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  • 92
    ATCC non o157 e coli
    Bacterial strains used in the study.
    Non O157 E Coli, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/non o157 e coli/product/ATCC
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    non o157 e coli - by Bioz Stars, 2024-06
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    93
    Santa Cruz Biotechnology p38α
    The ECS cell phenotype and MEK3/6 and p38 signaling. A-C) Cells were electroporated with 3 μg of Control-, MEK3-, or MEK6-siRNA and the impact on p38 activity, and spheroid formation and invasive, were measured. D) Cells were electroporated with 3 μg of Control-, MEK3-, or MEK6-siRNA, grown for 5 d as spheroids, and cell extracts (300 μg protein) were assayed for ability to enhance HUVEC tube formation as measured by junction, segment and node formation. E) Cells were electroporated with 3 μg of the indicated siRNA and p38 level and activity were measured at 48 h. F and G) Impact of p38 knockdown on spheroid formation and matrigel invasion. H and I) Treatment with SB203580, a <t>p38α/β</t> inhibitor, suppresses ECS cell spheroid formation and invasive potential. J and K) RhoA restores the ECS cell phenotype in NRP-1 knockdown cells. SCC-13 derived NRP-1 knockout cells were electroporated with 3 μg of empty vector or RhoA WT expression plasmid, and plated for spheroid formation (5 d). The immunoblot monitors NRP-1 knockdown, RhoA overexpression, and the impact on p38T and p38-P level. SCC-13 and SCC13-NRP-1-KOc8 cells were electroporated with 3 μg of the indicated plasmids and ability to form spheroids was monitored at 5 d. The asterisk indicates a significant reduction in spheroid formation in SCC13-NRP1-KOc8 cells versus SCC-13. The double asterisk indicates an increase in spheroid formation in RhoA WT expression plasmid-electroporated versus empty vector-electroporated SCC13-NRP1-KOc8 cells, n = 3, P ≤ 0.005. All bars = 100 μm. [Color figure can be viewed at wileyonlinelibrary.com]
    P38α, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p38α/product/Santa Cruz Biotechnology
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p38α - by Bioz Stars, 2024-06
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    93
    Santa Cruz Biotechnology p38α mapk shrna
    A1R-mediated decrease in GluA2 surface levels in primary hippocampal neurons was prevented by pharmacological inhibitors and genetic knockdown of p38 <t>MAPK</t> and JNK. A, Intensity levels of surface-expressed GluA2 were determined by confocal imaging and analyzing 10 μm dendritic lengths located 5 μm away from cell somas. Results showed that A1R-induced GluA2 endocytosis was inhibited by p38 MAPK inhibitor SB203580 (20 μm), but not by inactive analog SB202474, and JNK II inhibitor (5 μm), but not by its inactive analog JNK II-negative control. The compounds SB203580, SB202474, JNK II inhibitor, and JNK II-negative inhibitor were applied to hippocampal neurons for 1 h before CPA treatment (500 nm, 45 min). Surface GluA2 (green) was detected by using an antibody directed against the extracellular epitope of GluA2 in nonpermeabilized conditions, then subsequently permeabilized and stained with chicken anti-MAP2 antibody (red). The p38 MAPK and JNK inhibitors did not significantly affect CPA-mediated GluA1 internalization (see Results). B, Using an <t>shRNA</t> knockdown strategy, the shRNAs <t>p38α</t> MAPK and JNK1 prevented A1R-induced GluA2 internalization. Cultured neurons transfected with the control plasmid A (GFP-fluorescent), p38α MAPK, or JNK1 shRNA were treated with DMSO or CPA (500 nm, 45 min) and subsequently labeled with GluA2 and MAP2 as in A. CPA-induced GluA2 internalization was prevented by transfections of p38α MAPK and JNK1 shRNA plasmids. Average GluA2 intensity values in summary bar charts represent the mean ± SEM from 3 transfections, with the number of neurons indicated inside brackets. *p < 0.05 versus control. **p < 0.01 versus control. ***p < 0.001 versus control. Statistical significance was assessed using one-way ANOVA, followed by post hoc Student-Newman-Keuls test. Scale bars: A, B, 2 μm.
    P38α Mapk Shrna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/p38α mapk shrna/product/Santa Cruz Biotechnology
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p38α mapk shrna - by Bioz Stars, 2024-06
    93/100 stars
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    Image Search Results


    Bacterial strains used in the study.

