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Becton Dickinson anti actin
Anti Actin, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti actin/product/Becton Dickinson
Average 92 stars, based on 44 article reviews
Price from $9.99 to $1999.99
anti actin - by Bioz Stars, 2020-09
92/100 stars

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Article Snippet: Anti-paxillin, anti-p62, anti-actin, and anti-tubulin antibodies were purchased from BD Biosciences (San Jose, CA), MBL (Aichi, Japan), Millipore (Billerica, MA), and Invitrogen (Carlsbad, CA), respectively.

Article Title: Musk Kinase Activity is Modulated By A Serine Phosphorylation Site in The Kinase Loop
Article Snippet: Antibodies and Reagents The following antibodies were purchased from commercial sources: anti-phosphotyrosine PY99 (Santa Cruz Biotechnology, Dallas, TX) and PY-100 (Cell Signaling Technology, Leiden, The Netherlands), anti-AChR α (BD Biosciences), anti-AChR β (Sigma-Aldrich), anti-HA (Sigma-Aldrich), anti-Myc 9E10 (Sigma-Aldrich), anti-GFP (Santa Cruz), anti-Actin (BD Transduction Laboratories, Lexington, KT, USA), anti-Tubulin (Sigma-Aldrich).

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    Becton Dickinson β actin
    Optimized siRNAs showed higher and longer efficiency on IL-2 promoter activation in human or mouse primary CD4 + T cells. (A) HEK293T cells were transfected with siRNAs at the indicated concentrations and promoters activities were determined as described above. (B) Effects of optimized siRNAs on IL-2 mRNA level in human primary CD4 + T cells. Human primary CD4 + T cells were transfected with 120 pmol siRNAs for 12 hrs, and were subsequently stimulated with anti-CD3 (1 µg/ml) and anti-CD28 (5 µg/ml) antibodies for 84 hrs. IL-2 mRNA levels were determined by qRT-PCR as described above. (C) Western blot analysis of IL-2 protein in human primary CD4 + T cells in (B). The <t>β-actin</t> was selected as an internal control. (D) Effects of optimized siRNAs on IL-2 mRNA level in mouse primary CD4 + T cells. Mouse primary CD4 + T cells were transfected with 120 pmol siRNAs for 12 hrs, and were subsequently stimulated with anti-mouse CD3 (2 µg/ml) and anti-mouse CD28 (1 µg/ml) antibodies for 84 hrs. Mouse IL-2 mRNA levels were determined by qRT-PCR and normalized to mouse GAPDH. P -values were calculated using the two tailed unpaired Student’s t-test with equal variances. *, p
    β Actin, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/β actin/product/Becton Dickinson
    Average 92 stars, based on 29 article reviews
    Price from $9.99 to $1999.99
    β actin - by Bioz Stars, 2020-09
    92/100 stars
      Buy from Supplier

    89
    Becton Dickinson mouse monoclonal anti β actin antibodies
    S4 mediates baseline RhoG activity and associates with synectin, RhoGDI1, and RhoG. (a) Murine pulmonary microvascular endothelial cells from WT and S4 knockout mice were cultured in 0.5% FBS/DME for 24 h before assay of RhoG activity. <t>β-Actin</t> and RhoGDI were used as loading controls. (right) Quantification from three experiments is shown. *, P = 0.009. Error bar indicates SEM. (b) A synthetic biotinylated peptide corresponding to the transmembrane domain and cytoplasmic tail of S4 was used to pull down proteins after conjugation to streptavidin beads. Pull-downs were immunoblotted and probed for synectin (top) and RhoGDI (bottom). − indicates unconjugated streptavidin beads. In both cases, the target proteins were pulled down only when incubated with the S4 tail peptide. (c) Coimmunoprecipitations were performed with antibodies against RhoGDI and synectin in three cell lines: WT RFPECs (left), RFPECs expressing the S4-FcR chimera (middle), and RFPECs expressing the S4-FcR (PDZ−) chimera (right). β-Actin was used as a loading control. IP, immunoprecipitation. (d) Glutathione beads conjugated with recombinant RhoGDI1 (right) or without the recombinant protein (left) were incubated with lysates of RFPECs for 12 h at 4°C. After washing, proteins were denatured by boiling and subjected to SDS-PAGE. The proteins were transferred to a membrane and probed for RhoG and synectin. (e) RFPECs were transfected with the S4-FcR chimera. Cells were incubated with FITC-conjugated human IgG to stain the chimera (left), washed twice with PBS, fixed, permeabilized, and stained with antibodies against RhoGDI1 and RhoG (middle and right, respectively). Arrows indicate regions of colocalization. Bars, 10 µm.
    Mouse Monoclonal Anti β Actin Antibodies, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 89/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse monoclonal anti β actin antibodies/product/Becton Dickinson
    Average 89 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse monoclonal anti β actin antibodies - by Bioz Stars, 2020-09
    89/100 stars
      Buy from Supplier

