β-actin Millipore Search Results


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  • 79
    Millipore anti β actin millipore antibody
    Anti β Actin Millipore Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore beta actin
    CUDC-907 inhibits NF-kB signaling in ABC DLBCLs ( A ) Relative NF-kB-luciferase activity in two representative ABC DLBCL cell lines (HBL-1 and TMD-8). Cells were treated for 12 hours with indicated concentration of either panobinostat, BKM-120, the combination of these two drugs, CUDC-907 or DMSO. Cells were incubated with 2 ng of TNF-α as positive control for NF-kB activation. Error bars represent standard error of the mean (S.E.M) of triplicate experiments. ( B ) Western blot demonstrating that CUDC-907 (0.1 μM for 6 and 12 hours) inhibits NF-kB activation by increasing IkB alpha levels and decreasing IKK <t>beta</t> levels in two representative ABC DLBCL cell lines (HBL-1 and TMD-8). The changes were associated with a decrease in IRF4 levels (see Supplementary Figure 2B ). ( C ) ELISA assay showing a more pronounced decrease of nuclear NF-kB p65 in two representative ABC (HBL-1 and TMD-8) cell lines compared with two GCB (SUDHL-6 and SUDHL-4) treated with either 0.1 μM CUDC-907 or DMSO for 12 hours. Differences between groups were calculated with the Student's t test. * p
    Beta Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4030 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck KGaA beta actin
    CUDC-907 inhibits NF-kB signaling in ABC DLBCLs ( A ) Relative NF-kB-luciferase activity in two representative ABC DLBCL cell lines (HBL-1 and TMD-8). Cells were treated for 12 hours with indicated concentration of either panobinostat, BKM-120, the combination of these two drugs, CUDC-907 or DMSO. Cells were incubated with 2 ng of TNF-α as positive control for NF-kB activation. Error bars represent standard error of the mean (S.E.M) of triplicate experiments. ( B ) Western blot demonstrating that CUDC-907 (0.1 μM for 6 and 12 hours) inhibits NF-kB activation by increasing IkB alpha levels and decreasing IKK <t>beta</t> levels in two representative ABC DLBCL cell lines (HBL-1 and TMD-8). The changes were associated with a decrease in IRF4 levels (see Supplementary Figure 2B ). ( C ) ELISA assay showing a more pronounced decrease of nuclear NF-kB p65 in two representative ABC (HBL-1 and TMD-8) cell lines compared with two GCB (SUDHL-6 and SUDHL-4) treated with either 0.1 μM CUDC-907 or DMSO for 12 hours. Differences between groups were calculated with the Student's t test. * p
    Beta Actin, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 95/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore β actin
    CUDC-907 inhibits NF-kB signaling in ABC DLBCLs ( A ) Relative NF-kB-luciferase activity in two representative ABC DLBCL cell lines (HBL-1 and TMD-8). Cells were treated for 12 hours with indicated concentration of either panobinostat, BKM-120, the combination of these two drugs, CUDC-907 or DMSO. Cells were incubated with 2 ng of TNF-α as positive control for NF-kB activation. Error bars represent standard error of the mean (S.E.M) of triplicate experiments. ( B ) Western blot demonstrating that CUDC-907 (0.1 μM for 6 and 12 hours) inhibits NF-kB activation by increasing IkB alpha levels and decreasing IKK <t>beta</t> levels in two representative ABC DLBCL cell lines (HBL-1 and TMD-8). The changes were associated with a decrease in IRF4 levels (see Supplementary Figure 2B ). ( C ) ELISA assay showing a more pronounced decrease of nuclear NF-kB p65 in two representative ABC (HBL-1 and TMD-8) cell lines compared with two GCB (SUDHL-6 and SUDHL-4) treated with either 0.1 μM CUDC-907 or DMSO for 12 hours. Differences between groups were calculated with the Student's t test. * p
    β Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 49026 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore beta actin specific
    Reovirus-induced poly-ADP ribose polymerase (PARP) cleavage in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected (M) or infected with rsT1L (T1) or rsT3D (T3) at an MOI of 100 PFU/cell. Each cell line was treated with TNFα (5 ng/mL) and CHX (25 μg/mL) (T/C) 6 h prior to the 24 h time point. Whole cell lysates prepared at 24, 48, or 72 h post-infection were analyzed by SDS-PAGE and immunoblotted using a PARP-specific monoclonal antibody (top) and <t>β-actin</t> (bottom). Full-length and cleaved PARP proteins are indicated to the right of the upper panel. The images are representative of two independent experiments.
    Beta Actin Specific, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Merck KGaA β actin
    Reovirus-induced poly-ADP ribose polymerase (PARP) cleavage in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected (M) or infected with rsT1L (T1) or rsT3D (T3) at an MOI of 100 PFU/cell. Each cell line was treated with TNFα (5 ng/mL) and CHX (25 μg/mL) (T/C) 6 h prior to the 24 h time point. Whole cell lysates prepared at 24, 48, or 72 h post-infection were analyzed by SDS-PAGE and immunoblotted using a PARP-specific monoclonal antibody (top) and <t>β-actin</t> (bottom). Full-length and cleaved PARP proteins are indicated to the right of the upper panel. The images are representative of two independent experiments.
    β Actin, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 97/100, based on 233 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti smooth muscle α isoactin antibody
    Reovirus-induced poly-ADP ribose polymerase (PARP) cleavage in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected (M) or infected with rsT1L (T1) or rsT3D (T3) at an MOI of 100 PFU/cell. Each cell line was treated with TNFα (5 ng/mL) and CHX (25 μg/mL) (T/C) 6 h prior to the 24 h time point. Whole cell lysates prepared at 24, 48, or 72 h post-infection were analyzed by SDS-PAGE and immunoblotted using a PARP-specific monoclonal antibody (top) and <t>β-actin</t> (bottom). Full-length and cleaved PARP proteins are indicated to the right of the upper panel. The images are representative of two independent experiments.
    Anti Smooth Muscle α Isoactin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 77/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore β actin control
    Reovirus-induced poly-ADP ribose polymerase (PARP) cleavage in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected (M) or infected with rsT1L (T1) or rsT3D (T3) at an MOI of 100 PFU/cell. Each cell line was treated with TNFα (5 ng/mL) and CHX (25 μg/mL) (T/C) 6 h prior to the 24 h time point. Whole cell lysates prepared at 24, 48, or 72 h post-infection were analyzed by SDS-PAGE and immunoblotted using a PARP-specific monoclonal antibody (top) and <t>β-actin</t> (bottom). Full-length and cleaved PARP proteins are indicated to the right of the upper panel. The images are representative of two independent experiments.
