Structured Review

Nacalai nonidet p 40
Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5  cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s  t -test. **  p
Nonidet P 40, supplied by Nacalai, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Stimulation of Peritoneal Mesothelial Cells to Secrete Matrix Metalloproteinase-9 (MMP-9) by TNF-α: A Role in the Invasion of Gastric Carcinoma Cells"

Article Title: Stimulation of Peritoneal Mesothelial Cells to Secrete Matrix Metalloproteinase-9 (MMP-9) by TNF-α: A Role in the Invasion of Gastric Carcinoma Cells

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms19123961

Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5  cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s  t -test. **  p
Figure Legend Snippet: Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5 cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s t -test. ** p

Techniques Used: Incubation, Microscopy, Labeling, Fluorescence, Spectrophotometry, Inhibition

2) Product Images from "Constitutive Turnover of Phosphorylation at Thr-412 of Human p57/Coronin-1 Regulates the Interaction with Actin *"

Article Title: Constitutive Turnover of Phosphorylation at Thr-412 of Human p57/Coronin-1 Regulates the Interaction with Actin *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M112.349829

Transient phosphorylation at Thr-412 of p57/coronin-1 in phagocytosing cells.  Human neutrophils were incubated with opsonized zymosan at 37 °C for 0–30 min and lysed with a buffer containing 1% Nonidet P-40. The lysates were subjected to immunoprecipitation with Dynabeads® protein G/anti-p57/coronin-1 antibody (N7), and the immunoprecipitates were analyzed by SDS-PAGE/immunoblotting with anti-p57/coronin-1 antibody (N7) or anti-phospho-Thr-412 of p57/coronin-1 antibody ( pT412 ). The experiments were repeated three times, and representative results are shown.
Figure Legend Snippet: Transient phosphorylation at Thr-412 of p57/coronin-1 in phagocytosing cells. Human neutrophils were incubated with opsonized zymosan at 37 °C for 0–30 min and lysed with a buffer containing 1% Nonidet P-40. The lysates were subjected to immunoprecipitation with Dynabeads® protein G/anti-p57/coronin-1 antibody (N7), and the immunoprecipitates were analyzed by SDS-PAGE/immunoblotting with anti-p57/coronin-1 antibody (N7) or anti-phospho-Thr-412 of p57/coronin-1 antibody ( pT412 ). The experiments were repeated three times, and representative results are shown.

Techniques Used: Incubation, Immunoprecipitation, SDS Page

3) Product Images from "Stimulation of Peritoneal Mesothelial Cells to Secrete Matrix Metalloproteinase-9 (MMP-9) by TNF-α: A Role in the Invasion of Gastric Carcinoma Cells"

Article Title: Stimulation of Peritoneal Mesothelial Cells to Secrete Matrix Metalloproteinase-9 (MMP-9) by TNF-α: A Role in the Invasion of Gastric Carcinoma Cells

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms19123961

Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5  cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s  t -test. **  p
Figure Legend Snippet: Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5 cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s t -test. ** p

Techniques Used: Incubation, Microscopy, Labeling, Fluorescence, Spectrophotometry, Inhibition

4) Product Images from "Stimulation of Peritoneal Mesothelial Cells to Secrete Matrix Metalloproteinase-9 (MMP-9) by TNF-α: A Role in the Invasion of Gastric Carcinoma Cells"

Article Title: Stimulation of Peritoneal Mesothelial Cells to Secrete Matrix Metalloproteinase-9 (MMP-9) by TNF-α: A Role in the Invasion of Gastric Carcinoma Cells

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms19123961

Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5  cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s  t -test. **  p
Figure Legend Snippet: Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5 cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s t -test. ** p

Techniques Used: Incubation, Microscopy, Labeling, Fluorescence, Spectrophotometry, Inhibition

5) Product Images from "Stimulation of Peritoneal Mesothelial Cells to Secrete Matrix Metalloproteinase-9 (MMP-9) by TNF-α: A Role in the Invasion of Gastric Carcinoma Cells"

Article Title: Stimulation of Peritoneal Mesothelial Cells to Secrete Matrix Metalloproteinase-9 (MMP-9) by TNF-α: A Role in the Invasion of Gastric Carcinoma Cells