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    Optimized siRNAs showed higher and longer efficiency on IL-2 promoter activation in human or mouse primary CD4 + T cells. (A) HEK293T cells were transfected with siRNAs at the indicated concentrations and promoters activities were determined as described above. (B) Effects of optimized siRNAs on IL-2 mRNA level in human primary CD4 + T cells. Human primary CD4 + T cells were transfected with 120 pmol siRNAs for 12 hrs, and were subsequently stimulated with anti-CD3 (1 µg/ml) and anti-CD28 (5 µg/ml) antibodies for 84 hrs. IL-2 mRNA levels were determined by qRT-PCR as described above. (C) Western blot analysis of IL-2 protein in human primary CD4 + T cells in (B). The β-actin was selected as an internal control. (D) Effects of optimized siRNAs on IL-2 mRNA level in mouse primary CD4 + T cells. Mouse primary CD4 + T cells were transfected with 120 pmol siRNAs for 12 hrs, and were subsequently stimulated with anti-mouse CD3 (2 µg/ml) and anti-mouse CD28 (1 µg/ml) antibodies for 84 hrs. Mouse IL-2 mRNA levels were determined by qRT-PCR and normalized to mouse GAPDH. P -values were calculated using the two tailed unpaired Student’s t-test with equal variances. *, p

    Journal: PLoS ONE

    Article Title: Optimizations of SiRNA Design for the Activation of Gene Transcription by Targeting the TATA-Box Motif

    doi: 10.1371/journal.pone.0108253

    Figure Lengend Snippet: Optimized siRNAs showed higher and longer efficiency on IL-2 promoter activation in human or mouse primary CD4 + T cells. (A) HEK293T cells were transfected with siRNAs at the indicated concentrations and promoters activities were determined as described above. (B) Effects of optimized siRNAs on IL-2 mRNA level in human primary CD4 + T cells. Human primary CD4 + T cells were transfected with 120 pmol siRNAs for 12 hrs, and were subsequently stimulated with anti-CD3 (1 µg/ml) and anti-CD28 (5 µg/ml) antibodies for 84 hrs. IL-2 mRNA levels were determined by qRT-PCR as described above. (C) Western blot analysis of IL-2 protein in human primary CD4 + T cells in (B). The β-actin was selected as an internal control. (D) Effects of optimized siRNAs on IL-2 mRNA level in mouse primary CD4 + T cells. Mouse primary CD4 + T cells were transfected with 120 pmol siRNAs for 12 hrs, and were subsequently stimulated with anti-mouse CD3 (2 µg/ml) and anti-mouse CD28 (1 µg/ml) antibodies for 84 hrs. Mouse IL-2 mRNA levels were determined by qRT-PCR and normalized to mouse GAPDH. P -values were calculated using the two tailed unpaired Student’s t-test with equal variances. *, p

    Article Snippet: The lysates were then separated by 15% SDS-PAGE and analyzed by immunoblotting using primary antibodies specific for human IL-2 (rabbit monoclonal, Abcam) or β-actin (mouse monoclonal, BD).

    Techniques: Activation Assay, Transfection, Quantitative RT-PCR, Western Blot, Two Tailed Test

    Certain chemical modifications enhance the siRNAs efficacy on gene promoter activation. (A – B ) Effects of chemical modified siRNAs on IL-2 mRNA level in Jurkat cell line. 2–3×10 4 Jurkat cells were transfected with 120 pmol siRNAs for 12 hrs, and were subsequently treated with PMA (50 ng/ml) and ionomycin (1 µM) till ( A ) 2 days or ( B ) 4 days post transfection. IL-2 mRNA levels were then evaluated by qRT-PCR and normalized to β-actin. P -values were calculated using the two tailed unpaired Student’s t-test with equal variances. n = 3. *, p