    β Actin Control, supplied by Millipore, used in various techniques. Bioz Stars score: 87/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore total β actin
    Reovirus-induced poly-ADP ribose polymerase (PARP) cleavage in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected (M) or infected with rsT1L (T1) or rsT3D (T3) at an MOI of 100 PFU/cell. Each cell line was treated with TNFα (5 ng/mL) and CHX (25 μg/mL) (T/C) 6 h prior to the 24 h time point. Whole cell lysates prepared at 24, 48, or 72 h post-infection were analyzed by SDS-PAGE and immunoblotted using a PARP-specific monoclonal antibody (top) and <t>β-actin</t> (bottom). Full-length and cleaved PARP proteins are indicated to the right of the upper panel. The images are representative of two independent experiments.
    Total β Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Millipore β actin primers
    Reovirus-induced poly-ADP ribose polymerase (PARP) cleavage in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected (M) or infected with rsT1L (T1) or rsT3D (T3) at an MOI of 100 PFU/cell. Each cell line was treated with TNFα (5 ng/mL) and CHX (25 μg/mL) (T/C) 6 h prior to the 24 h time point. Whole cell lysates prepared at 24, 48, or 72 h post-infection were analyzed by SDS-PAGE and immunoblotted using a PARP-specific monoclonal antibody (top) and <t>β-actin</t> (bottom). Full-length and cleaved PARP proteins are indicated to the right of the upper panel. The images are representative of two independent experiments.
    β Actin Primers, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Millipore structural protein beta actin
    Reovirus-induced poly-ADP ribose polymerase (PARP) cleavage in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected (M) or infected with rsT1L (T1) or rsT3D (T3) at an MOI of 100 PFU/cell. Each cell line was treated with TNFα (5 ng/mL) and CHX (25 μg/mL) (T/C) 6 h prior to the 24 h time point. Whole cell lysates prepared at 24, 48, or 72 h post-infection were analyzed by SDS-PAGE and immunoblotted using a PARP-specific monoclonal antibody (top) and <t>β-actin</t> (bottom). Full-length and cleaved PARP proteins are indicated to the right of the upper panel. The images are representative of two independent experiments.
    Structural Protein Beta Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 82/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore cytoplasmic β actin
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
    Cytoplasmic β Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore β actin antibodiy
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
    β Actin Antibodiy, supplied by Millipore, used in various techniques. Bioz Stars score: 70/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore protein β actin
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
    Protein β Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 134 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore bax6a7and β actin
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
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    Millipore β actin immunoblots
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
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    Millipore murine β actin
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
    Murine β Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore β actin ac15
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
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    Millipore mouse beta actin
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
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    Millipore rat beta actin
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
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    Millipore β actin a 2228
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
    β Actin A 2228, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore β actin detection
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
    β Actin Detection, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 144 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore beta actin ac74 antibodies
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
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    Cell Signaling Technology Inc β actin antibody
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
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    Millipore human β actin
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
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    Millipore control protein β actin
    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to <t>β-actin</t> mRNA. Lean animal
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    Millipore beta actin primary antibody
    2D and 3D growth pattern of large-cell NEC cell lines. NEC-DUE1 and –DUE2 were cultivated in 2D (upper panel) or 3D culture systems (middle panel). The colon cancer cell line HCT116 served as control. Spheroids were grown in lrECM 3D microenvironments for seven days. Confocal laser scanning fluorescence microscopy images of isolated 3D spheroids (lower panel) stained with <t>beta-actin</t> (green) and DAPI (blue) revealed a grape-like growth pattern for both NEC cell lines.
    Beta Actin Primary Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    CUDC-907 inhibits NF-kB signaling in ABC DLBCLs ( A ) Relative NF-kB-luciferase activity in two representative ABC DLBCL cell lines (HBL-1 and TMD-8). Cells were treated for 12 hours with indicated concentration of either panobinostat, BKM-120, the combination of these two drugs, CUDC-907 or DMSO. Cells were incubated with 2 ng of TNF-α as positive control for NF-kB activation. Error bars represent standard error of the mean (S.E.M) of triplicate experiments. ( B ) Western blot demonstrating that CUDC-907 (0.1 μM for 6 and 12 hours) inhibits NF-kB activation by increasing IkB alpha levels and decreasing IKK beta levels in two representative ABC DLBCL cell lines (HBL-1 and TMD-8). The changes were associated with a decrease in IRF4 levels (see Supplementary Figure 2B ). ( C ) ELISA assay showing a more pronounced decrease of nuclear NF-kB p65 in two representative ABC (HBL-1 and TMD-8) cell lines compared with two GCB (SUDHL-6 and SUDHL-4) treated with either 0.1 μM CUDC-907 or DMSO for 12 hours. Differences between groups were calculated with the Student's t test. * p