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms19123961

Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5  cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s  t -test. **  p
Figure Legend Snippet: Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5 cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s t -test. ** p

Techniques Used: Incubation, Microscopy, Labeling, Fluorescence, Spectrophotometry, Inhibition

6) Product Images from "Endogenous Molecules Stimulating N-Acylethanolamine-Hydrolyzing Acid Amidase (NAAA)"

Article Title: Endogenous Molecules Stimulating N-Acylethanolamine-Hydrolyzing Acid Amidase (NAAA)

Journal: ACS Chemical Neuroscience

doi: 10.1021/cn300007s

Substrate specificity of NAAA in the presenceof different stimulators.Recombinant NAAA (0.3–3 μg of protein) was allowed toreact with the indicated  14 C-labeled NAEs at 100 μMin the presence or absence of 0.1% Nonidet P-40,
Figure Legend Snippet: Substrate specificity of NAAA in the presenceof different stimulators.Recombinant NAAA (0.3–3 μg of protein) was allowed toreact with the indicated 14 C-labeled NAEs at 100 μMin the presence or absence of 0.1% Nonidet P-40,

Techniques Used: Recombinant, Labeling

Effects of various buffers on NAAA activity. Recombinant NAAA (300ng of protein) was allowed to react with 100 μM [ 14 C]PEA in the presence of 3 mM DTT and 0.1% Nonidet P-40 at pH 4.5.The pH was adjusted with the following buffers (100 mM): citrate-Na
Figure Legend Snippet: Effects of various buffers on NAAA activity. Recombinant NAAA (300ng of protein) was allowed to react with 100 μM [ 14 C]PEA in the presence of 3 mM DTT and 0.1% Nonidet P-40 at pH 4.5.The pH was adjusted with the following buffers (100 mM): citrate-Na

Techniques Used: Activity Assay, Recombinant

Effects of various phospholipid classes on NAAA activity.RecombinantNAAA (300 ng of protein) was allowed to react with 100 μM [ 14 C]PEA. (A) The reactions were carried out in the presenceof 3 mM DTT and either Nonidet P-40 at 0.1% (w/v) or the
Figure Legend Snippet: Effects of various phospholipid classes on NAAA activity.RecombinantNAAA (300 ng of protein) was allowed to react with 100 μM [ 14 C]PEA. (A) The reactions were carried out in the presenceof 3 mM DTT and either Nonidet P-40 at 0.1% (w/v) or the

Techniques Used: Activity Assay

Effects of various thiol compounds onNAAA activity. RecombinantNAAA (300 ng of protein) was allowed to react with 100 μM [ 14 C]PEA. (A) The reactions were carried out in the presenceof 0.1% Nonidet P-40 and the indicated compound at 3 mM. (B)
Figure Legend Snippet: Effects of various thiol compounds onNAAA activity. RecombinantNAAA (300 ng of protein) was allowed to react with 100 μM [ 14 C]PEA. (A) The reactions were carried out in the presenceof 0.1% Nonidet P-40 and the indicated compound at 3 mM. (B)

Techniques Used: Activity Assay

Related Articles

Activity Assay:

Article Title: Interaction of Phospholipase A/Acyltransferase-3 with Pex19p
Article Snippet: .. To measure PLA1/2 activity, the harvested cells were suspended in homogenization buffer (0.25 m sucrose, 1 m m EDTA, and 20 m m Tris-HCl, pH 7.4) and sonicated three times each for 3 s. The cell homogenates (30 μg of protein) were incubated with 200 μ m 1,2-[1-14 C]dipalmitoyl-PC (45,000 cpm) in 100 μl of 50 m m Tris-HCl (pH 8.0), 2 m m DTT, and 0.1% Nonidet P-40 at 37 °C for 30 min. ..

