article Snippet: After manual setup, 20 μL of this mixture and subsequently 5 μL sample DNA were distributed automatically into the wells of 96-well reaction plates (MicroAmp, Life Technologies) using a pipetting robot (epMotion 5070, Eppendorf, Hamburg, Germany, or Piro, Dornier-LTF, Lindau, Germany) at constant cooling to 4°C.

    Techniques: Real-time Polymerase Chain Reaction, Negative Control

    Effect of baseline/threshold setting on relative deviation from nominal value. Each partial figure depicts the relative absolute deviation from the nominal value of the measured reference material (|arithmetic mean – nominal value|/nominal value) for five different settings of baseline/threshold (1–5; Table 1 ) and two numbers of replicates (2x 2 and 2x 4). The headings state the name of the event and the nominal value of the measured reference material. Each partial figure is based on experimental data from a single 96-well plate.

    Journal: BMC Bioinformatics

    Article Title: A statistical approach to quantification of genetically modified organisms (GMO) using frequency distributions

    doi: 10.1186/s12859-014-0407-x

    Figure Lengend Snippet: Effect of baseline/threshold setting on relative deviation from nominal value. Each partial figure depicts the relative absolute deviation from the nominal value of the measured reference material (|arithmetic mean – nominal value|/nominal value) for five different settings of baseline/threshold (1–5; Table 1 ) and two numbers of replicates (2x 2 and 2x 4). The headings state the name of the event and the nominal value of the measured reference material. Each partial figure is based on experimental data from a single 96-well plate.

    Article Snippet: After manual setup, 20 μL of this mixture and subsequently 5 μL sample DNA were distributed automatically into the wells of 96-well reaction plates (MicroAmp, Life Technologies) using a pipetting robot (epMotion 5070, Eppendorf, Hamburg, Germany, or Piro, Dornier-LTF, Lindau, Germany) at constant cooling to 4°C.

    Techniques:

    Effect of TPT on the proliferative response of bidirectional MLR and anti-CD3/CD28–stimulated CD4 + T cells. Allogeneic human PBMCs from 2 different donors (3 × 10 5 cells/well each) were cocultured in 96-well flat-bottom plates in the presence

    Journal:

    Article Title: Triptolide, a constituent of immunosuppressive Chinese herbal medicine, is a potent suppressor of dendritic-cell maturation and trafficking

    doi: 10.1182/blood-2005-03-0854

    Figure Lengend Snippet: Effect of TPT on the proliferative response of bidirectional MLR and anti-CD3/CD28–stimulated CD4 + T cells. Allogeneic human PBMCs from 2 different donors (3 × 10 5 cells/well each) were cocultured in 96-well flat-bottom plates in the presence

    Article Snippet: Purified CD4+ T cells (105 /well) were cultured in 96-well flat-bottom plates with CD3/CD28 T-cell expansion Dynabeads (5 × 103 /well; Dynal ASA, Oslo, Norway).

    Techniques:

    Binding of SP-D NCRD proteins to mycobacterial species. Bacilli (5 × 10 5 ) were dried down into each well of a 96-well microtiter plate and incubated with the 5 μg/mL NCRD protein in the presence or absence of 100 mM maltose as

    Journal:

    Article Title: Critical role of amino acid position 343 of surfactant protein-D in the selective binding of glycolipids from Mycobacterium tuberculosis

    doi: 10.1093/glycob/cwp122

    Figure Lengend Snippet: Binding of SP-D NCRD proteins to mycobacterial species. Bacilli (5 × 10 5 ) were dried down into each well of a 96-well microtiter plate and incubated with the 5 μg/mL NCRD protein in the presence or absence of 100 mM maltose as

    Article Snippet: Bacterial single cell suspensions (5 × 105 ) in 50 μL TBS (50 mM Tris-hydrochloride + 150 mM sodium chloride, pH 7.5) were added and dried onto triplicate wells of a 96-well microtiter plate (Immulon 1; Thermo Electron Corporation, Milford, MA) followed by overnight UV irradiation treatment to kill the bacteria.

    Techniques: Binding Assay, Incubation

    Specific binding of SP-D NCRD proteins to ManLAM, PILAM, and LM. LAMs (5 μg) or LM (5 μg) were dried down in ethanol into each well of a 96-well microtiter plate and incubated with 5 μg/mL NCRD protein in the presence or absence

    Journal:

    Article Title: Critical role of amino acid position 343 of surfactant protein-D in the selective binding of glycolipids from Mycobacterium tuberculosis

    doi: 10.1093/glycob/cwp122

    Figure Lengend Snippet: Specific binding of SP-D NCRD proteins to ManLAM, PILAM, and LM. LAMs (5 μg) or LM (5 μg) were dried down in ethanol into each well of a 96-well microtiter plate and incubated with 5 μg/mL NCRD protein in the presence or absence

    Article Snippet: Bacterial single cell suspensions (5 × 105 ) in 50 μL TBS (50 mM Tris-hydrochloride + 150 mM sodium chloride, pH 7.5) were added and dried onto triplicate wells of a 96-well microtiter plate (Immulon 1; Thermo Electron Corporation, Milford, MA) followed by overnight UV irradiation treatment to kill the bacteria.