    Journal: Oncotarget

    Article Title: Dual inhibition of histone deacetylases and phosphoinositide 3-kinase enhances therapeutic activity against B cell lymphoma

    doi: 10.18632/oncotarget.14876

    Figure Lengend Snippet: CUDC-907 inhibits NF-kB signaling in ABC DLBCLs ( A ) Relative NF-kB-luciferase activity in two representative ABC DLBCL cell lines (HBL-1 and TMD-8). Cells were treated for 12 hours with indicated concentration of either panobinostat, BKM-120, the combination of these two drugs, CUDC-907 or DMSO. Cells were incubated with 2 ng of TNF-α as positive control for NF-kB activation. Error bars represent standard error of the mean (S.E.M) of triplicate experiments. ( B ) Western blot demonstrating that CUDC-907 (0.1 μM for 6 and 12 hours) inhibits NF-kB activation by increasing IkB alpha levels and decreasing IKK beta levels in two representative ABC DLBCL cell lines (HBL-1 and TMD-8). The changes were associated with a decrease in IRF4 levels (see Supplementary Figure 2B ). ( C ) ELISA assay showing a more pronounced decrease of nuclear NF-kB p65 in two representative ABC (HBL-1 and TMD-8) cell lines compared with two GCB (SUDHL-6 and SUDHL-4) treated with either 0.1 μM CUDC-907 or DMSO for 12 hours. Differences between groups were calculated with the Student's t test. * p

    Article Snippet: Beta-Actin was from SIGMA (A5316#).

    Techniques: Luciferase, Activity Assay, Concentration Assay, Incubation, Positive Control, Activation Assay, Western Blot, Enzyme-linked Immunosorbent Assay

    CBL expression in human pancreatic ductal adenocarcinoma (PDAC) is inversely correlated with EGFR expression and activation. A, immunohistochemistry staining of human PDAC tumors stained for CBL, pEGFR, and EGFR reveals an inverse expression in 12 of 15 tumors (2 representative individual patient samples are shown), suggesting a possible regulatory effect of CBL on EGFR. B, correspondingly, when stimulated by EGF ligand, immunoblots of Panc-1 cells with CBL knockdown show increased phosphorylation of EGFR (Y1068) when compared to the isogenic parental cell line, with increased downstream pERK and pAKT (columns 2 versus 4). Relative densitometry values normalized to β-actin as a loading control are displayed above each phosphoprotein band and, C, plotted as a bar graph.

