β actin c4 Search Results


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  • 91
    Santa Cruz Biotechnology β actin c4
    β Actin C4, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 335 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam β actin
    miR-23a/b directly targets Tmem64 . ( a ) Schematic representation of the predicted miR-23a/b target site in the 3′-UTR of mouse Tmem64 . The alignment of miR-23a/b with WT and MUT 3′-UTR region is shown by complementary pairing, and three mutated nucleotides are underlined. ( b ) BMSCs were co-transfected with the luciferase reporter carrying WT-pGL3- Tmem64 or MUT-pGL3- Tmem64 along with agomiR-23a/b or agomiR-NC. The effects of miR-23a/b on the luciferase reporter constructs were determined 48 h after transfection. The firefly luciferase values were normalized to Renilla luciferase; n =5. ( c ) After BMSCs were transfected with agomiR-23a/b or antagomiR-23a/b, the relative levels of Tmem64 protein expression were determined by western blot; <t>β-actin</t> was used as loading control; n =5. ( d ) The relative levels of Tmem64 mRNA were determined using qRT-PCR and normalized to β-actin; n =5. ( e ) Tmem64 protein levels in BMSCs from 3- and 18-month-old mice were measured by western blot and expressed as the densitometry of Tmem64/β-actin. Tmem64 mRNA levels were determined by qRT-PCR and are shown as the fold-induction relative to β-actin; n =3. ( f ) The increase in ALP activity induced by agomiR-23a/b was blocked by the transfection of MUT Tmem64 3′-UTR into osteogenic-induced-BMSCs. * P
    β Actin, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 25813 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology anti β actin c4
    (A) Amounts of DNMT3A and DNMT1 in U937 cells and HL-60 cells after treatment with the indicated agent for 48 h. Values indicate the relative amounts of DNMT3A and DNMT1 normalized with <t>β-ACTIN.</t> (B) Amounts of DNMT3A and DNMT1 in R-U937 and R-HL-60 cells after treatment with the indicated agent for 48 h. Values indicate the relative amounts of DNMT3A and DNMT1 normalized with β-ACTIN.
    Anti β Actin C4, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 187 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology mouse anti β actin c4 antibody
    (A) Amounts of DNMT3A and DNMT1 in U937 cells and HL-60 cells after treatment with the indicated agent for 48 h. Values indicate the relative amounts of DNMT3A and DNMT1 normalized with <t>β-ACTIN.</t> (B) Amounts of DNMT3A and DNMT1 in R-U937 and R-HL-60 cells after treatment with the indicated agent for 48 h. Values indicate the relative amounts of DNMT3A and DNMT1 normalized with β-ACTIN.
    Mouse Anti β Actin C4 Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology β actin c4 mouse monoclonal igg1
    p300 is a transcriptional coactivator for GR-regulated DUSP1 gene transcription. A Glucocorticoid treatment increased the level of p300 and CBP at the DUSP1 GLS2 region. A549 cells were treated with DMSO or DEX (0.5 µM) for 10 min, and ChIP was performed with antibodies against p300, CBP and <t>IgG</t> (control). Data is shown from qPCR analyses with primers specific to the DUSP1 GLS2. B RNAi knockdown causes substantial reduction of p300 protein and CBP protein. A549 cells reverse transfected with p300, CBP or scramble siRNA were harvested 48 h post-transfection, then probed by Western blot using an antibody against p300 or CBP, with <t>β-actin</t> as a loading control. C RNAi against p300 but not CBP decreased DEX-induced DUSP1 gene expression. p300, CBP or scramble (control) siRNA was transfected into A549 cells. 48 h post-transfection, cells were treated with DMSO or DEX (0.5 µM) for 5 h. Total RNA was isolated and converted to cDNA. qPCR was used to monitor the expression of DUSP1 gene. The expression of Rpl19 gene was used as an internal control. Data represents the SEM of DEX-induced DUSP1 gene expression (DEX-treated cells divided by DMSO-treated cells), as a percent of the control siRNA response from at least three experiments.
    β Actin C4 Mouse Monoclonal Igg1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology anti β actin c4 sc 47778
    p300 is a transcriptional coactivator for GR-regulated DUSP1 gene transcription. A Glucocorticoid treatment increased the level of p300 and CBP at the DUSP1 GLS2 region. A549 cells were treated with DMSO or DEX (0.5 µM) for 10 min, and ChIP was performed with antibodies against p300, CBP and <t>IgG</t> (control). Data is shown from qPCR analyses with primers specific to the DUSP1 GLS2. B RNAi knockdown causes substantial reduction of p300 protein and CBP protein. A549 cells reverse transfected with p300, CBP or scramble siRNA were harvested 48 h post-transfection, then probed by Western blot using an antibody against p300 or CBP, with <t>β-actin</t> as a loading control. C RNAi against p300 but not CBP decreased DEX-induced DUSP1 gene expression. p300, CBP or scramble (control) siRNA was transfected into A549 cells. 48 h post-transfection, cells were treated with DMSO or DEX (0.5 µM) for 5 h. Total RNA was isolated and converted to cDNA. qPCR was used to monitor the expression of DUSP1 gene. The expression of Rpl19 gene was used as an internal control. Data represents the SEM of DEX-induced DUSP1 gene expression (DEX-treated cells divided by DMSO-treated cells), as a percent of the control siRNA response from at least three experiments.