Article Title: Regulation of Peroxisomal Lipid Metabolism by Catalytic Activity of Tumor Suppressor H-rev107 *
Article Snippet: Clonal cell lines were isolated by colony lifting and maintained in the Geneticin-containing medium. .. To measure PLA1/2 activity, the harvested cells were suspended in 20 m m Tris-HCl (pH 7.4) and sonicated three times each for 3 s. The cell homogenates (30 μg of protein) were incubated with 200 μ m 1,2-[1-14 C]dipalmitoyl-PC (45,000 cpm) in 100 μl of 50 m m Tris-HCl (pH 8.0), 2 m m DTT, and 0.1% Nonidet P-40 at 37 °C for 30 min. ..

Homogenization:

Article Title: Interaction of Phospholipase A/Acyltransferase-3 with Pex19p
Article Snippet: .. To measure PLA1/2 activity, the harvested cells were suspended in homogenization buffer (0.25 m sucrose, 1 m m EDTA, and 20 m m Tris-HCl, pH 7.4) and sonicated three times each for 3 s. The cell homogenates (30 μg of protein) were incubated with 200 μ m 1,2-[1-14 C]dipalmitoyl-PC (45,000 cpm) in 100 μl of 50 m m Tris-HCl (pH 8.0), 2 m m DTT, and 0.1% Nonidet P-40 at 37 °C for 30 min. ..

Sonication:

Article Title: Interaction of Phospholipase A/Acyltransferase-3 with Pex19p
Article Snippet: .. To measure PLA1/2 activity, the harvested cells were suspended in homogenization buffer (0.25 m sucrose, 1 m m EDTA, and 20 m m Tris-HCl, pH 7.4) and sonicated three times each for 3 s. The cell homogenates (30 μg of protein) were incubated with 200 μ m 1,2-[1-14 C]dipalmitoyl-PC (45,000 cpm) in 100 μl of 50 m m Tris-HCl (pH 8.0), 2 m m DTT, and 0.1% Nonidet P-40 at 37 °C for 30 min. ..

Article Title: Regulation of Peroxisomal Lipid Metabolism by Catalytic Activity of Tumor Suppressor H-rev107 *
Article Snippet: Clonal cell lines were isolated by colony lifting and maintained in the Geneticin-containing medium. .. To measure PLA1/2 activity, the harvested cells were suspended in 20 m m Tris-HCl (pH 7.4) and sonicated three times each for 3 s. The cell homogenates (30 μg of protein) were incubated with 200 μ m 1,2-[1-14 C]dipalmitoyl-PC (45,000 cpm) in 100 μl of 50 m m Tris-HCl (pH 8.0), 2 m m DTT, and 0.1% Nonidet P-40 at 37 °C for 30 min. ..

Incubation:

Article Title: Interaction of Phospholipase A/Acyltransferase-3 with Pex19p
Article Snippet: .. To measure PLA1/2 activity, the harvested cells were suspended in homogenization buffer (0.25 m sucrose, 1 m m EDTA, and 20 m m Tris-HCl, pH 7.4) and sonicated three times each for 3 s. The cell homogenates (30 μg of protein) were incubated with 200 μ m 1,2-[1-14 C]dipalmitoyl-PC (45,000 cpm) in 100 μl of 50 m m Tris-HCl (pH 8.0), 2 m m DTT, and 0.1% Nonidet P-40 at 37 °C for 30 min. ..

Article Title: The tumor suppressor gene H-Rev107 functions as a novel Ca2+-independent cytosolic phospholipase A1/2 of the thiol hydrolase type
Article Snippet: The protein concentration was determined by the method of Bradford with BSA as a standard. .. For the PLA1/2 assay, the enzyme was incubated with 200 μM 1,2-[1-14 C]dipalmitoyl-PC (45,000 cpm) in 100 μl of 50 mM glycine-NaOH (pH 9.0), 2 mM DTT, and 0.05% Nonidet P-40 at 37°C for 30 min. For the PE N -acylation assay, the enzyme was incubated with 40 μM 1,2-[1-14 C]dipalmitoyl-PC (45,000 cpm) and 75 μM 1,2-dioleoyl-PE in 100 μl of 50 mM glycine-NaOH (pH 9.0), 2 mM DTT, and 0.05% Nonidet P-40 at 37°C for 30 min. For the lipase assay, the enzyme was incubated with 200 μM [carboxy-14 C]triolein (61,000 cpm) in 100 μl of 50 mM potassium phosphate buffer (pH 7.0) containing 2% BSA , or in 100 μl of 50 mM Tris-HCl (pH 8.0), 2 mM DTT, and 0.05% Nonidet P-40 at 37°C for 30 min. .. The reaction was terminated with the addition of 320 μl of a mixture of chloroform-methanol (2:1, v/v) containing 5 mM 3(2)- t -butyl-4-hydroxyanisole.