    Journal: Clinical cancer research : an official journal of the American Association for Cancer Research

    Article Title: Low expression of the E3 Ubiquitin Ligase CBL Confers Chemoresistance in Human Pancreatic Cancer and is Targeted by Epidermal Growth Factor Receptor Inhibition

    doi: 10.1158/1078-0432.CCR-14-0610

    Figure Lengend Snippet: CBL expression in human pancreatic ductal adenocarcinoma (PDAC) is inversely correlated with EGFR expression and activation. A, immunohistochemistry staining of human PDAC tumors stained for CBL, pEGFR, and EGFR reveals an inverse expression in 12 of 15 tumors (2 representative individual patient samples are shown), suggesting a possible regulatory effect of CBL on EGFR. B, correspondingly, when stimulated by EGF ligand, immunoblots of Panc-1 cells with CBL knockdown show increased phosphorylation of EGFR (Y1068) when compared to the isogenic parental cell line, with increased downstream pERK and pAKT (columns 2 versus 4). Relative densitometry values normalized to β-actin as a loading control are displayed above each phosphoprotein band and, C, plotted as a bar graph.

    Article Snippet: Membranes were first blocked with 5% bovine serum albumin (BSA) in Tris-buffered saline + 0.1% Tween20 (TBST), washed ×3 in TBST, then incubated overnight at 4°C in 5% BSA in TBS containing primary antibody at 1:1000 dilution unless otherwise noted: CBL, pAKT 1:500, AKT, pEGFR (Y1068), pEGFR (Y1045), EGFR 1:2000, pERK, ERK (Cell Signaling). β-actin 1:5000 (Sigma) was used to normalize sample loading.

    Techniques: Expressing, Activation Assay, Immunohistochemistry, Staining, Western Blot

    Increase in total tyrosine and threonine phosphorylation. Whole cell lysates were collected from SAEC at both (A) 6 h and (B) 24 h treated with 0.0, 5.0, 25.0, or 50.0 µg/ml administered dose of CoO or La 2 O 3 nanoparticles. Western blotting was used to detect changes in total tyrosine phosphorylation and total threonine phosphorylation. Beta Actin was used for internal control within the samples. Western blots are representative of n = 3.

    Journal: Toxicological Sciences

    Article Title: Toxicological Assessment of CoO and La2O3 Metal Oxide Nanoparticles in Human Small Airway Epithelial Cells

    doi: 10.1093/toxsci/kfw005

    Figure Lengend Snippet: Increase in total tyrosine and threonine phosphorylation. Whole cell lysates were collected from SAEC at both (A) 6 h and (B) 24 h treated with 0.0, 5.0, 25.0, or 50.0 µg/ml administered dose of CoO or La 2 O 3 nanoparticles. Western blotting was used to detect changes in total tyrosine phosphorylation and total threonine phosphorylation. Beta Actin was used for internal control within the samples. Western blots are representative of n = 3.

    Article Snippet: The membranes were probed with total phospho-tyrosine antibody, total phospho-threonine antibody, HIF-1α antibody (Cell Signaling Technology, Boston, Massachusetts), or beta actin antibody (Sigma Aldrich, St. Louis, Missouri) as an internal control.

    Techniques: Western Blot

    Induction of HIF-1α due to CoO nanoparticles. Whole cell lysates were collected from SAEC at 6 h with 0.0, 5.0, 25.0, or 50.0 µg/ml administered dose of CoO or La 2 O 3 nanoparticles. Western blotting was used to detect changes in HIF-1α protein expression. Beta Actin was used for internal control within the samples. Western blots are representative of n = 3.

    Journal: Toxicological Sciences

    Article Title: Toxicological Assessment of CoO and La2O3 Metal Oxide Nanoparticles in Human Small Airway Epithelial Cells

    doi: 10.1093/toxsci/kfw005

    Figure Lengend Snippet: Induction of HIF-1α due to CoO nanoparticles. Whole cell lysates were collected from SAEC at 6 h with 0.0, 5.0, 25.0, or 50.0 µg/ml administered dose of CoO or La 2 O 3 nanoparticles. Western blotting was used to detect changes in HIF-1α protein expression. Beta Actin was used for internal control within the samples. Western blots are representative of n = 3.

    Article Snippet: The membranes were probed with total phospho-tyrosine antibody, total phospho-threonine antibody, HIF-1α antibody (Cell Signaling Technology, Boston, Massachusetts), or beta actin antibody (Sigma Aldrich, St. Louis, Missouri) as an internal control.

    Techniques: Western Blot, Expressing

    Rolipram reduces SCI-induced increases in PDE4B1 and PDE4A5 protein production as well as PDE4A5 phosphorylation. A–C. Immunoblot analysis of injured spinal cord homogenates revealed an SCI-induced increase in PDE4B1 at 25 h that was significantly abrogated by Rolipram treatment, when given at either 1 or 24 h after SCI ( A, B ). PDE4D1/2 was not regulated by either SCI or Rolipram treatment at the protein level ( A, C ). D–H. Unlike PDE4A1 ( D–E ), PDE4A5 protein production ( F, G ) and phosphorylation ( F, H ) was increased from 4 to 25 h after SCI. Rolipram, when given at either 1 or 24 h after SCI (black and diagonal line bars, respectively), significantly abated these SCI-induced increases. Vehicle delivery (at 1 h, dotted white bars) did not affect the protein production or phosphorylation of the PDE4s examined post-SCI. Density readings of PDE4 bands were normalized to β-actin immunoreactivity performed on the same blots. Statistical significance indicated at *p

