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    Millipore pbst
    TWEEN 20

    https://www.bioz.com/result/pbst/product/Millipore
    Average 99 stars, based on 62 article reviews
    Price from $9.99 to $1999.99
    pbst - by Bioz Stars, 2020-07
    99/100 stars

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    1) Product Images from "High throughput screening for inhibitors of the HECT ubiquitin E3 ligase ITCH identifies antidepressant drugs as regulators of autophagy"

    Article Title: High throughput screening for inhibitors of the HECT ubiquitin E3 ligase ITCH identifies antidepressant drugs as regulators of autophagy

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2014.113

    High throughput screening (HTS) for ITCH inhibitors. ( a ) Schematic representation of the layout of the ELISA assay used for the HTS. Recombinant GST-ITCH or ubiquitin ligase dead mutant GST-ITCH C830A were immobilized to glutathione-coated ELISA plates and incubated with either complete ubiquitylation reaction mixtures containing E1, E2 (UbcH7) and FLAG-ubiquitin or partial mixtures as indicated in ( b ). Reactions were performed for 1 h at RT and stopped by washing with PBST before development with HRP-conjugated anti-FLAG antibody for 1 h at RT. After final washes, the wells were incubated with TMB substrate for 15 min at RT, and then stopped with acid and OD450 nm measurements were made with a plate reader. ( b ) Different combinations of the ubiquitin reaction components were used to evaluate the specificity of the ubiquitylation reaction (E3, GST-ITCH; E3m, E3 ligase dead mutant GST-ITCH C830A). ( c ) Complete reactions were performed as in ( b ) using a range of E3 or E3m concentrations immobilized to the ELISA plate as shown. ( d ) Normalized screening data for 1040 compounds from the NINDS library. Immobilized GST-ITCH was incubated with test compounds (10 μ M) and E1/E2/Ub mix. After incubation at RT for 2 h, plates were developed with HRP-conjugated anti-FLAG and TMB substrate as above. Percentage residual activity (%RA) was calculated using the formula %RA=(OD450 sample—mean OD450 low controls)/(mean high controls—mean OD450 low controls) × 100. Z prime values were calculated with a threshold of > 0.5 set for acceptable data. 70 and 50% thresholds are indicated with lines. ( e ) Confirmation of six positive hits using does response and the ELISA system as in Figure 1c
    Figure Legend Snippet: High throughput screening (HTS) for ITCH inhibitors. ( a ) Schematic representation of the layout of the ELISA assay used for the HTS. Recombinant GST-ITCH or ubiquitin ligase dead mutant GST-ITCH C830A were immobilized to glutathione-coated ELISA plates and incubated with either complete ubiquitylation reaction mixtures containing E1, E2 (UbcH7) and FLAG-ubiquitin or partial mixtures as indicated in ( b ). Reactions were performed for 1 h at RT and stopped by washing with PBST before development with HRP-conjugated anti-FLAG antibody for 1 h at RT. After final washes, the wells were incubated with TMB substrate for 15 min at RT, and then stopped with acid and OD450 nm measurements were made with a plate reader. ( b ) Different combinations of the ubiquitin reaction components were used to evaluate the specificity of the ubiquitylation reaction (E3, GST-ITCH; E3m, E3 ligase dead mutant GST-ITCH C830A). ( c ) Complete reactions were performed as in ( b ) using a range of E3 or E3m concentrations immobilized to the ELISA plate as shown. ( d ) Normalized screening data for 1040 compounds from the NINDS library. Immobilized GST-ITCH was incubated with test compounds (10 μ M) and E1/E2/Ub mix. After incubation at RT for 2 h, plates were developed with HRP-conjugated anti-FLAG and TMB substrate as above. Percentage residual activity (%RA) was calculated using the formula %RA=(OD450 sample—mean OD450 low controls)/(mean high controls—mean OD450 low controls) × 100. Z prime values were calculated with a threshold of > 0.5 set for acceptable data. 70 and 50% thresholds are indicated with lines. ( e ) Confirmation of six positive hits using does response and the ELISA system as in Figure 1c

    Techniques Used: High Throughput Screening Assay, Enzyme-linked Immunosorbent Assay, Recombinant, Mutagenesis, Incubation, Activity Assay

    2) Product Images from "A PCR-Based Method for RNA Probes and Applications in Neuroscience"

    Article Title: A PCR-Based Method for RNA Probes and Applications in Neuroscience