    Journal: PLoS ONE

    Article Title: Optimizations of SiRNA Design for the Activation of Gene Transcription by Targeting the TATA-Box Motif

    doi: 10.1371/journal.pone.0108253

    Figure Lengend Snippet: Certain chemical modifications enhance the siRNAs efficacy on gene promoter activation. (A – B ) Effects of chemical modified siRNAs on IL-2 mRNA level in Jurkat cell line. 2–3×10 4 Jurkat cells were transfected with 120 pmol siRNAs for 12 hrs, and were subsequently treated with PMA (50 ng/ml) and ionomycin (1 µM) till ( A ) 2 days or ( B ) 4 days post transfection. IL-2 mRNA levels were then evaluated by qRT-PCR and normalized to β-actin. P -values were calculated using the two tailed unpaired Student’s t-test with equal variances. n = 3. *, p

    Article Snippet: The lysates were then separated by 15% SDS-PAGE and analyzed by immunoblotting using primary antibodies specific for human IL-2 (rabbit monoclonal, Abcam) or β-actin (mouse monoclonal, BD).

    Techniques: Activation Assay, Modification, Transfection, Quantitative RT-PCR, Two Tailed Test

    EPHX2 and AR signaling. A: Western blot analysis of AR and PSA protein levels after siRNA-induced EPHX2 gene silencing. β-Actin was used as a loading control. Relative value for each blot is indicated; relative expression in control sample was

    Journal: The American Journal of Pathology

    Article Title: Arachidonic Acid Pathway Members PLA2G7, HPGD, EPHX2, and CYP4F8 Identified as Putative Novel Therapeutic Targets in Prostate Cancer

    doi: 10.1016/j.ajpath.2010.10.002

    Figure Lengend Snippet: EPHX2 and AR signaling. A: Western blot analysis of AR and PSA protein levels after siRNA-induced EPHX2 gene silencing. β-Actin was used as a loading control. Relative value for each blot is indicated; relative expression in control sample was

    Article Snippet: Antibodies against AR (1:1000, NeoMarkers, Fremont, CA), PSA (1:1000, Dako), platelet activating factor (PAF) acetylhydrolase (encoded by PLA2G7 ) (1:500, Cayman Chemical), 15-PGDH (encoded by HPGD ) (1:500, Sigma-Aldrich), and β-actin (1:5000, mouse-monoclonal, Becton Dickinson, Franklin Lakes, NJ) were used.

    Techniques: Western Blot, Expressing

    Cell-permeable iron inhibits VEGFR-2 signaling through FAK and p38 MAPK affecting migration HUVEC-I cells were stimulated with VEGF-A (100 ng/ml) for 10 min to 60 min in the presence of 35 μM iron. ( A ) Cell lysates were then analyzed by Western blots to determine relative levels of phosphorylated FAK (pTyr-397 and pTyr-861). ( B ) Cumulative data showing relative levels of FAK phosphorylation and total FAK levels from two-four independent experiments. ( C ) Western blots showing phosphorylated p38-MAPK and total levels of PTP1B following VEGF-A stimulation of HUVEC-I cells in the presence of cell-permeable iron. ( D ) Densitometric analyses of Western blots from two independent experiments. Beta-Actin levels were used for normalization of phospho and total p38 MAPK levels. GAPDH levels were used to normalize PTP1B levels. * P

    Journal: Oncotarget

    Article Title: Cell-permeable iron inhibits vascular endothelial growth factor receptor-2 signaling and tumor angiogenesis

    doi: 10.18632/oncotarget.11689

    Figure Lengend Snippet: Cell-permeable iron inhibits VEGFR-2 signaling through FAK and p38 MAPK affecting migration HUVEC-I cells were stimulated with VEGF-A (100 ng/ml) for 10 min to 60 min in the presence of 35 μM iron. ( A ) Cell lysates were then analyzed by Western blots to determine relative levels of phosphorylated FAK (pTyr-397 and pTyr-861). ( B ) Cumulative data showing relative levels of FAK phosphorylation and total FAK levels from two-four independent experiments. ( C ) Western blots showing phosphorylated p38-MAPK and total levels of PTP1B following VEGF-A stimulation of HUVEC-I cells in the presence of cell-permeable iron. ( D ) Densitometric analyses of Western blots from two independent experiments. Beta-Actin levels were used for normalization of phospho and total p38 MAPK levels. GAPDH levels were used to normalize PTP1B levels. * P