    Journal: PLoS ONE

    Article Title: A Rapid Subtractive Immunization Method to Prepare Discriminatory Monoclonal Antibodies for Food E. coli O157:H7 Contamination

    doi: 10.1371/journal.pone.0031352

    Figure Lengend Snippet: Bacterial strains used in the study.

    Article Snippet: The following strains were tested including Salmonella sp. (CMCC 50325), Citrobacter freundii (IHEM 1.5001), Staphylococcus aureus (CMCC 29213), Shigella (CMCC 51081,51066), Non-O157 E. coli (CMCC 44216, 44505), E. coli O157:H19 (CMCC 44752), E. coli O157:H7 (ATCC 43895).

    Techniques:

    A, sera from Cy-treated mice (experimental group) and no Cy-treated mice (control group) were diluted and tested for antibody reactivity to E. coli O157:H19 in whole cell ELISA (OD 450 nm); B, sera were diluted and tested for reactivity to E. coli O157:H7 and E. coli O157:H19 (▪: experimental group; •: control group).

    Journal: PLoS ONE

    Article Title: A Rapid Subtractive Immunization Method to Prepare Discriminatory Monoclonal Antibodies for Food E. coli O157:H7 Contamination

    doi: 10.1371/journal.pone.0031352

    Figure Lengend Snippet: A, sera from Cy-treated mice (experimental group) and no Cy-treated mice (control group) were diluted and tested for antibody reactivity to E. coli O157:H19 in whole cell ELISA (OD 450 nm); B, sera were diluted and tested for reactivity to E. coli O157:H7 and E. coli O157:H19 (▪: experimental group; •: control group).

    Article Snippet: The following strains were tested including Salmonella sp. (CMCC 50325), Citrobacter freundii (IHEM 1.5001), Staphylococcus aureus (CMCC 29213), Shigella (CMCC 51081,51066), Non-O157 E. coli (CMCC 44216, 44505), E. coli O157:H19 (CMCC 44752), E. coli O157:H7 (ATCC 43895).

    Techniques: Enzyme-linked Immunosorbent Assay

    Summary of the characteristic of some mAbs reacting with Escherichia coli  O157:H7  and others.

    Journal: PLoS ONE

    Article Title: A Rapid Subtractive Immunization Method to Prepare Discriminatory Monoclonal Antibodies for Food E. coli O157:H7 Contamination

    doi: 10.1371/journal.pone.0031352

    Figure Lengend Snippet: Summary of the characteristic of some mAbs reacting with Escherichia coli O157:H7 and others.

    Article Snippet: The following strains were tested including Salmonella sp. (CMCC 50325), Citrobacter freundii (IHEM 1.5001), Staphylococcus aureus (CMCC 29213), Shigella (CMCC 51081,51066), Non-O157 E. coli (CMCC 44216, 44505), E. coli O157:H19 (CMCC 44752), E. coli O157:H7 (ATCC 43895).

    Techniques:

    The characteristics of mAbs against E. coli  O157:H7.

    Journal: PLoS ONE

    Article Title: A Rapid Subtractive Immunization Method to Prepare Discriminatory Monoclonal Antibodies for Food E. coli O157:H7 Contamination

    doi: 10.1371/journal.pone.0031352

    Figure Lengend Snippet: The characteristics of mAbs against E. coli O157:H7.

    Article Snippet: The following strains were tested including Salmonella sp. (CMCC 50325), Citrobacter freundii (IHEM 1.5001), Staphylococcus aureus (CMCC 29213), Shigella (CMCC 51081,51066), Non-O157 E. coli (CMCC 44216, 44505), E. coli O157:H19 (CMCC 44752), E. coli O157:H7 (ATCC 43895).

    Techniques:

    E. coli O157:H7 cell lysates were subjected to SDS–PAGE, transferred to nitrocellulose filter, and probed with 1C6 (lane 1), 1D8, (lane 2), 4A7 (lane 3), 5A2 (lane 4), 5D8 (lane 5). The sizes of molecular weight standards are shown at the right (lane 6).