    Journal: PLoS ONE

    Article Title: The Therapeutic Profile of Rolipram, PDE Target and Mechanism of Action as a Neuroprotectant following Spinal Cord Injury

    doi: 10.1371/journal.pone.0043634

    Figure Lengend Snippet: Rolipram reduces SCI-induced increases in PDE4B1 and PDE4A5 protein production as well as PDE4A5 phosphorylation. A–C. Immunoblot analysis of injured spinal cord homogenates revealed an SCI-induced increase in PDE4B1 at 25 h that was significantly abrogated by Rolipram treatment, when given at either 1 or 24 h after SCI ( A, B ). PDE4D1/2 was not regulated by either SCI or Rolipram treatment at the protein level ( A, C ). D–H. Unlike PDE4A1 ( D–E ), PDE4A5 protein production ( F, G ) and phosphorylation ( F, H ) was increased from 4 to 25 h after SCI. Rolipram, when given at either 1 or 24 h after SCI (black and diagonal line bars, respectively), significantly abated these SCI-induced increases. Vehicle delivery (at 1 h, dotted white bars) did not affect the protein production or phosphorylation of the PDE4s examined post-SCI. Density readings of PDE4 bands were normalized to β-actin immunoreactivity performed on the same blots. Statistical significance indicated at *p

    Article Snippet: Density readings were normalized to β-actin immunoreactivity (1∶10,000, Sigma-Aldrich) performed on the same blot.

    Techniques:

    miR-26b Promotes Microvascular Growth In Vivo (A and B) The expression of (A) miR-26b and (B) PTEN in Matrigel plug mixed with miR-26b mimic and control mimic after 12 days. (C) Western blot analysis of PTEN expression in Matrigel plugs. β-actin was detected as a loading control. Lower panel: quantification of western blotting is shown. Error bars are mean ± SEM; *p

    Journal: Molecular Therapy. Nucleic Acids

    Article Title: Phenotypic miRNA Screen Identifies miR-26b to Promote the Growth and Survival of Endothelial Cells

    doi: 10.1016/j.omtn.2018.08.006

    Figure Lengend Snippet: miR-26b Promotes Microvascular Growth In Vivo (A and B) The expression of (A) miR-26b and (B) PTEN in Matrigel plug mixed with miR-26b mimic and control mimic after 12 days. (C) Western blot analysis of PTEN expression in Matrigel plugs. β-actin was detected as a loading control. Lower panel: quantification of western blotting is shown. Error bars are mean ± SEM; *p

    Article Snippet: Membranes were blocked with 5% skim milk, followed by incubation with primary antibodies β-actin (Sigma; 1:1,000), PMAIP1 (Cell Signaling Technology; 1:1,000), PTEN, (Cell Signaling Technology; 1:1,000), PPP2R2A (Cell Signaling Technology; 1:1,000), total AKT1 (Cell Signaling Technology; 1:1,000), and S473 p-AKT (Cell Signaling Technology; 1:1,000) at 4 °C overnight.

    Techniques: In Vivo, Expressing, Western Blot

    Functional evaluation of NPAS3 expression in human astrocytes. A: Western blot analysis of NPAS3 expression in a panel of engineered astrocyte cell lines, with β-actin as a positive control, and with the NPAS3 shRNA plasmids targeting exons 5

    Journal: The American Journal of Pathology

    Article Title: NPAS3 Demonstrates Features of a Tumor Suppressive Role in Driving the Progression of Astrocytomas

    doi: 10.1016/j.ajpath.2011.03.044

    Figure Lengend Snippet: Functional evaluation of NPAS3 expression in human astrocytes. A: Western blot analysis of NPAS3 expression in a panel of engineered astrocyte cell lines, with β-actin as a positive control, and with the NPAS3 shRNA plasmids targeting exons 5

    Article Snippet: The blots were stripped with Western blot stripping buffer (Pierce Chemical Co., Rockford, IL) and re-probed using β-actin monoclonal clone AC-15 (Sigma-Aldrich Corp.) to detect loading differences.

    Techniques: Functional Assay, Expressing, Western Blot, Positive Control, shRNA

    Functional evaluation of NPAS3 protein expression in human malignant glioma cell lines. A: Left panel , Western blot analysis using a panel of glioma cell lines and a β-actin–positive control. Right panel . Protein expression levels of NPAS3

    Journal: The American Journal of Pathology

    Article Title: NPAS3 Demonstrates Features of a Tumor Suppressive Role in Driving the Progression of Astrocytomas

    doi: 10.1016/j.ajpath.2011.03.044

    Figure Lengend Snippet: Functional evaluation of NPAS3 protein expression in human malignant glioma cell lines. A: Left panel , Western blot analysis using a panel of glioma cell lines and a β-actin–positive control. Right panel . Protein expression levels of NPAS3

    Article Snippet: The blots were stripped with Western blot stripping buffer (Pierce Chemical Co., Rockford, IL) and re-probed using β-actin monoclonal clone AC-15 (Sigma-Aldrich Corp.) to detect loading differences.