    Journal: Frontiers in Neuroscience

    doi: 10.3389/fnins.2018.00266

    Preparation and visualization of SST probe in mouse brain sections. Two-step polymerase chain reaction (PCR) amplifications were performed and PCR products were examined by agarose gel electrophoresis. (A) Products of SST from the first PCR. (B) Products of SST containing the T7 promoter from the second PCR. (C) In vitro -transcribed RNA probe of SST. (D) Staining for SST mRNA expression revealed the effect of tissue permeability on signal intensity. The left images show treatment with 1 × PBST (1% Tween-20 in 0.01 M PBS) for 20 min at room temperature (RT); the middle images show treatment with 2 μg/ml proteinase K at RT; and the right images show treatment with 2 μg/ml proteinase K at 37°C. The upper images were captured using 10 × magnification (scale bar = 500 μm), and the bottom images were captured using 20 × magnification (scale bar = 100 μm). (E) Sections were stained with different concentrations of the SST probe at 0, 0.5, 2, and 4 μg/ml, respectively. Images were captured using 10 × magnification (scale bar = 200 μm). SST, somatostatin.
    Figure Legend Snippet: Preparation and visualization of SST probe in mouse brain sections. Two-step polymerase chain reaction (PCR) amplifications were performed and PCR products were examined by agarose gel electrophoresis. (A) Products of SST from the first PCR. (B) Products of SST containing the T7 promoter from the second PCR. (C) In vitro -transcribed RNA probe of SST. (D) Staining for SST mRNA expression revealed the effect of tissue permeability on signal intensity. The left images show treatment with 1 × PBST (1% Tween-20 in 0.01 M PBS) for 20 min at room temperature (RT); the middle images show treatment with 2 μg/ml proteinase K at RT; and the right images show treatment with 2 μg/ml proteinase K at 37°C. The upper images were captured using 10 × magnification (scale bar = 500 μm), and the bottom images were captured using 20 × magnification (scale bar = 100 μm). (E) Sections were stained with different concentrations of the SST probe at 0, 0.5, 2, and 4 μg/ml, respectively. Images were captured using 10 × magnification (scale bar = 200 μm). SST, somatostatin.

    Techniques Used: Polymerase Chain Reaction, Agarose Gel Electrophoresis, In Vitro, Staining, Expressing, Permeability

    3) Product Images from "Suppression of p75 Neurotrophin Receptor Surface Expression with Intrabodies Influences Bcl-xL mRNA Expression and Neurite Outgrowth in PC12 Cells"

    Article Title: Suppression of p75 Neurotrophin Receptor Surface Expression with Intrabodies Influences Bcl-xL mRNA Expression and Neurite Outgrowth in PC12 Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0030684

    Competition ELISA for epitope overlapping. 100 ng of mouse p75NTRex-Fc fusion protein was immobilized in plates for each well. Serial diluted p75NTR-specific scFvs were added and incubated for 1.5 hr at 37°C. After 3× washing with PBST, the plates were incubated with mouse anti-p75NTR mAb (MLR2, 1∶5,000) for 1.5 hr at 37°C. The plate was washed 3× with PBST. The scFvs and mouse anti-p75NTR mAb (MLR2) were detected by mouse anti-His 5 mAb HRP conjugated (1∶5,000) and goat anti-mouse IgG HRP conjugated (1∶5,000) in corresponding plates.
    Figure Legend Snippet: Competition ELISA for epitope overlapping. 100 ng of mouse p75NTRex-Fc fusion protein was immobilized in plates for each well. Serial diluted p75NTR-specific scFvs were added and incubated for 1.5 hr at 37°C. After 3× washing with PBST, the plates were incubated with mouse anti-p75NTR mAb (MLR2, 1∶5,000) for 1.5 hr at 37°C. The plate was washed 3× with PBST. The scFvs and mouse anti-p75NTR mAb (MLR2) were detected by mouse anti-His 5 mAb HRP conjugated (1∶5,000) and goat anti-mouse IgG HRP conjugated (1∶5,000) in corresponding plates.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Incubation

    Stress response (UPR) in cells transfected with intrabody construct SH325-G7-KDEL. The SH325-G7-KDEL transfected PC12 cells from different time points (2–8 days) were sorted based on the EGFP-F fluorescence. Cells treated with 20 µg/mL of tunicamycin (Tun) or solvent alone (DMSO) were used as the positive or negative control, respectively. Cell extracts were prepared and blotted on a PVDF membrane. The membrane was incubated with rabbit anti-GRP94 (1∶1,000) and rabbit anti-GAPDH (1∶5,000) for 1 hr at RT. After 3× washing with PBST, the membrane was subsequently incubated with goat anti-rabbit IgG AP conjugated antibody (1∶5,000) for 1 hr at RT. GAPDH served as an internal control to ensure equal protein loading.
    Figure Legend Snippet: Stress response (UPR) in cells transfected with intrabody construct SH325-G7-KDEL. The SH325-G7-KDEL transfected PC12 cells from different time points (2–8 days) were sorted based on the EGFP-F fluorescence. Cells treated with 20 µg/mL of tunicamycin (Tun) or solvent alone (DMSO) were used as the positive or negative control, respectively. Cell extracts were prepared and blotted on a PVDF membrane. The membrane was incubated with rabbit anti-GRP94 (1∶1,000) and rabbit anti-GAPDH (1∶5,000) for 1 hr at RT. After 3× washing with PBST, the membrane was subsequently incubated with goat anti-rabbit IgG AP conjugated antibody (1∶5,000) for 1 hr at RT. GAPDH served as an internal control to ensure equal protein loading.