    Anti β Actin C4 Sc 47778, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology β actin c4 hrp
    p300 is a transcriptional coactivator for GR-regulated DUSP1 gene transcription. A Glucocorticoid treatment increased the level of p300 and CBP at the DUSP1 GLS2 region. A549 cells were treated with DMSO or DEX (0.5 µM) for 10 min, and ChIP was performed with antibodies against p300, CBP and <t>IgG</t> (control). Data is shown from qPCR analyses with primers specific to the DUSP1 GLS2. B RNAi knockdown causes substantial reduction of p300 protein and CBP protein. A549 cells reverse transfected with p300, CBP or scramble siRNA were harvested 48 h post-transfection, then probed by Western blot using an antibody against p300 or CBP, with <t>β-actin</t> as a loading control. C RNAi against p300 but not CBP decreased DEX-induced DUSP1 gene expression. p300, CBP or scramble (control) siRNA was transfected into A549 cells. 48 h post-transfection, cells were treated with DMSO or DEX (0.5 µM) for 5 h. Total RNA was isolated and converted to cDNA. qPCR was used to monitor the expression of DUSP1 gene. The expression of Rpl19 gene was used as an internal control. Data represents the SEM of DEX-induced DUSP1 gene expression (DEX-treated cells divided by DMSO-treated cells), as a percent of the control siRNA response from at least three experiments.
    β Actin C4 Hrp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Santa Cruz Biotechnology β actin c4 mab
    p300 is a transcriptional coactivator for GR-regulated DUSP1 gene transcription. A Glucocorticoid treatment increased the level of p300 and CBP at the DUSP1 GLS2 region. A549 cells were treated with DMSO or DEX (0.5 µM) for 10 min, and ChIP was performed with antibodies against p300, CBP and <t>IgG</t> (control). Data is shown from qPCR analyses with primers specific to the DUSP1 GLS2. B RNAi knockdown causes substantial reduction of p300 protein and CBP protein. A549 cells reverse transfected with p300, CBP or scramble siRNA were harvested 48 h post-transfection, then probed by Western blot using an antibody against p300 or CBP, with <t>β-actin</t> as a loading control. C RNAi against p300 but not CBP decreased DEX-induced DUSP1 gene expression. p300, CBP or scramble (control) siRNA was transfected into A549 cells. 48 h post-transfection, cells were treated with DMSO or DEX (0.5 µM) for 5 h. Total RNA was isolated and converted to cDNA. qPCR was used to monitor the expression of DUSP1 gene. The expression of Rpl19 gene was used as an internal control. Data represents the SEM of DEX-induced DUSP1 gene expression (DEX-treated cells divided by DMSO-treated cells), as a percent of the control siRNA response from at least three experiments.
    β Actin C4 Mab, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Santa Cruz Biotechnology mouse anti β actin c 4
    p300 is a transcriptional coactivator for GR-regulated DUSP1 gene transcription. A Glucocorticoid treatment increased the level of p300 and CBP at the DUSP1 GLS2 region. A549 cells were treated with DMSO or DEX (0.5 µM) for 10 min, and ChIP was performed with antibodies against p300, CBP and <t>IgG</t> (control). Data is shown from qPCR analyses with primers specific to the DUSP1 GLS2. B RNAi knockdown causes substantial reduction of p300 protein and CBP protein. A549 cells reverse transfected with p300, CBP or scramble siRNA were harvested 48 h post-transfection, then probed by Western blot using an antibody against p300 or CBP, with <t>β-actin</t> as a loading control. C RNAi against p300 but not CBP decreased DEX-induced DUSP1 gene expression. p300, CBP or scramble (control) siRNA was transfected into A549 cells. 48 h post-transfection, cells were treated with DMSO or DEX (0.5 µM) for 5 h. Total RNA was isolated and converted to cDNA. qPCR was used to monitor the expression of DUSP1 gene. The expression of Rpl19 gene was used as an internal control. Data represents the SEM of DEX-induced DUSP1 gene expression (DEX-treated cells divided by DMSO-treated cells), as a percent of the control siRNA response from at least three experiments.
    Mouse Anti β Actin C 4, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    miR-23a/b directly targets Tmem64 . ( a ) Schematic representation of the predicted miR-23a/b target site in the 3′-UTR of mouse Tmem64 . The alignment of miR-23a/b with WT and MUT 3′-UTR region is shown by complementary pairing, and three mutated nucleotides are underlined. ( b ) BMSCs were co-transfected with the luciferase reporter carrying WT-pGL3- Tmem64 or MUT-pGL3- Tmem64 along with agomiR-23a/b or agomiR-NC. The effects of miR-23a/b on the luciferase reporter constructs were determined 48 h after transfection. The firefly luciferase values were normalized to Renilla luciferase; n =5. ( c ) After BMSCs were transfected with agomiR-23a/b or antagomiR-23a/b, the relative levels of Tmem64 protein expression were determined by western blot; β-actin was used as loading control; n =5. ( d ) The relative levels of Tmem64 mRNA were determined using qRT-PCR and normalized to β-actin; n =5. ( e ) Tmem64 protein levels in BMSCs from 3- and 18-month-old mice were measured by western blot and expressed as the densitometry of Tmem64/β-actin. Tmem64 mRNA levels were determined by qRT-PCR and are shown as the fold-induction relative to β-actin; n =3. ( f ) The increase in ALP activity induced by agomiR-23a/b was blocked by the transfection of MUT Tmem64 3′-UTR into osteogenic-induced-BMSCs. * P