    Techniques: Functional Assay, Expressing, Western Blot, Positive Control

    Autophagy flux is induced by cela in A549 cells. A549 cells were treated with cela (4 µM) for 12 h and then exposed to TRAIL for an additional 1 h. (A) LC3-II and p62 protein levels were assessed by western blot analysis. Bar charts indicate the (B) LC3-II/LC3-I and (C) p62/β-actin ratios. (D) Cells were immunostained with p62 (red) and evaluated using fluorescence microscopy. Scale bar=50 µm. (E) Ac-cas3 and Ac-cas8 protein levels were assessed by western blot analysis. Bar charts indicate the (F) Ac-cas8/β-actin and (G) Ac-cas3/β-actin ratios. (H) Cells were immunostained with Ac-cas3 (green) antibody and evaluated using fluorescence microscopy. Scale bar=50 µm. β-actin was used as a control. **P

    Journal: Molecular Medicine Reports

    Article Title: Autophagy flux inhibition mediated by celastrol sensitized lung cancer cells to TRAIL-induced apoptosis via regulation of mitochondrial transmembrane potential and reactive oxygen species

    doi: 10.3892/mmr.2018.9757

    Figure Lengend Snippet: Autophagy flux is induced by cela in A549 cells. A549 cells were treated with cela (4 µM) for 12 h and then exposed to TRAIL for an additional 1 h. (A) LC3-II and p62 protein levels were assessed by western blot analysis. Bar charts indicate the (B) LC3-II/LC3-I and (C) p62/β-actin ratios. (D) Cells were immunostained with p62 (red) and evaluated using fluorescence microscopy. Scale bar=50 µm. (E) Ac-cas3 and Ac-cas8 protein levels were assessed by western blot analysis. Bar charts indicate the (F) Ac-cas8/β-actin and (G) Ac-cas3/β-actin ratios. (H) Cells were immunostained with Ac-cas3 (green) antibody and evaluated using fluorescence microscopy. Scale bar=50 µm. β-actin was used as a control. **P

    Article Snippet: Antibodies against β-actin were purchased from Sigma-Aldrich; Merck KGaA, and those against cleaved caspase-8 were obtained from BD Pharmingen (BD Biosciences, Franklin Lakes, NJ, USA).

    Techniques: Western Blot, Fluorescence, Microscopy

    Cela induces a promotion of the TRAIL-initiated apoptotic mechanism by attenuating autophagy flux. A549 cells were pretreated with CQ prior to exposure to cela (4 µM) for 12 h and then exposure to TRAIL for an additional 1 h. (A) LC3-II and p62 protein levels were assessed by western blot analysis. Bar charts indicate the (B) LC3-II/LC3-I and (C) p62/β-actin ratios. (D) Cells were immunostained with p62 (red) and evaluated using fluorescence microscopy. Scale bar=50 µm. (E) Ac-cas3 and Ac-cas8 protein levels were assessed by western blot analysis. Bar charts indicate the (F) Ac-cas8/β-actin and (G) Ac-cas3/β-actin ratios. (H) Cells were immunostained with Ac-cas3 (green) antibody and evaluated using fluorescence microscopy. Scale bar=50 µm. β-actin was used as a control. **P

    Journal: Molecular Medicine Reports

    Article Title: Autophagy flux inhibition mediated by celastrol sensitized lung cancer cells to TRAIL-induced apoptosis via regulation of mitochondrial transmembrane potential and reactive oxygen species

    doi: 10.3892/mmr.2018.9757

    Figure Lengend Snippet: Cela induces a promotion of the TRAIL-initiated apoptotic mechanism by attenuating autophagy flux. A549 cells were pretreated with CQ prior to exposure to cela (4 µM) for 12 h and then exposure to TRAIL for an additional 1 h. (A) LC3-II and p62 protein levels were assessed by western blot analysis. Bar charts indicate the (B) LC3-II/LC3-I and (C) p62/β-actin ratios. (D) Cells were immunostained with p62 (red) and evaluated using fluorescence microscopy. Scale bar=50 µm. (E) Ac-cas3 and Ac-cas8 protein levels were assessed by western blot analysis. Bar charts indicate the (F) Ac-cas8/β-actin and (G) Ac-cas3/β-actin ratios. (H) Cells were immunostained with Ac-cas3 (green) antibody and evaluated using fluorescence microscopy. Scale bar=50 µm. β-actin was used as a control. **P

    Article Snippet: Antibodies against β-actin were purchased from Sigma-Aldrich; Merck KGaA, and those against cleaved caspase-8 were obtained from BD Pharmingen (BD Biosciences, Franklin Lakes, NJ, USA).