    Techniques Used: Transfection, Construct, Fluorescence, Negative Control, Incubation

    4) Product Images from "Estrogen Affects Levels of Bcl-2 Protein and mRNA in Medial Amygdala of Ovariectomized Rats"

    Article Title: Estrogen Affects Levels of Bcl-2 Protein and mRNA in Medial Amygdala of Ovariectomized Rats

    Journal: Journal of neuroscience research

    doi: 10.1002/jnr.21801

    Comparison of levels of Bcl-2 protein following various E regimens by gold immunolabeling in the medial (MeA) and central (CeA) amygdala. (A) Low magnification light micrographs of tissue sections from MeA and CeA of rats treated with 2.5μg/14d demonstrating the specificity of the antibody (Ab) to Bcl-2. In the negative control on the left, the primary antibody was omitted and replaced by 1% BSA in PBST containing 0.25% Triton X-100. No labeling is visible. In the preabsoption control in the middle, the antibody was preabsorbed with Bcl-2 blocking peptide and this solution was incubated with the tissue section, as described in the Results; no labeling is visible on the section. Incubation of the section with the antibody to Bcl-2 resulted in labeling of cell bodies throughout the section on the right. opt, Optic nerve. Scale bar = 150 μm. (B) Low and high magnification light micrographs of Bcl-2 immunolabeling in the CeA and MeA of ovariectomized E- and vehicle-treated rats. Top: Low magnification light micrographs of Bcl-2 immunoreactivity in the CeA and MeA of rats treated with the indicated regimens. Scale bar = 250μm. Bottom: Bcl-2 immunopositive cell bodies in the CeA and MeA at high magnification Scale bar = 10μm. (C) Quantitation of Bcl-2 immunogold labeling (number of immunogold particles per 100μm 2 area) in MeA (top) and CeA (bottom). There was a significant difference among treatment groups in MeA ( F 3, 22 =15.4, P
    Figure Legend Snippet: Comparison of levels of Bcl-2 protein following various E regimens by gold immunolabeling in the medial (MeA) and central (CeA) amygdala. (A) Low magnification light micrographs of tissue sections from MeA and CeA of rats treated with 2.5μg/14d demonstrating the specificity of the antibody (Ab) to Bcl-2. In the negative control on the left, the primary antibody was omitted and replaced by 1% BSA in PBST containing 0.25% Triton X-100. No labeling is visible. In the preabsoption control in the middle, the antibody was preabsorbed with Bcl-2 blocking peptide and this solution was incubated with the tissue section, as described in the Results; no labeling is visible on the section. Incubation of the section with the antibody to Bcl-2 resulted in labeling of cell bodies throughout the section on the right. opt, Optic nerve. Scale bar = 150 μm. (B) Low and high magnification light micrographs of Bcl-2 immunolabeling in the CeA and MeA of ovariectomized E- and vehicle-treated rats. Top: Low magnification light micrographs of Bcl-2 immunoreactivity in the CeA and MeA of rats treated with the indicated regimens. Scale bar = 250μm. Bottom: Bcl-2 immunopositive cell bodies in the CeA and MeA at high magnification Scale bar = 10μm. (C) Quantitation of Bcl-2 immunogold labeling (number of immunogold particles per 100μm 2 area) in MeA (top) and CeA (bottom). There was a significant difference among treatment groups in MeA ( F 3, 22 =15.4, P

    Techniques Used: Immunolabeling, Microelectrode Array, Negative Control, Labeling, Blocking Assay, Incubation, Quantitation Assay

    5) Product Images from "A PCR-Based Method for RNA Probes and Applications in Neuroscience"

    Article Title: A PCR-Based Method for RNA Probes and Applications in Neuroscience