    Journal: Bone Research

    Article Title: miR-23a/b regulates the balance between osteoblast and adipocyte differentiation in bone marrow mesenchymal stem cells

    doi: 10.1038/boneres.2016.22

    Figure Lengend Snippet: miR-23a/b directly targets Tmem64 . ( a ) Schematic representation of the predicted miR-23a/b target site in the 3′-UTR of mouse Tmem64 . The alignment of miR-23a/b with WT and MUT 3′-UTR region is shown by complementary pairing, and three mutated nucleotides are underlined. ( b ) BMSCs were co-transfected with the luciferase reporter carrying WT-pGL3- Tmem64 or MUT-pGL3- Tmem64 along with agomiR-23a/b or agomiR-NC. The effects of miR-23a/b on the luciferase reporter constructs were determined 48 h after transfection. The firefly luciferase values were normalized to Renilla luciferase; n =5. ( c ) After BMSCs were transfected with agomiR-23a/b or antagomiR-23a/b, the relative levels of Tmem64 protein expression were determined by western blot; β-actin was used as loading control; n =5. ( d ) The relative levels of Tmem64 mRNA were determined using qRT-PCR and normalized to β-actin; n =5. ( e ) Tmem64 protein levels in BMSCs from 3- and 18-month-old mice were measured by western blot and expressed as the densitometry of Tmem64/β-actin. Tmem64 mRNA levels were determined by qRT-PCR and are shown as the fold-induction relative to β-actin; n =3. ( f ) The increase in ALP activity induced by agomiR-23a/b was blocked by the transfection of MUT Tmem64 3′-UTR into osteogenic-induced-BMSCs. * P

    Article Snippet: Tmem64 levels were detected using an anti-Tmem64 antibody (sc-87460; Santa Cruz, Dallas, TX, USA) and were normalized to β-actin (ab3280; Abcam, Cambridge, MA, USA).