    Techniques: Binding Assay, Incubation

    Specific binding of SP-D NCRD proteins to PIMs. Purified PIM families from M.tb H 37 R v (PIM 2 f, PIM 5 f, and PIM 6 f 5 μg/well) were dried down in ethanol into each well of a 96-well microtiter plate and incubated with 5 μg/mL NCRD protein in

    Journal:

    Article Title: Critical role of amino acid position 343 of surfactant protein-D in the selective binding of glycolipids from Mycobacterium tuberculosis

    doi: 10.1093/glycob/cwp122

    Figure Lengend Snippet: Specific binding of SP-D NCRD proteins to PIMs. Purified PIM families from M.tb H 37 R v (PIM 2 f, PIM 5 f, and PIM 6 f 5 μg/well) were dried down in ethanol into each well of a 96-well microtiter plate and incubated with 5 μg/mL NCRD protein in

    Article Snippet: Bacterial single cell suspensions (5 × 105 ) in 50 μL TBS (50 mM Tris-hydrochloride + 150 mM sodium chloride, pH 7.5) were added and dried onto triplicate wells of a 96-well microtiter plate (Immulon 1; Thermo Electron Corporation, Milford, MA) followed by overnight UV irradiation treatment to kill the bacteria.

    Techniques: Binding Assay, Purification, Incubation

    Roles of CLP proteins in bacterial aggregation. (A) Cells were grown in liquid LB medium for 72 h in 96-well plates. The images were obtained by viewing from the top to the bottom. (B) Cells viewed from front to back after standing for 10 h following 24 h incubation in glass test tubes. (C) Cell sedimentation assy. WT, Δ clpA , Δ clpB , Δ clpC , and Δ clpD bacteria were grown until OD 600 = 0.7 and the bacterial precipitates were suspended by mixing, before the OD 600 values were measured at 1 h intervals.

    Journal: PLoS ONE

    Article Title: Collagen-Like Proteins (ClpA, ClpB, ClpC, and ClpD) Are Required for Biofilm Formation and Adhesion to Plant Roots by Bacillus amyloliquefaciens FZB42

    doi: 10.1371/journal.pone.0117414

    Figure Lengend Snippet: Roles of CLP proteins in bacterial aggregation. (A) Cells were grown in liquid LB medium for 72 h in 96-well plates. The images were obtained by viewing from the top to the bottom. (B) Cells viewed from front to back after standing for 10 h following 24 h incubation in glass test tubes. (C) Cell sedimentation assy. WT, Δ clpA , Δ clpB , Δ clpC , and Δ clpD bacteria were grown until OD 600 = 0.7 and the bacterial precipitates were suspended by mixing, before the OD 600 values were measured at 1 h intervals.

    Article Snippet: To quantify biofilm growth, we applied the crystal violet staining method in 96-well polystyrene plates (Thermo) [ – ].

    Techniques: Incubation, Sedimentation

    Variations in biofilm formation by the wild type and clp mutants. Biofilm formation by wild type and clp mutants in LB medium (A) and on MSgg medium plates (B). The images of colonies were obtained after incubation for 48 h at 37°C. (C) The biofilm images are top-down views of 96-well plates, which were obtained after incubation for 24 h at 37°C in MSgg liquid medium. (D) Quantitative spectrophotometric biofilm assay following crystal violet staining in MSgg medium. Analysis of variance detected a significant main group effect between the wild type and clp mutants (b, P

    Journal: PLoS ONE

    Article Title: Collagen-Like Proteins (ClpA, ClpB, ClpC, and ClpD) Are Required for Biofilm Formation and Adhesion to Plant Roots by Bacillus amyloliquefaciens FZB42

    doi: 10.1371/journal.pone.0117414

    Figure Lengend Snippet: Variations in biofilm formation by the wild type and clp mutants. Biofilm formation by wild type and clp mutants in LB medium (A) and on MSgg medium plates (B). The images of colonies were obtained after incubation for 48 h at 37°C. (C) The biofilm images are top-down views of 96-well plates, which were obtained after incubation for 24 h at 37°C in MSgg liquid medium. (D) Quantitative spectrophotometric biofilm assay following crystal violet staining in MSgg medium. Analysis of variance detected a significant main group effect between the wild type and clp mutants (b, P

    Article Snippet: To quantify biofilm growth, we applied the crystal violet staining method in 96-well polystyrene plates (Thermo) [ – ].

    Techniques: Incubation, Biofilm Production Assay, Staining