    Journal: Frontiers in Neuroscience

    doi: 10.3389/fnins.2018.00266

    Preparation and visualization of SST probe in mouse brain sections. Two-step polymerase chain reaction (PCR) amplifications were performed and PCR products were examined by agarose gel electrophoresis. (A) Products of SST from the first PCR. (B) Products of SST containing the T7 promoter from the second PCR. (C) In vitro -transcribed RNA probe of SST. (D) Staining for SST mRNA expression revealed the effect of tissue permeability on signal intensity. The left images show treatment with 1 × PBST (1% Tween-20 in 0.01 M PBS) for 20 min at room temperature (RT); the middle images show treatment with 2 μg/ml proteinase K at RT; and the right images show treatment with 2 μg/ml proteinase K at 37°C. The upper images were captured using 10 × magnification (scale bar = 500 μm), and the bottom images were captured using 20 × magnification (scale bar = 100 μm). (E) Sections were stained with different concentrations of the SST probe at 0, 0.5, 2, and 4 μg/ml, respectively. Images were captured using 10 × magnification (scale bar = 200 μm). SST, somatostatin.
    Figure Legend Snippet: Preparation and visualization of SST probe in mouse brain sections. Two-step polymerase chain reaction (PCR) amplifications were performed and PCR products were examined by agarose gel electrophoresis. (A) Products of SST from the first PCR. (B) Products of SST containing the T7 promoter from the second PCR. (C) In vitro -transcribed RNA probe of SST. (D) Staining for SST mRNA expression revealed the effect of tissue permeability on signal intensity. The left images show treatment with 1 × PBST (1% Tween-20 in 0.01 M PBS) for 20 min at room temperature (RT); the middle images show treatment with 2 μg/ml proteinase K at RT; and the right images show treatment with 2 μg/ml proteinase K at 37°C. The upper images were captured using 10 × magnification (scale bar = 500 μm), and the bottom images were captured using 20 × magnification (scale bar = 100 μm). (E) Sections were stained with different concentrations of the SST probe at 0, 0.5, 2, and 4 μg/ml, respectively. Images were captured using 10 × magnification (scale bar = 200 μm). SST, somatostatin.

    Techniques Used: Polymerase Chain Reaction, Agarose Gel Electrophoresis, In Vitro, Staining, Expressing, Permeability

    6) Product Images from "Identification of a novel protein promoting the colonization and survival of Finegoldia magna, a bacterial commensal and opportunistic pathogen"

    Article Title: Identification of a novel protein promoting the colonization and survival of Finegoldia magna, a bacterial commensal and opportunistic pathogen

    Journal: Molecular Microbiology

    doi: 10.1111/j.1365-2958.2008.06439.x

    F. magna bacteria adhere to basement membranes. Human skin biopsies were incubated with ALB8 or 505 bacteria for 1 h at room temperature. Non-adherent bacteria were removed by washing in PBS, and the biopsies were incubated anaerobically at 37°C for 48 h, washed with PBST, fixed and prepared for SEM. A. ALB8 bacteria; B. 505 bacteria. The arrows point at ALB8 colonies and the arrowheads point at the basement membrane covering the junction between epidermis and dermis. The bar represents 10 μm.
    Figure Legend Snippet: F. magna bacteria adhere to basement membranes. Human skin biopsies were incubated with ALB8 or 505 bacteria for 1 h at room temperature. Non-adherent bacteria were removed by washing in PBS, and the biopsies were incubated anaerobically at 37°C for 48 h, washed with PBST, fixed and prepared for SEM. A. ALB8 bacteria; B. 505 bacteria. The arrows point at ALB8 colonies and the arrowheads point at the basement membrane covering the junction between epidermis and dermis. The bar represents 10 μm.

    Techniques Used: Incubation

    7) Product Images from "Suppression of p75 Neurotrophin Receptor Surface Expression with Intrabodies Influences Bcl-xL mRNA Expression and Neurite Outgrowth in PC12 Cells"

    Article Title: Suppression of p75 Neurotrophin Receptor Surface Expression with Intrabodies Influences Bcl-xL mRNA Expression and Neurite Outgrowth in PC12 Cells

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0030684

    Competition ELISA for epitope overlapping. 100 ng of mouse p75NTRex-Fc fusion protein was immobilized in plates for each well. Serial diluted p75NTR-specific scFvs were added and incubated for 1.5 hr at 37°C. After 3× washing with PBST, the plates were incubated with mouse anti-p75NTR mAb (MLR2, 1∶5,000) for 1.5 hr at 37°C. The plate was washed 3× with PBST. The scFvs and mouse anti-p75NTR mAb (MLR2) were detected by mouse anti-His 5 mAb HRP conjugated (1∶5,000) and goat anti-mouse IgG HRP conjugated (1∶5,000) in corresponding plates.
    Figure Legend Snippet: Competition ELISA for epitope overlapping. 100 ng of mouse p75NTRex-Fc fusion protein was immobilized in plates for each well. Serial diluted p75NTR-specific scFvs were added and incubated for 1.5 hr at 37°C. After 3× washing with PBST, the plates were incubated with mouse anti-p75NTR mAb (MLR2, 1∶5,000) for 1.5 hr at 37°C. The plate was washed 3× with PBST. The scFvs and mouse anti-p75NTR mAb (MLR2) were detected by mouse anti-His 5 mAb HRP conjugated (1∶5,000) and goat anti-mouse IgG HRP conjugated (1∶5,000) in corresponding plates.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Incubation