    Techniques: Transfection, Luciferase, Construct, Expressing, Western Blot, Quantitative RT-PCR, Mouse Assay, ALP Assay, Activity Assay

    Constitutive expression of a NLS–β-actin R62D transgene opposes LN1-mediated transcriptional repression. ( A ) (i) Nuclei from ScP2 cells cultured under growth conditions were analyzed for colocalization of NLS–β-actin with

    Journal: Journal of Cell Science

    Article Title: Depletion of nuclear actin is a key mediator of quiescence in epithelial cells

    doi: 10.1242/jcs.073197

    Figure Lengend Snippet: Constitutive expression of a NLS–β-actin R62D transgene opposes LN1-mediated transcriptional repression. ( A ) (i) Nuclei from ScP2 cells cultured under growth conditions were analyzed for colocalization of NLS–β-actin with

    Article Snippet: The following antibodies were used: rabbit-anti-lamin A/C (Santa Cruz 1/500), -anti-β-actin (ab1801 from Abcam; used for immunolabeling experiments at 1/100), -anti-histone H3 (Abcam, 1/10,000), -anti-acetylated histone H4 (Upstate Biotech, 1/500), -anti-cofilin (Abcam, 1/1000), -anti-Pol II (Santa Cruz: N20, 1/100), -anti-RNA Pol II P -Ser5 (Abcam, 1/500), -anti-RPC32 (Santa Cruz Biotech, CA), -anti-FLAG (Sigma, 1/750); mouse-anti-β-actin [A5441 (Clone AC-15) from Sigma, used for western blot analysis at 1/1000], -anti-β-actin [Ab3280 (ACTN05-C4) from Abcam, used for western blot analysis at 1:1000], -anti-bromodeoxyuridine (BrdU) (Invitrogen, 1/75; Roche, 1/10), -anti-FLAG (Sigma, 1/750); rat-anti-BrdU (Abcam, 1/100), -anti-LN1 α1 chain (clones 198 and 200; a kind gift from Lydia Sorokin, 1/50); sheep anti-BrdU (Abcam, 1/100); anti-rabbit, -mouse, -rat and -sheep secondary antibodies conjugated to Alexa Fluor 488 or 594 (Invitrogen, 1/400).

    Techniques: Expressing, Cell Culture

    The levels of β-actin are high in the invading tip of terminal end buds and correlate inversely with LN1 localization. Sections of terminal end buds from pre-pubertal mouse mammary glands were labeled with ( A ) an antibody against β-actin

    Journal: Journal of Cell Science

    Article Title: Depletion of nuclear actin is a key mediator of quiescence in epithelial cells

    doi: 10.1242/jcs.073197

    Figure Lengend Snippet: The levels of β-actin are high in the invading tip of terminal end buds and correlate inversely with LN1 localization. Sections of terminal end buds from pre-pubertal mouse mammary glands were labeled with ( A ) an antibody against β-actin

    Article Snippet: The following antibodies were used: rabbit-anti-lamin A/C (Santa Cruz 1/500), -anti-β-actin (ab1801 from Abcam; used for immunolabeling experiments at 1/100), -anti-histone H3 (Abcam, 1/10,000), -anti-acetylated histone H4 (Upstate Biotech, 1/500), -anti-cofilin (Abcam, 1/1000), -anti-Pol II (Santa Cruz: N20, 1/100), -anti-RNA Pol II P -Ser5 (Abcam, 1/500), -anti-RPC32 (Santa Cruz Biotech, CA), -anti-FLAG (Sigma, 1/750); mouse-anti-β-actin [A5441 (Clone AC-15) from Sigma, used for western blot analysis at 1/1000], -anti-β-actin [Ab3280 (ACTN05-C4) from Abcam, used for western blot analysis at 1:1000], -anti-bromodeoxyuridine (BrdU) (Invitrogen, 1/75; Roche, 1/10), -anti-FLAG (Sigma, 1/750); rat-anti-BrdU (Abcam, 1/100), -anti-LN1 α1 chain (clones 198 and 200; a kind gift from Lydia Sorokin, 1/50); sheep anti-BrdU (Abcam, 1/100); anti-rabbit, -mouse, -rat and -sheep secondary antibodies conjugated to Alexa Fluor 488 or 594 (Invitrogen, 1/400).