    Article Snippet: Antibodies used were: anti p44/42 MAPK (CST#4696S), anti phospho-p44/42 MAPK (CST#4370S), anti VEGFR-2 (FLK-1) (sc-2651), anti phospho-Tyr 1175 VEGFR-2 (CST#2478S), anti phospho-Tyr 1214 VEGFR2 (ab5475), anti AKT (CST#2920S), anti phospho-Ser 473 AKT (CST#3787S), anti FAK (EMD Millipore 05-537), anti phospho-Tyr 397 FAK (CST#3283S), anti phospho-Tyr 861 FAK (ab4804), anti p38 MAPK (CST#9211S), anti phospho-p38 MAPK (CST#4511S), anti GAPDH (MAB374), anti Beta-Actin (sc-47778), anti PTP1B (sc-1718), anti HIF-2α (sc-13596), anti HIF-1α (NB 100-479), PE conjugated anti-CD31 (BD Pharminogen-52477), FITC-conjugated anti-αSMA (Sigma-F377), FITC-conjugated anti-cleaved PARP (Asp 214, BD Biosciences) and FITC-conjugated anti-cleaved caspase-3 (Asp 175, BD Biosciences).

    Techniques: Migration, Western Blot

    Cell-permeable iron inhibits VEGFR-2 receptor phosphorylation and downstream signaling HUVEC-I cells were stimulated with VEGF-A (100 ng/ml) for 10 min to 60 min in the presence of 35 μM iron. ( A ) Cell lysates were probed for phosphorylated tyrosine residues (pTyr-1175 and pTyr-1214) by Western blots using site-specific antibodies. Representative blot from two-three independent experiments is shown. ( B ) Densitometry analyses were used to determine relative levels of phosphorylated VEGFR-2 and total VEGFR-2. GAPDH levels were used for normalization for pTyr-1175 and total receptor levels. Beta-Actin levels were used for normalizing pTyr-1214 VEGFR-2 levels. Data represent mean ± SD from two-three independent experiments. ( C ) Representative Western blot showing phosphorylated p44/p42 MAPK and phosphorylated AKT. ( D ) Densitometric analysis of relative levels of phosphorylated and total p44/p42 MAPK and p-AKT. GAPDH levels were used for normalization. Data represent mean ± SD from two-three independent experiments. * P

    Journal: Oncotarget

    Article Title: Cell-permeable iron inhibits vascular endothelial growth factor receptor-2 signaling and tumor angiogenesis

    doi: 10.18632/oncotarget.11689

    Figure Lengend Snippet: Cell-permeable iron inhibits VEGFR-2 receptor phosphorylation and downstream signaling HUVEC-I cells were stimulated with VEGF-A (100 ng/ml) for 10 min to 60 min in the presence of 35 μM iron. ( A ) Cell lysates were probed for phosphorylated tyrosine residues (pTyr-1175 and pTyr-1214) by Western blots using site-specific antibodies. Representative blot from two-three independent experiments is shown. ( B ) Densitometry analyses were used to determine relative levels of phosphorylated VEGFR-2 and total VEGFR-2. GAPDH levels were used for normalization for pTyr-1175 and total receptor levels. Beta-Actin levels were used for normalizing pTyr-1214 VEGFR-2 levels. Data represent mean ± SD from two-three independent experiments. ( C ) Representative Western blot showing phosphorylated p44/p42 MAPK and phosphorylated AKT. ( D ) Densitometric analysis of relative levels of phosphorylated and total p44/p42 MAPK and p-AKT. GAPDH levels were used for normalization. Data represent mean ± SD from two-three independent experiments. * P

    Article Snippet: Antibodies used were: anti p44/42 MAPK (CST#4696S), anti phospho-p44/42 MAPK (CST#4370S), anti VEGFR-2 (FLK-1) (sc-2651), anti phospho-Tyr 1175 VEGFR-2 (CST#2478S), anti phospho-Tyr 1214 VEGFR2 (ab5475), anti AKT (CST#2920S), anti phospho-Ser 473 AKT (CST#3787S), anti FAK (EMD Millipore 05-537), anti phospho-Tyr 397 FAK (CST#3283S), anti phospho-Tyr 861 FAK (ab4804), anti p38 MAPK (CST#9211S), anti phospho-p38 MAPK (CST#4511S), anti GAPDH (MAB374), anti Beta-Actin (sc-47778), anti PTP1B (sc-1718), anti HIF-2α (sc-13596), anti HIF-1α (NB 100-479), PE conjugated anti-CD31 (BD Pharminogen-52477), FITC-conjugated anti-αSMA (Sigma-F377), FITC-conjugated anti-cleaved PARP (Asp 214, BD Biosciences) and FITC-conjugated anti-cleaved caspase-3 (Asp 175, BD Biosciences).