    Techniques: Western Blot, Fluorescence, Microscopy

    Reovirus-induced poly-ADP ribose polymerase (PARP) cleavage in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected (M) or infected with rsT1L (T1) or rsT3D (T3) at an MOI of 100 PFU/cell. Each cell line was treated with TNFα (5 ng/mL) and CHX (25 μg/mL) (T/C) 6 h prior to the 24 h time point. Whole cell lysates prepared at 24, 48, or 72 h post-infection were analyzed by SDS-PAGE and immunoblotted using a PARP-specific monoclonal antibody (top) and β-actin (bottom). Full-length and cleaved PARP proteins are indicated to the right of the upper panel. The images are representative of two independent experiments.

    Journal: Viruses

    Article Title: Serotype-Specific Killing of Large Cell Carcinoma Cells by Reovirus

    doi: 10.3390/v9060140

    Figure Lengend Snippet: Reovirus-induced poly-ADP ribose polymerase (PARP) cleavage in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected (M) or infected with rsT1L (T1) or rsT3D (T3) at an MOI of 100 PFU/cell. Each cell line was treated with TNFα (5 ng/mL) and CHX (25 μg/mL) (T/C) 6 h prior to the 24 h time point. Whole cell lysates prepared at 24, 48, or 72 h post-infection were analyzed by SDS-PAGE and immunoblotted using a PARP-specific monoclonal antibody (top) and β-actin (bottom). Full-length and cleaved PARP proteins are indicated to the right of the upper panel. The images are representative of two independent experiments.

    Article Snippet: Proteins were separated by SDS-PAGE and immunoblotted [ ] using reovirus—(1:10,000 dilution), PARP—(Cell Signaling; 1:1000 dilution), or β-actin-specific (Sigma-Aldrich; 1:10,000 dilution) antibodies.

    Techniques: Infection, SDS Page

    Reovirus protein synthesis in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected or infected with rsT1L or rsT3D at an MOI of 10 PFU/cell. Whole cell lysates prepared at 6, 12, 18, or 24 h post-infection were analyzed by SDS-PAGE and immunoblotted using reovirus-specific antiserum (top) or β-actin (bottom). Reovirus proteins are indicated to the right of the top panel. The images are representative of the results from two independent experiments.

    Journal: Viruses

    Article Title: Serotype-Specific Killing of Large Cell Carcinoma Cells by Reovirus

    doi: 10.3390/v9060140

    Figure Lengend Snippet: Reovirus protein synthesis in NSCLC cell lines. ( A ) H661; ( B ) H1299; ( C ) H1437; ( D ) H1563; and ( E ) H1975 cells were mock infected or infected with rsT1L or rsT3D at an MOI of 10 PFU/cell. Whole cell lysates prepared at 6, 12, 18, or 24 h post-infection were analyzed by SDS-PAGE and immunoblotted using reovirus-specific antiserum (top) or β-actin (bottom). Reovirus proteins are indicated to the right of the top panel. The images are representative of the results from two independent experiments.

    Article Snippet: Proteins were separated by SDS-PAGE and immunoblotted [ ] using reovirus—(1:10,000 dilution), PARP—(Cell Signaling; 1:1000 dilution), or β-actin-specific (Sigma-Aldrich; 1:10,000 dilution) antibodies.

    Techniques: Infection, SDS Page

    Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to β-actin mRNA. Lean animal

    Journal: Biochimica et biophysica acta

    Article Title: Metabolic Regulation of APOBEC-1 Complementation Factor Trafficking in Mouse Models of Obesity and its Positive Correlation with the Expression of ApoB Protein in Hepatocytes

    doi: 10.1016/j.bbadis.2010.06.003

    Figure Lengend Snippet: Increased ACF mRNA and protein expression in Ob/Ob liver. A . The abundance of Ob/Ob hepatic apoB, apobec-1 and acf mRNA relative to that quantified from lean control liver was assessed by real time PCR and normalized to β-actin mRNA. Lean animal

    Article Snippet: Whole liver extracts were prepared by Teflon to glass homogenization of liver in 0.25 STM (0.25 M sucrose, 50 mM Tris pH 7.0 and 5 mM MgCl2 ) supplemented with Complete Protease Inhibitors (Roche, Indianapolis, IN) and phosphatase inhibitors, PhosStop (Roche) then cleared at 3,000 X g for 10 min. Nuclear and cytoplasmic preparations were centrifuged as previously described [ ] and the quality of the separation was assessed by western blotting extracts for cytoplasmic β-actin (Sigma) and nuclear histone H1 (Santa Cruz Biotechnology, Santa Cruz, CA).