    Techniques: Labeling

    Growth and quiescence correlate with nuclear β-actin levels. ( A ) Mouse ScP2 cells were cultured under growth conditions for 48 hours and co-immunolabeled with antibodies against β-actin (green) and BrdU (red). The data show that, during

    Journal: Journal of Cell Science

    Article Title: Depletion of nuclear actin is a key mediator of quiescence in epithelial cells

    doi: 10.1242/jcs.073197

    Figure Lengend Snippet: Growth and quiescence correlate with nuclear β-actin levels. ( A ) Mouse ScP2 cells were cultured under growth conditions for 48 hours and co-immunolabeled with antibodies against β-actin (green) and BrdU (red). The data show that, during

    Article Snippet: The following antibodies were used: rabbit-anti-lamin A/C (Santa Cruz 1/500), -anti-β-actin (ab1801 from Abcam; used for immunolabeling experiments at 1/100), -anti-histone H3 (Abcam, 1/10,000), -anti-acetylated histone H4 (Upstate Biotech, 1/500), -anti-cofilin (Abcam, 1/1000), -anti-Pol II (Santa Cruz: N20, 1/100), -anti-RNA Pol II P -Ser5 (Abcam, 1/500), -anti-RPC32 (Santa Cruz Biotech, CA), -anti-FLAG (Sigma, 1/750); mouse-anti-β-actin [A5441 (Clone AC-15) from Sigma, used for western blot analysis at 1/1000], -anti-β-actin [Ab3280 (ACTN05-C4) from Abcam, used for western blot analysis at 1:1000], -anti-bromodeoxyuridine (BrdU) (Invitrogen, 1/75; Roche, 1/10), -anti-FLAG (Sigma, 1/750); rat-anti-BrdU (Abcam, 1/100), -anti-LN1 α1 chain (clones 198 and 200; a kind gift from Lydia Sorokin, 1/50); sheep anti-BrdU (Abcam, 1/100); anti-rabbit, -mouse, -rat and -sheep secondary antibodies conjugated to Alexa Fluor 488 or 594 (Invitrogen, 1/400).

    Techniques: Cell Culture, Immunolabeling

    Constitutive expression of a NLS–β-actin or NLS–β-actin R62D transgene opposes LN1-mediated growth arrest. ( A ) EpH4 cells were stably transfected with FLAG-tagged NLS–wild-type-β-actin. Clones expressing

    Journal: Journal of Cell Science

    Article Title: Depletion of nuclear actin is a key mediator of quiescence in epithelial cells

    doi: 10.1242/jcs.073197

    Figure Lengend Snippet: Constitutive expression of a NLS–β-actin or NLS–β-actin R62D transgene opposes LN1-mediated growth arrest. ( A ) EpH4 cells were stably transfected with FLAG-tagged NLS–wild-type-β-actin. Clones expressing

    Article Snippet: The following antibodies were used: rabbit-anti-lamin A/C (Santa Cruz 1/500), -anti-β-actin (ab1801 from Abcam; used for immunolabeling experiments at 1/100), -anti-histone H3 (Abcam, 1/10,000), -anti-acetylated histone H4 (Upstate Biotech, 1/500), -anti-cofilin (Abcam, 1/1000), -anti-Pol II (Santa Cruz: N20, 1/100), -anti-RNA Pol II P -Ser5 (Abcam, 1/500), -anti-RPC32 (Santa Cruz Biotech, CA), -anti-FLAG (Sigma, 1/750); mouse-anti-β-actin [A5441 (Clone AC-15) from Sigma, used for western blot analysis at 1/1000], -anti-β-actin [Ab3280 (ACTN05-C4) from Abcam, used for western blot analysis at 1:1000], -anti-bromodeoxyuridine (BrdU) (Invitrogen, 1/75; Roche, 1/10), -anti-FLAG (Sigma, 1/750); rat-anti-BrdU (Abcam, 1/100), -anti-LN1 α1 chain (clones 198 and 200; a kind gift from Lydia Sorokin, 1/50); sheep anti-BrdU (Abcam, 1/100); anti-rabbit, -mouse, -rat and -sheep secondary antibodies conjugated to Alexa Fluor 488 or 594 (Invitrogen, 1/400).