    Stress response (UPR) in cells transfected with intrabody construct SH325-G7-KDEL. The SH325-G7-KDEL transfected PC12 cells from different time points (2–8 days) were sorted based on the EGFP-F fluorescence. Cells treated with 20 µg/mL of tunicamycin (Tun) or solvent alone (DMSO) were used as the positive or negative control, respectively. Cell extracts were prepared and blotted on a PVDF membrane. The membrane was incubated with rabbit anti-GRP94 (1∶1,000) and rabbit anti-GAPDH (1∶5,000) for 1 hr at RT. After 3× washing with PBST, the membrane was subsequently incubated with goat anti-rabbit IgG AP conjugated antibody (1∶5,000) for 1 hr at RT. GAPDH served as an internal control to ensure equal protein loading.
    Figure Legend Snippet: Stress response (UPR) in cells transfected with intrabody construct SH325-G7-KDEL. The SH325-G7-KDEL transfected PC12 cells from different time points (2–8 days) were sorted based on the EGFP-F fluorescence. Cells treated with 20 µg/mL of tunicamycin (Tun) or solvent alone (DMSO) were used as the positive or negative control, respectively. Cell extracts were prepared and blotted on a PVDF membrane. The membrane was incubated with rabbit anti-GRP94 (1∶1,000) and rabbit anti-GAPDH (1∶5,000) for 1 hr at RT. After 3× washing with PBST, the membrane was subsequently incubated with goat anti-rabbit IgG AP conjugated antibody (1∶5,000) for 1 hr at RT. GAPDH served as an internal control to ensure equal protein loading.

    Techniques Used: Transfection, Construct, Fluorescence, Negative Control, Incubation

    8) Product Images from "High throughput screening for inhibitors of the HECT ubiquitin E3 ligase ITCH identifies antidepressant drugs as regulators of autophagy"

    Article Title: High throughput screening for inhibitors of the HECT ubiquitin E3 ligase ITCH identifies antidepressant drugs as regulators of autophagy

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2014.113

    High throughput screening (HTS) for ITCH inhibitors. ( a ) Schematic representation of the layout of the ELISA assay used for the HTS. Recombinant GST-ITCH or ubiquitin ligase dead mutant GST-ITCH C830A were immobilized to glutathione-coated ELISA plates and incubated with either complete ubiquitylation reaction mixtures containing E1, E2 (UbcH7) and FLAG-ubiquitin or partial mixtures as indicated in ( b ). Reactions were performed for 1 h at RT and stopped by washing with PBST before development with HRP-conjugated anti-FLAG antibody for 1 h at RT. After final washes, the wells were incubated with TMB substrate for 15 min at RT, and then stopped with acid and OD450 nm measurements were made with a plate reader. ( b ) Different combinations of the ubiquitin reaction components were used to evaluate the specificity of the ubiquitylation reaction (E3, GST-ITCH; E3m, E3 ligase dead mutant GST-ITCH C830A). ( c ) Complete reactions were performed as in ( b ) using a range of E3 or E3m concentrations immobilized to the ELISA plate as shown. ( d ) Normalized screening data for 1040 compounds from the NINDS library. Immobilized GST-ITCH was incubated with test compounds (10 μ M) and E1/E2/Ub mix. After incubation at RT for 2 h, plates were developed with HRP-conjugated anti-FLAG and TMB substrate as above. Percentage residual activity (%RA) was calculated using the formula %RA=(OD450 sample—mean OD450 low controls)/(mean high controls—mean OD450 low controls) × 100. Z prime values were calculated with a threshold of > 0.5 set for acceptable data. 70 and 50% thresholds are indicated with lines. ( e ) Confirmation of six positive hits using does response and the ELISA system as in Figure 1c
    Figure Legend Snippet: High throughput screening (HTS) for ITCH inhibitors. ( a ) Schematic representation of the layout of the ELISA assay used for the HTS. Recombinant GST-ITCH or ubiquitin ligase dead mutant GST-ITCH C830A were immobilized to glutathione-coated ELISA plates and incubated with either complete ubiquitylation reaction mixtures containing E1, E2 (UbcH7) and FLAG-ubiquitin or partial mixtures as indicated in ( b ). Reactions were performed for 1 h at RT and stopped by washing with PBST before development with HRP-conjugated anti-FLAG antibody for 1 h at RT. After final washes, the wells were incubated with TMB substrate for 15 min at RT, and then stopped with acid and OD450 nm measurements were made with a plate reader. ( b ) Different combinations of the ubiquitin reaction components were used to evaluate the specificity of the ubiquitylation reaction (E3, GST-ITCH; E3m, E3 ligase dead mutant GST-ITCH C830A). ( c ) Complete reactions were performed as in ( b ) using a range of E3 or E3m concentrations immobilized to the ELISA plate as shown. ( d ) Normalized screening data for 1040 compounds from the NINDS library. Immobilized GST-ITCH was incubated with test compounds (10 μ M) and E1/E2/Ub mix. After incubation at RT for 2 h, plates were developed with HRP-conjugated anti-FLAG and TMB substrate as above. Percentage residual activity (%RA) was calculated using the formula %RA=(OD450 sample—mean OD450 low controls)/(mean high controls—mean OD450 low controls) × 100. Z prime values were calculated with a threshold of > 0.5 set for acceptable data. 70 and 50% thresholds are indicated with lines. ( e ) Confirmation of six positive hits using does response and the ELISA system as in Figure 1c