    Journal: PLoS ONE

    Article Title: A Rapid Subtractive Immunization Method to Prepare Discriminatory Monoclonal Antibodies for Food E. coli O157:H7 Contamination

    doi: 10.1371/journal.pone.0031352

    Figure Lengend Snippet: E. coli O157:H7 cell lysates were subjected to SDS–PAGE, transferred to nitrocellulose filter, and probed with 1C6 (lane 1), 1D8, (lane 2), 4A7 (lane 3), 5A2 (lane 4), 5D8 (lane 5). The sizes of molecular weight standards are shown at the right (lane 6).

    Article Snippet: The following strains were tested including Salmonella sp. (CMCC 50325), Citrobacter freundii (IHEM 1.5001), Staphylococcus aureus (CMCC 29213), Shigella (CMCC 51081,51066), Non-O157 E. coli (CMCC 44216, 44505), E. coli O157:H19 (CMCC 44752), E. coli O157:H7 (ATCC 43895).

    Techniques: SDS Page, Molecular Weight

    Immune-colloidal gold probes coated with mAb 5A2 were applied to special single out E. coli O157:H7 contaminated minced beef from others which included food samples contaminated by ATCC 43895 (A1,B1,C1,D1), IHEM 1.3001 (A2), IHEM 1.3002 (A3), IHEM 1.3003 (A4), CMCC 50303 (B2), CMCC 50115 (B3), CMCC 50309 (B4), CMCC 51135 (C2), CMCC 51081 (C3), CMCC 51066 (C4), CMCC 44102 (D2), CMCC 44109 (D3), CMCC 44156 (D4). Negative control A5, B5, C5, D5) refers to food samples which have no bacterial contamination.

    Journal: PLoS ONE

    Article Title: A Rapid Subtractive Immunization Method to Prepare Discriminatory Monoclonal Antibodies for Food E. coli O157:H7 Contamination

    doi: 10.1371/journal.pone.0031352

    Figure Lengend Snippet: Immune-colloidal gold probes coated with mAb 5A2 were applied to special single out E. coli O157:H7 contaminated minced beef from others which included food samples contaminated by ATCC 43895 (A1,B1,C1,D1), IHEM 1.3001 (A2), IHEM 1.3002 (A3), IHEM 1.3003 (A4), CMCC 50303 (B2), CMCC 50115 (B3), CMCC 50309 (B4), CMCC 51135 (C2), CMCC 51081 (C3), CMCC 51066 (C4), CMCC 44102 (D2), CMCC 44109 (D3), CMCC 44156 (D4). Negative control A5, B5, C5, D5) refers to food samples which have no bacterial contamination.

    Article Snippet: The following strains were tested including Salmonella sp. (CMCC 50325), Citrobacter freundii (IHEM 1.5001), Staphylococcus aureus (CMCC 29213), Shigella (CMCC 51081,51066), Non-O157 E. coli (CMCC 44216, 44505), E. coli O157:H19 (CMCC 44752), E. coli O157:H7 (ATCC 43895).

    Techniques: Negative Control

    The ECS cell phenotype and MEK3/6 and p38 signaling. A-C) Cells were electroporated with 3 μg of Control-, MEK3-, or MEK6-siRNA and the impact on p38 activity, and spheroid formation and invasive, were measured. D) Cells were electroporated with 3 μg of Control-, MEK3-, or MEK6-siRNA, grown for 5 d as spheroids, and cell extracts (300 μg protein) were assayed for ability to enhance HUVEC tube formation as measured by junction, segment and node formation. E) Cells were electroporated with 3 μg of the indicated siRNA and p38 level and activity were measured at 48 h. F and G) Impact of p38 knockdown on spheroid formation and matrigel invasion. H and I) Treatment with SB203580, a p38α/β inhibitor, suppresses ECS cell spheroid formation and invasive potential. J and K) RhoA restores the ECS cell phenotype in NRP-1 knockdown cells. SCC-13 derived NRP-1 knockout cells were electroporated with 3 μg of empty vector or RhoA WT expression plasmid, and plated for spheroid formation (5 d). The immunoblot monitors NRP-1 knockdown, RhoA overexpression, and the impact on p38T and p38-P level. SCC-13 and SCC13-NRP-1-KOc8 cells were electroporated with 3 μg of the indicated plasmids and ability to form spheroids was monitored at 5 d. The asterisk indicates a significant reduction in spheroid formation in SCC13-NRP1-KOc8 cells versus SCC-13. The double asterisk indicates an increase in spheroid formation in RhoA WT expression plasmid-electroporated versus empty vector-electroporated SCC13-NRP1-KOc8 cells, n = 3, P ≤ 0.005. All bars = 100 μm. [Color figure can be viewed at wileyonlinelibrary.com]