    Techniques: Western Blot

    S4 mediates baseline RhoG activity and associates with synectin, RhoGDI1, and RhoG. (a) Murine pulmonary microvascular endothelial cells from WT and S4 knockout mice were cultured in 0.5% FBS/DME for 24 h before assay of RhoG activity. β-Actin and RhoGDI were used as loading controls. (right) Quantification from three experiments is shown. *, P = 0.009. Error bar indicates SEM. (b) A synthetic biotinylated peptide corresponding to the transmembrane domain and cytoplasmic tail of S4 was used to pull down proteins after conjugation to streptavidin beads. Pull-downs were immunoblotted and probed for synectin (top) and RhoGDI (bottom). − indicates unconjugated streptavidin beads. In both cases, the target proteins were pulled down only when incubated with the S4 tail peptide. (c) Coimmunoprecipitations were performed with antibodies against RhoGDI and synectin in three cell lines: WT RFPECs (left), RFPECs expressing the S4-FcR chimera (middle), and RFPECs expressing the S4-FcR (PDZ−) chimera (right). β-Actin was used as a loading control. IP, immunoprecipitation. (d) Glutathione beads conjugated with recombinant RhoGDI1 (right) or without the recombinant protein (left) were incubated with lysates of RFPECs for 12 h at 4°C. After washing, proteins were denatured by boiling and subjected to SDS-PAGE. The proteins were transferred to a membrane and probed for RhoG and synectin. (e) RFPECs were transfected with the S4-FcR chimera. Cells were incubated with FITC-conjugated human IgG to stain the chimera (left), washed twice with PBS, fixed, permeabilized, and stained with antibodies against RhoGDI1 and RhoG (middle and right, respectively). Arrows indicate regions of colocalization. Bars, 10 µm.

    Journal: The Journal of Cell Biology

    Article Title: Suppression of RhoG activity is mediated by a syndecan 4-synectin-RhoGDI1 complex and is reversed by PKC? in a Rac1 activation pathway

    doi: 10.1083/jcb.200810179

    Figure Lengend Snippet: S4 mediates baseline RhoG activity and associates with synectin, RhoGDI1, and RhoG. (a) Murine pulmonary microvascular endothelial cells from WT and S4 knockout mice were cultured in 0.5% FBS/DME for 24 h before assay of RhoG activity. β-Actin and RhoGDI were used as loading controls. (right) Quantification from three experiments is shown. *, P = 0.009. Error bar indicates SEM. (b) A synthetic biotinylated peptide corresponding to the transmembrane domain and cytoplasmic tail of S4 was used to pull down proteins after conjugation to streptavidin beads. Pull-downs were immunoblotted and probed for synectin (top) and RhoGDI (bottom). − indicates unconjugated streptavidin beads. In both cases, the target proteins were pulled down only when incubated with the S4 tail peptide. (c) Coimmunoprecipitations were performed with antibodies against RhoGDI and synectin in three cell lines: WT RFPECs (left), RFPECs expressing the S4-FcR chimera (middle), and RFPECs expressing the S4-FcR (PDZ−) chimera (right). β-Actin was used as a loading control. IP, immunoprecipitation. (d) Glutathione beads conjugated with recombinant RhoGDI1 (right) or without the recombinant protein (left) were incubated with lysates of RFPECs for 12 h at 4°C. After washing, proteins were denatured by boiling and subjected to SDS-PAGE. The proteins were transferred to a membrane and probed for RhoG and synectin. (e) RFPECs were transfected with the S4-FcR chimera. Cells were incubated with FITC-conjugated human IgG to stain the chimera (left), washed twice with PBS, fixed, permeabilized, and stained with antibodies against RhoGDI1 and RhoG (middle and right, respectively). Arrows indicate regions of colocalization. Bars, 10 µm.

    Article Snippet: Mouse monoclonal anti–β actin antibodies were obtained from BD.

    Techniques: Activity Assay, Knock-Out, Mouse Assay, Cell Culture, Conjugation Assay, Incubation, Expressing, Immunoprecipitation, Recombinant, SDS Page, Transfection, Staining