    Techniques Used: High Throughput Screening Assay, Enzyme-linked Immunosorbent Assay, Recombinant, Mutagenesis, Incubation, Activity Assay

    9) Product Images from "Estrogen Affects Levels of Bcl-2 Protein and mRNA in Medial Amygdala of Ovariectomized Rats"

    Article Title: Estrogen Affects Levels of Bcl-2 Protein and mRNA in Medial Amygdala of Ovariectomized Rats

    Journal: Journal of neuroscience research

    doi: 10.1002/jnr.21801

    Comparison of levels of Bcl-2 protein following various E regimens by gold immunolabeling in the medial (MeA) and central (CeA) amygdala. (A) Low magnification light micrographs of tissue sections from MeA and CeA of rats treated with 2.5μg/14d demonstrating the specificity of the antibody (Ab) to Bcl-2. In the negative control on the left, the primary antibody was omitted and replaced by 1% BSA in PBST containing 0.25% Triton X-100. No labeling is visible. In the preabsoption control in the middle, the antibody was preabsorbed with Bcl-2 blocking peptide and this solution was incubated with the tissue section, as described in the Results; no labeling is visible on the section. Incubation of the section with the antibody to Bcl-2 resulted in labeling of cell bodies throughout the section on the right. opt, Optic nerve. Scale bar = 150 μm. (B) Low and high magnification light micrographs of Bcl-2 immunolabeling in the CeA and MeA of ovariectomized E- and vehicle-treated rats. Top: Low magnification light micrographs of Bcl-2 immunoreactivity in the CeA and MeA of rats treated with the indicated regimens. Scale bar = 250μm. Bottom: Bcl-2 immunopositive cell bodies in the CeA and MeA at high magnification Scale bar = 10μm. (C) Quantitation of Bcl-2 immunogold labeling (number of immunogold particles per 100μm 2 area) in MeA (top) and CeA (bottom). There was a significant difference among treatment groups in MeA ( F 3, 22 =15.4, P
    Figure Legend Snippet: Comparison of levels of Bcl-2 protein following various E regimens by gold immunolabeling in the medial (MeA) and central (CeA) amygdala. (A) Low magnification light micrographs of tissue sections from MeA and CeA of rats treated with 2.5μg/14d demonstrating the specificity of the antibody (Ab) to Bcl-2. In the negative control on the left, the primary antibody was omitted and replaced by 1% BSA in PBST containing 0.25% Triton X-100. No labeling is visible. In the preabsoption control in the middle, the antibody was preabsorbed with Bcl-2 blocking peptide and this solution was incubated with the tissue section, as described in the Results; no labeling is visible on the section. Incubation of the section with the antibody to Bcl-2 resulted in labeling of cell bodies throughout the section on the right. opt, Optic nerve. Scale bar = 150 μm. (B) Low and high magnification light micrographs of Bcl-2 immunolabeling in the CeA and MeA of ovariectomized E- and vehicle-treated rats. Top: Low magnification light micrographs of Bcl-2 immunoreactivity in the CeA and MeA of rats treated with the indicated regimens. Scale bar = 250μm. Bottom: Bcl-2 immunopositive cell bodies in the CeA and MeA at high magnification Scale bar = 10μm. (C) Quantitation of Bcl-2 immunogold labeling (number of immunogold particles per 100μm 2 area) in MeA (top) and CeA (bottom). There was a significant difference among treatment groups in MeA ( F 3, 22 =15.4, P

    Techniques Used: Immunolabeling, Microelectrode Array, Negative Control, Labeling, Blocking Assay, Incubation, Quantitation Assay

    10) Product Images from "Generation and characterization of the human neutralizing antibody fragment Fab091 against rabies virus"

    Article Title: Generation and characterization of the human neutralizing antibody fragment Fab091 against rabies virus

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2010.209

    Indirect ELISA of the different dilutions of Fab091 fragment. The ELISA plate was coated with rabies virus strain CTN at 2 μg/mL. (1–8): The virus reacted with Fab091 which was in serial two-fold dilution (1:5, 1:10, 1:20, 1:40, 1:80, 1:160, 1:320, and 1:640) and incubated for 2h at room temperature. E coli Top10F' supernatant was used as control. The plate was washed five times with PBST, followed by incubation with goat anti-human IgG HRP-conjugated (1:5000).
    Figure Legend Snippet: Indirect ELISA of the different dilutions of Fab091 fragment. The ELISA plate was coated with rabies virus strain CTN at 2 μg/mL. (1–8): The virus reacted with Fab091 which was in serial two-fold dilution (1:5, 1:10, 1:20, 1:40, 1:80, 1:160, 1:320, and 1:640) and incubated for 2h at room temperature. E coli Top10F' supernatant was used as control. The plate was washed five times with PBST, followed by incubation with goat anti-human IgG HRP-conjugated (1:5000).