    Journal: Molecular carcinogenesis

    Article Title: NRP-1 interacts with GIPC1 and SYX to activate p38 MAPK signaling and cancer stem cell survival

    doi: 10.1002/mc.22943

    Figure Lengend Snippet: The ECS cell phenotype and MEK3/6 and p38 signaling. A-C) Cells were electroporated with 3 μg of Control-, MEK3-, or MEK6-siRNA and the impact on p38 activity, and spheroid formation and invasive, were measured. D) Cells were electroporated with 3 μg of Control-, MEK3-, or MEK6-siRNA, grown for 5 d as spheroids, and cell extracts (300 μg protein) were assayed for ability to enhance HUVEC tube formation as measured by junction, segment and node formation. E) Cells were electroporated with 3 μg of the indicated siRNA and p38 level and activity were measured at 48 h. F and G) Impact of p38 knockdown on spheroid formation and matrigel invasion. H and I) Treatment with SB203580, a p38α/β inhibitor, suppresses ECS cell spheroid formation and invasive potential. J and K) RhoA restores the ECS cell phenotype in NRP-1 knockdown cells. SCC-13 derived NRP-1 knockout cells were electroporated with 3 μg of empty vector or RhoA WT expression plasmid, and plated for spheroid formation (5 d). The immunoblot monitors NRP-1 knockdown, RhoA overexpression, and the impact on p38T and p38-P level. SCC-13 and SCC13-NRP-1-KOc8 cells were electroporated with 3 μg of the indicated plasmids and ability to form spheroids was monitored at 5 d. The asterisk indicates a significant reduction in spheroid formation in SCC13-NRP1-KOc8 cells versus SCC-13. The double asterisk indicates an increase in spheroid formation in RhoA WT expression plasmid-electroporated versus empty vector-electroporated SCC13-NRP1-KOc8 cells, n = 3, P ≤ 0.005. All bars = 100 μm. [Color figure can be viewed at wileyonlinelibrary.com]

    Article Snippet: Electroporation For electroporation, 1 × 10 6 cells were electroporated with 3 μg of control- (D-001206–13-05, Dharmacon), VEGF-A (sc-29520, Santa Cruz), NRP-1 (sc-36038, Santa Cruz), GIPC1 (M-019997–02-005, Dharmacon), p38α (sc-29433, Santa Cruz), p38β (sc-39116, Santa Cruz), p38γ (sc-39118, Santa Cruz), p38δ (sc-36456, Santa Cruz), MEKK1 (sc-35898, Santa Cruz), MEK3 (sc-35907, Santa Cruz), MEK6 (sc-35913, Santa Cruz), Syx (Dharmacon, M-013873–01-0005) or RhoA (Santa Cruz, sc-29471) siRNA using the Amaxa electroporator and the VPD-1002 nucleofection kit (Germany).

    Techniques: Activity Assay, Derivative Assay, Knock-Out, Plasmid Preparation, Expressing, Western Blot, Over Expression