Article Title: Regulation of Peroxisomal Lipid Metabolism by Catalytic Activity of Tumor Suppressor H-rev107 *
Article Snippet: Clonal cell lines were isolated by colony lifting and maintained in the Geneticin-containing medium. .. To measure PLA1/2 activity, the harvested cells were suspended in 20 m m Tris-HCl (pH 7.4) and sonicated three times each for 3 s. The cell homogenates (30 μg of protein) were incubated with 200 μ m 1,2-[1-14 C]dipalmitoyl-PC (45,000 cpm) in 100 μl of 50 m m Tris-HCl (pH 8.0), 2 m m DTT, and 0.1% Nonidet P-40 at 37 °C for 30 min. ..

Article Title: Enzymological analysis of the tumor suppressor A-C1 reveals a novel group of phospholipid-metabolizing enzymes
Article Snippet: The protein concentration was determined by the method of Bradford with BSA as a standard (29). .. For the PLA1/2 assay, the enzyme was incubated with 200 μM 1,2-[14 C]dipalmitoyl-PC (45,000 cpm) in 100 μl of 50 mM Tris-HCl (pH 8), 2 mM DTT, and 0.1% Nonidet P-40 at 37°C for 30 min. For the PE N -acylation assay, the enzyme was incubated with 200 μM 1,2-[14 C]dipalmitoyl-PC (45,000 cpm) and 100 μM 1,2-dioleoyl-PE in 100 μl of 50 mM Tris-HCl (pH 9), 2 mM DTT, and 0.1% Nonidet P-40 at 37°C for 30 min. For the lyso PC O -acylation assay, the enzyme was incubated with 200 μM dipalmitoyl-PC and either 100 μM 1-[14 C]palmitoyl-lyso PC (20,000 cpm) or 100 μM 2-[14 C]palmitoyl-lyso PC (18,000 cpm) in 100 μl of 50 mM Tris-HCl (pH 8.0), 2 mM DTT, and 0.1% Nonidet P-40 at 37°C for 30 min. ..

Binding Assay:

Article Title: Direct in Vitro and in Vivo
Article Snippet: .. The assay was performed in a 384-well plate in 20 μl of binding buffer containing 10 n m recombinant GST-Hsp47 protein, 300 n m biotinylated collagen model peptide, 83.4 n m SA-XL665, 0.37 n m anti-GST-Eu-K antibody, 50 m m HEPES/NaOH, 150 m m NaCl, 1 m m EDTA, 0.01% Nonidet P-40, 0.1% BSA, and 100 m m KF. ..

Recombinant:

Article Title: Direct in Vitro and in Vivo
Article Snippet: .. The assay was performed in a 384-well plate in 20 μl of binding buffer containing 10 n m recombinant GST-Hsp47 protein, 300 n m biotinylated collagen model peptide, 83.4 n m SA-XL665, 0.37 n m anti-GST-Eu-K antibody, 50 m m HEPES/NaOH, 150 m m NaCl, 1 m m EDTA, 0.01% Nonidet P-40, 0.1% BSA, and 100 m m KF. ..

Inhibition:

Article Title: Enzymological analysis of the tumor suppressor A-C1 reveals a novel group of phospholipid-metabolizing enzymes
Article Snippet: .. All of these proteins required DTT and Nonidet P-40 for full activities, were sensitive to the inhibition by iodoacetate, and preferred esterolysis at the sn -1 position to that at sn -2 position. .. As compared with the other members, A-C1 showed a relatively high lyso PC O -acyltransferase activity, and its PE N -acylation activity was as high as those of iNAT and HRASLS2.