    Techniques Used: Indirect ELISA, Enzyme-linked Immunosorbent Assay, Incubation

    11) Product Images from "Generation and characterization of the human neutralizing antibody fragment Fab091 against rabies virus"

    Article Title: Generation and characterization of the human neutralizing antibody fragment Fab091 against rabies virus

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2010.209

    Indirect ELISA of the different dilutions of Fab091 fragment. The ELISA plate was coated with rabies virus strain CTN at 2 μg/mL. (1–8): The virus reacted with Fab091 which was in serial two-fold dilution (1:5, 1:10, 1:20, 1:40, 1:80, 1:160, 1:320, and 1:640) and incubated for 2h at room temperature. E coli Top10F' supernatant was used as control. The plate was washed five times with PBST, followed by incubation with goat anti-human IgG HRP-conjugated (1:5000).
    Figure Legend Snippet: Indirect ELISA of the different dilutions of Fab091 fragment. The ELISA plate was coated with rabies virus strain CTN at 2 μg/mL. (1–8): The virus reacted with Fab091 which was in serial two-fold dilution (1:5, 1:10, 1:20, 1:40, 1:80, 1:160, 1:320, and 1:640) and incubated for 2h at room temperature. E coli Top10F' supernatant was used as control. The plate was washed five times with PBST, followed by incubation with goat anti-human IgG HRP-conjugated (1:5000).

    Techniques Used: Indirect ELISA, Enzyme-linked Immunosorbent Assay, Incubation

    12) Product Images from "Broadening the versatility of lentiviral vectors as a tool in nucleic acid research via genetic code expansion"

    Article Title: Broadening the versatility of lentiviral vectors as a tool in nucleic acid research via genetic code expansion

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkv202

    Development of a NAEK-containing lentiviral vector as a vehicle for the selective delivery of nucleic acid macromolecules into cells with high expression of integrins. ( A ) Expression of integrin α v β 3 in MDA-MB-435S vs. MCF-7 cells as detected by flow cytometry. The trypsinized cells, after sequential blocking by 10% BSA and washing, were incubated with monoclonal integrin α v β 3 antibody (red line) and an isotype control IgG antibody (green line) overnight in parallel and then incubated with Alexa 488 labeled secondary antibody for 1 h. After washing three times with PBST, the treated cells were analyzed by Guava EasyCyte Plus. The level of integrin α v β 3 expression on the cell surface of MDA-MB-435S cells is almost 3-fold higher than that on MCF-7 cells according to flow cytometry. ( B ) Characterization of the enhanced infectivity of NAEK-containing lentiviral vectors (Vector) and vectors upon conjugation with RGD (Vector-RGD) or RAD (Vector-RAD) at different sites towards MDA-MB-435S cells. The significance was confirmed by one-way ANOVA test (* P
    Figure Legend Snippet: Development of a NAEK-containing lentiviral vector as a vehicle for the selective delivery of nucleic acid macromolecules into cells with high expression of integrins. ( A ) Expression of integrin α v β 3 in MDA-MB-435S vs. MCF-7 cells as detected by flow cytometry. The trypsinized cells, after sequential blocking by 10% BSA and washing, were incubated with monoclonal integrin α v β 3 antibody (red line) and an isotype control IgG antibody (green line) overnight in parallel and then incubated with Alexa 488 labeled secondary antibody for 1 h. After washing three times with PBST, the treated cells were analyzed by Guava EasyCyte Plus. The level of integrin α v β 3 expression on the cell surface of MDA-MB-435S cells is almost 3-fold higher than that on MCF-7 cells according to flow cytometry. ( B ) Characterization of the enhanced infectivity of NAEK-containing lentiviral vectors (Vector) and vectors upon conjugation with RGD (Vector-RGD) or RAD (Vector-RAD) at different sites towards MDA-MB-435S cells. The significance was confirmed by one-way ANOVA test (* P

    Techniques Used: Plasmid Preparation, Expressing, Multiple Displacement Amplification, Flow Cytometry, Cytometry, Blocking Assay, Incubation, Labeling, Infection, Conjugation Assay

    13) Product Images from "Is Trichloroacetic Acid an Insufficient Sample Quencher of Redox Reactions?"

    Article Title: Is Trichloroacetic Acid an Insufficient Sample Quencher of Redox Reactions?

    Journal: Antioxidants & Redox Signaling

    doi: 10.1089/ars.2012.4949

    The activity of TCA as quencher of β-actin reduction by DTT. ELISA plates were coated with β-actin. The wells were then reduced by 1 m M or 5 m M DTT in PBST or TCA, respectively. Subsequently, the wells were exposed to biotin-maleimide,
    Figure Legend Snippet: The activity of TCA as quencher of β-actin reduction by DTT. ELISA plates were coated with β-actin. The wells were then reduced by 1 m M or 5 m M DTT in PBST or TCA, respectively. Subsequently, the wells were exposed to biotin-maleimide,

    Techniques Used: Activity Assay, Enzyme-linked Immunosorbent Assay

    14) Product Images from "Is Trichloroacetic Acid an Insufficient Sample Quencher of Redox Reactions?"