    A1R-mediated decrease in GluA2 surface levels in primary hippocampal neurons was prevented by pharmacological inhibitors and genetic knockdown of p38 MAPK and JNK. A, Intensity levels of surface-expressed GluA2 were determined by confocal imaging and analyzing 10 μm dendritic lengths located 5 μm away from cell somas. Results showed that A1R-induced GluA2 endocytosis was inhibited by p38 MAPK inhibitor SB203580 (20 μm), but not by inactive analog SB202474, and JNK II inhibitor (5 μm), but not by its inactive analog JNK II-negative control. The compounds SB203580, SB202474, JNK II inhibitor, and JNK II-negative inhibitor were applied to hippocampal neurons for 1 h before CPA treatment (500 nm, 45 min). Surface GluA2 (green) was detected by using an antibody directed against the extracellular epitope of GluA2 in nonpermeabilized conditions, then subsequently permeabilized and stained with chicken anti-MAP2 antibody (red). The p38 MAPK and JNK inhibitors did not significantly affect CPA-mediated GluA1 internalization (see Results). B, Using an shRNA knockdown strategy, the shRNAs p38α MAPK and JNK1 prevented A1R-induced GluA2 internalization. Cultured neurons transfected with the control plasmid A (GFP-fluorescent), p38α MAPK, or JNK1 shRNA were treated with DMSO or CPA (500 nm, 45 min) and subsequently labeled with GluA2 and MAP2 as in A. CPA-induced GluA2 internalization was prevented by transfections of p38α MAPK and JNK1 shRNA plasmids. Average GluA2 intensity values in summary bar charts represent the mean ± SEM from 3 transfections, with the number of neurons indicated inside brackets. *p < 0.05 versus control. **p < 0.01 versus control. ***p < 0.001 versus control. Statistical significance was assessed using one-way ANOVA, followed by post hoc Student-Newman-Keuls test. Scale bars: A, B, 2 μm.

    Journal: The Journal of Neuroscience

    Article Title: Prolonged Adenosine A1 Receptor Activation in Hypoxia and Pial Vessel Disruption Focal Cortical Ischemia Facilitates Clathrin-Mediated AMPA Receptor Endocytosis and Long-Lasting Synaptic Inhibition in Rat Hippocampal CA3-CA1 Synapses: Differential Regulation of GluA2 and GluA1 Subunits by p38 MAPK and JNK

    doi: 10.1523/JNEUROSCI.3991-13.2014

    Figure Lengend Snippet: A1R-mediated decrease in GluA2 surface levels in primary hippocampal neurons was prevented by pharmacological inhibitors and genetic knockdown of p38 MAPK and JNK. A, Intensity levels of surface-expressed GluA2 were determined by confocal imaging and analyzing 10 μm dendritic lengths located 5 μm away from cell somas. Results showed that A1R-induced GluA2 endocytosis was inhibited by p38 MAPK inhibitor SB203580 (20 μm), but not by inactive analog SB202474, and JNK II inhibitor (5 μm), but not by its inactive analog JNK II-negative control. The compounds SB203580, SB202474, JNK II inhibitor, and JNK II-negative inhibitor were applied to hippocampal neurons for 1 h before CPA treatment (500 nm, 45 min). Surface GluA2 (green) was detected by using an antibody directed against the extracellular epitope of GluA2 in nonpermeabilized conditions, then subsequently permeabilized and stained with chicken anti-MAP2 antibody (red). The p38 MAPK and JNK inhibitors did not significantly affect CPA-mediated GluA1 internalization (see Results). B, Using an shRNA knockdown strategy, the shRNAs p38α MAPK and JNK1 prevented A1R-induced GluA2 internalization. Cultured neurons transfected with the control plasmid A (GFP-fluorescent), p38α MAPK, or JNK1 shRNA were treated with DMSO or CPA (500 nm, 45 min) and subsequently labeled with GluA2 and MAP2 as in A. CPA-induced GluA2 internalization was prevented by transfections of p38α MAPK and JNK1 shRNA plasmids. Average GluA2 intensity values in summary bar charts represent the mean ± SEM from 3 transfections, with the number of neurons indicated inside brackets. *p < 0.05 versus control. **p < 0.01 versus control. ***p < 0.001 versus control. Statistical significance was assessed using one-way ANOVA, followed by post hoc Student-Newman-Keuls test. Scale bars: A, B, 2 μm.

    Article Snippet: For transfection experiments, hippocampal neurons were transfected with 1 μg of p38α MAPK shRNA, JNK1 shRNA, or control plasmid A (Santa Cruz Biotechnology) and 2 μl Lipofectamine 2000 (Invitrogen).

    Techniques: Imaging, Negative Control, Staining, shRNA, Cell Culture, Transfection, Plasmid Preparation, Labeling