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    Nacalai nonidet p 40
    Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5  cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s  t -test. **  p
    Nonidet P 40, supplied by Nacalai, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nonidet p 40/product/Nacalai
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5  cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s  t -test. **  p

    Journal: International Journal of Molecular Sciences

    Article Title: Stimulation of Peritoneal Mesothelial Cells to Secrete Matrix Metalloproteinase-9 (MMP-9) by TNF-α: A Role in the Invasion of Gastric Carcinoma Cells

    doi: 10.3390/ijms19123961

    Figure Lengend Snippet: Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5 cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s t -test. ** p

    Article Snippet: Nonidet P-40 was from Nacalai Tesque (Kyoto, Japan).

    Techniques: Incubation, Microscopy, Labeling, Fluorescence, Spectrophotometry, Inhibition

    Transient phosphorylation at Thr-412 of p57/coronin-1 in phagocytosing cells.  Human neutrophils were incubated with opsonized zymosan at 37 °C for 0–30 min and lysed with a buffer containing 1% Nonidet P-40. The lysates were subjected to immunoprecipitation with Dynabeads® protein G/anti-p57/coronin-1 antibody (N7), and the immunoprecipitates were analyzed by SDS-PAGE/immunoblotting with anti-p57/coronin-1 antibody (N7) or anti-phospho-Thr-412 of p57/coronin-1 antibody ( pT412 ). The experiments were repeated three times, and representative results are shown.

    Journal: The Journal of Biological Chemistry

    Article Title: Constitutive Turnover of Phosphorylation at Thr-412 of Human p57/Coronin-1 Regulates the Interaction with Actin *

    doi: 10.1074/jbc.M112.349829

    Figure Lengend Snippet: Transient phosphorylation at Thr-412 of p57/coronin-1 in phagocytosing cells. Human neutrophils were incubated with opsonized zymosan at 37 °C for 0–30 min and lysed with a buffer containing 1% Nonidet P-40. The lysates were subjected to immunoprecipitation with Dynabeads® protein G/anti-p57/coronin-1 antibody (N7), and the immunoprecipitates were analyzed by SDS-PAGE/immunoblotting with anti-p57/coronin-1 antibody (N7) or anti-phospho-Thr-412 of p57/coronin-1 antibody ( pT412 ). The experiments were repeated three times, and representative results are shown.

    Article Snippet: Nonidet P-40 and Phos-tag® acrylamide were from Nacalai Tesque (Kyoto, Japan) and NARD Institute Ltd. (Amagasaki, Japan), respectively.

    Techniques: Incubation, Immunoprecipitation, SDS Page

    Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5  cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s  t -test. **  p

    Journal: International Journal of Molecular Sciences

    Article Title: Stimulation of Peritoneal Mesothelial Cells to Secrete Matrix Metalloproteinase-9 (MMP-9) by TNF-α: A Role in the Invasion of Gastric Carcinoma Cells

    doi: 10.3390/ijms19123961

    Figure Lengend Snippet: Invasion and adhesion of MKN1 cells and effects of the anti-α3 integrin antibody. A monolayer of mesothelial cells was stimulated with TNF-α (10 ng/mL) for 6 h. ( A ) MKN1 cells (1 × 10 5 cells/0.2 mL) in ASF104 serum-free medium were added to the inner chamber of the reconstituted mesothelium and incubated at 37 °C for 16 h. The cells that had migrated into the outer chamber through the membrane were counted under a microscope. ( B ) Fluorescently labeled MKN1 cells were added to the monolayer of mesothelial cells in a 96-well culture plate, and incubated at 37 °C for 40 min. After non-adherent cells were removed by washing, adherent cells were lysed with 1% Nonidet P-40 and measured with a fluorescence spectrophotometer (Ex = 490 nm, Em = 520 nm). For the inhibition experiments, MKN1 cells were treated with the anti-α3 integrin antibody (SM-T1, 10 μg/mL) at 0 °C for 30 min. Experiments were performed in triplicate, and the data are presented as the mean ± SEM. Statistical data analysis was conducted using the Student’s t -test. ** p

    Article Snippet: Adherent cells were lysed with 0.1 mL of 1% Nonidet P-40, and the lysates were diluted with 9 volumes of PBS.

    Techniques: Incubation, Microscopy, Labeling, Fluorescence, Spectrophotometry, Inhibition