    Article Title: Is Trichloroacetic Acid an Insufficient Sample Quencher of Redox Reactions?

    Journal: Antioxidants & Redox Signaling

    doi: 10.1089/ars.2012.4949

    The activity of TCA as quencher of β-actin reduction by DTT. ELISA plates were coated with β-actin. The wells were then reduced by 1 m M or 5 m M DTT in PBST or TCA, respectively. Subsequently, the wells were exposed to biotin-maleimide,
    Figure Legend Snippet: The activity of TCA as quencher of β-actin reduction by DTT. ELISA plates were coated with β-actin. The wells were then reduced by 1 m M or 5 m M DTT in PBST or TCA, respectively. Subsequently, the wells were exposed to biotin-maleimide,

    Techniques Used: Activity Assay, Enzyme-linked Immunosorbent Assay

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    Millipore pbst
    Development of a NAEK-containing lentiviral vector as a vehicle for the selective delivery of nucleic acid macromolecules into cells with high expression of integrins. ( A ) Expression of integrin α v β 3 in MDA-MB-435S vs. MCF-7 cells as detected by flow cytometry. The trypsinized cells, after sequential blocking by 10% <t>BSA</t> and washing, were incubated with monoclonal integrin α v β 3 antibody (red line) and an isotype control IgG antibody (green line) overnight in parallel and then incubated with Alexa 488 labeled secondary antibody for 1 h. After washing three times with <t>PBST,</t> the treated cells were analyzed by Guava EasyCyte Plus. The level of integrin α v β 3 expression on the cell surface of MDA-MB-435S cells is almost 3-fold higher than that on MCF-7 cells according to flow cytometry. ( B ) Characterization of the enhanced infectivity of NAEK-containing lentiviral vectors (Vector) and vectors upon conjugation with RGD (Vector-RGD) or RAD (Vector-RAD) at different sites towards MDA-MB-435S cells. The significance was confirmed by one-way ANOVA test (* P
    Pbst, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Development of a NAEK-containing lentiviral vector as a vehicle for the selective delivery of nucleic acid macromolecules into cells with high expression of integrins. ( A ) Expression of integrin α v β 3 in MDA-MB-435S vs. MCF-7 cells as detected by flow cytometry. The trypsinized cells, after sequential blocking by 10% BSA and washing, were incubated with monoclonal integrin α v β 3 antibody (red line) and an isotype control IgG antibody (green line) overnight in parallel and then incubated with Alexa 488 labeled secondary antibody for 1 h. After washing three times with PBST, the treated cells were analyzed by Guava EasyCyte Plus. The level of integrin α v β 3 expression on the cell surface of MDA-MB-435S cells is almost 3-fold higher than that on MCF-7 cells according to flow cytometry. ( B ) Characterization of the enhanced infectivity of NAEK-containing lentiviral vectors (Vector) and vectors upon conjugation with RGD (Vector-RGD) or RAD (Vector-RAD) at different sites towards MDA-MB-435S cells. The significance was confirmed by one-way ANOVA test (* P

    Journal: Nucleic Acids Research

    Article Title: Broadening the versatility of lentiviral vectors as a tool in nucleic acid research via genetic code expansion

    doi: 10.1093/nar/gkv202

    Figure Lengend Snippet: Development of a NAEK-containing lentiviral vector as a vehicle for the selective delivery of nucleic acid macromolecules into cells with high expression of integrins. ( A ) Expression of integrin α v β 3 in MDA-MB-435S vs. MCF-7 cells as detected by flow cytometry. The trypsinized cells, after sequential blocking by 10% BSA and washing, were incubated with monoclonal integrin α v β 3 antibody (red line) and an isotype control IgG antibody (green line) overnight in parallel and then incubated with Alexa 488 labeled secondary antibody for 1 h. After washing three times with PBST, the treated cells were analyzed by Guava EasyCyte Plus. The level of integrin α v β 3 expression on the cell surface of MDA-MB-435S cells is almost 3-fold higher than that on MCF-7 cells according to flow cytometry. ( B ) Characterization of the enhanced infectivity of NAEK-containing lentiviral vectors (Vector) and vectors upon conjugation with RGD (Vector-RGD) or RAD (Vector-RAD) at different sites towards MDA-MB-435S cells. The significance was confirmed by one-way ANOVA test (* P

    Article Snippet: The treated cells were blocked with 10% BSA in PBST for 1 h, washed and incubated with monoclonal anti-integrin αv β3 (Millipore) (1:1000) at 4°C overnight.

    Techniques: Plasmid Preparation, Expressing, Multiple Displacement Amplification, Flow Cytometry, Cytometry, Blocking Assay, Incubation, Labeling, Infection, Conjugation Assay