    Techniques: Expressing, Real-time Polymerase Chain Reaction

    Enhanced ACF abundance supports increases in intracellular ApoB protein. A. Real time PCR was performed on poly A+ purified RNA from cytoplasmic and nuclear subcellular extracts of Ob/Ob and cogenic control animal liver. β-actin mRNA was quantified

    Journal: Biochimica et biophysica acta

    Article Title: Metabolic Regulation of APOBEC-1 Complementation Factor Trafficking in Mouse Models of Obesity and its Positive Correlation with the Expression of ApoB Protein in Hepatocytes

    doi: 10.1016/j.bbadis.2010.06.003

    Figure Lengend Snippet: Enhanced ACF abundance supports increases in intracellular ApoB protein. A. Real time PCR was performed on poly A+ purified RNA from cytoplasmic and nuclear subcellular extracts of Ob/Ob and cogenic control animal liver. β-actin mRNA was quantified

    Article Snippet: Whole liver extracts were prepared by Teflon to glass homogenization of liver in 0.25 STM (0.25 M sucrose, 50 mM Tris pH 7.0 and 5 mM MgCl2 ) supplemented with Complete Protease Inhibitors (Roche, Indianapolis, IN) and phosphatase inhibitors, PhosStop (Roche) then cleared at 3,000 X g for 10 min. Nuclear and cytoplasmic preparations were centrifuged as previously described [ ] and the quality of the separation was assessed by western blotting extracts for cytoplasmic β-actin (Sigma) and nuclear histone H1 (Santa Cruz Biotechnology, Santa Cruz, CA).

    Techniques: Real-time Polymerase Chain Reaction, Purification

    Acute leptin treatment suppresses acf mRNA abundance. The relative abundance of acf mRNA in primary mouse hepatocytes, normalized to β-actin mRNA abundance was determined by real time PCR following 4 hours of treatment with increasing concentrations

    Journal: Biochimica et biophysica acta

    Article Title: Metabolic Regulation of APOBEC-1 Complementation Factor Trafficking in Mouse Models of Obesity and its Positive Correlation with the Expression of ApoB Protein in Hepatocytes

    doi: 10.1016/j.bbadis.2010.06.003

    Figure Lengend Snippet: Acute leptin treatment suppresses acf mRNA abundance. The relative abundance of acf mRNA in primary mouse hepatocytes, normalized to β-actin mRNA abundance was determined by real time PCR following 4 hours of treatment with increasing concentrations

    Article Snippet: Whole liver extracts were prepared by Teflon to glass homogenization of liver in 0.25 STM (0.25 M sucrose, 50 mM Tris pH 7.0 and 5 mM MgCl2 ) supplemented with Complete Protease Inhibitors (Roche, Indianapolis, IN) and phosphatase inhibitors, PhosStop (Roche) then cleared at 3,000 X g for 10 min. Nuclear and cytoplasmic preparations were centrifuged as previously described [ ] and the quality of the separation was assessed by western blotting extracts for cytoplasmic β-actin (Sigma) and nuclear histone H1 (Santa Cruz Biotechnology, Santa Cruz, CA).

    Techniques: Real-time Polymerase Chain Reaction

    2D and 3D growth pattern of large-cell NEC cell lines. NEC-DUE1 and –DUE2 were cultivated in 2D (upper panel) or 3D culture systems (middle panel). The colon cancer cell line HCT116 served as control. Spheroids were grown in lrECM 3D microenvironments for seven days. Confocal laser scanning fluorescence microscopy images of isolated 3D spheroids (lower panel) stained with beta-actin (green) and DAPI (blue) revealed a grape-like growth pattern for both NEC cell lines.

    Journal: PLoS ONE

    Article Title: New Model for Gastroenteropancreatic Large-Cell Neuroendocrine Carcinoma: Establishment of Two Clinically Relevant Cell Lines

    doi: 10.1371/journal.pone.0088713

    Figure Lengend Snippet: 2D and 3D growth pattern of large-cell NEC cell lines. NEC-DUE1 and –DUE2 were cultivated in 2D (upper panel) or 3D culture systems (middle panel). The colon cancer cell line HCT116 served as control. Spheroids were grown in lrECM 3D microenvironments for seven days. Confocal laser scanning fluorescence microscopy images of isolated 3D spheroids (lower panel) stained with beta-actin (green) and DAPI (blue) revealed a grape-like growth pattern for both NEC cell lines.

    Article Snippet: Unspecific binding sites were blocked for 20 minutes with 5% milk/TBS-T. Primary antibody beta-Actin (Sigma-Aldrich, Hamburg, Germany) was diluted 1∶5000 in 5% milk/TBS-T and incubated overnight at 4°C.

    Techniques: Fluorescence, Microscopy, Isolation, Staining