    Techniques: Expressing, Stable Transfection, Transfection, Clone Assay

    There is a statistically significant colocalization of nuclear β-actin with transcription foci. ( A ) Immunofluorescence localization of FU incorporation sites in a tissue section of a terminal end bud from pre-pubertal mouse mammary gland. Note

    Journal: Journal of Cell Science

    Article Title: Depletion of nuclear actin is a key mediator of quiescence in epithelial cells

    doi: 10.1242/jcs.073197

    Figure Lengend Snippet: There is a statistically significant colocalization of nuclear β-actin with transcription foci. ( A ) Immunofluorescence localization of FU incorporation sites in a tissue section of a terminal end bud from pre-pubertal mouse mammary gland. Note

    Article Snippet: The following antibodies were used: rabbit-anti-lamin A/C (Santa Cruz 1/500), -anti-β-actin (ab1801 from Abcam; used for immunolabeling experiments at 1/100), -anti-histone H3 (Abcam, 1/10,000), -anti-acetylated histone H4 (Upstate Biotech, 1/500), -anti-cofilin (Abcam, 1/1000), -anti-Pol II (Santa Cruz: N20, 1/100), -anti-RNA Pol II P -Ser5 (Abcam, 1/500), -anti-RPC32 (Santa Cruz Biotech, CA), -anti-FLAG (Sigma, 1/750); mouse-anti-β-actin [A5441 (Clone AC-15) from Sigma, used for western blot analysis at 1/1000], -anti-β-actin [Ab3280 (ACTN05-C4) from Abcam, used for western blot analysis at 1:1000], -anti-bromodeoxyuridine (BrdU) (Invitrogen, 1/75; Roche, 1/10), -anti-FLAG (Sigma, 1/750); rat-anti-BrdU (Abcam, 1/100), -anti-LN1 α1 chain (clones 198 and 200; a kind gift from Lydia Sorokin, 1/50); sheep anti-BrdU (Abcam, 1/100); anti-rabbit, -mouse, -rat and -sheep secondary antibodies conjugated to Alexa Fluor 488 or 594 (Invitrogen, 1/400).

    Techniques: Immunofluorescence

    Schematic model of the sequence of LN1-initiated events that give rise to quiescence. ( A ) Exposure of mammary epithelial cells to LN1 induces a dramatic decline in the levels of nuclear β-actin, nuclear matrix (NM)-associated RNA Pol III and DNA

    Journal: Journal of Cell Science

    Article Title: Depletion of nuclear actin is a key mediator of quiescence in epithelial cells

    doi: 10.1242/jcs.073197

    Figure Lengend Snippet: Schematic model of the sequence of LN1-initiated events that give rise to quiescence. ( A ) Exposure of mammary epithelial cells to LN1 induces a dramatic decline in the levels of nuclear β-actin, nuclear matrix (NM)-associated RNA Pol III and DNA

    Article Snippet: The following antibodies were used: rabbit-anti-lamin A/C (Santa Cruz 1/500), -anti-β-actin (ab1801 from Abcam; used for immunolabeling experiments at 1/100), -anti-histone H3 (Abcam, 1/10,000), -anti-acetylated histone H4 (Upstate Biotech, 1/500), -anti-cofilin (Abcam, 1/1000), -anti-Pol II (Santa Cruz: N20, 1/100), -anti-RNA Pol II P -Ser5 (Abcam, 1/500), -anti-RPC32 (Santa Cruz Biotech, CA), -anti-FLAG (Sigma, 1/750); mouse-anti-β-actin [A5441 (Clone AC-15) from Sigma, used for western blot analysis at 1/1000], -anti-β-actin [Ab3280 (ACTN05-C4) from Abcam, used for western blot analysis at 1:1000], -anti-bromodeoxyuridine (BrdU) (Invitrogen, 1/75; Roche, 1/10), -anti-FLAG (Sigma, 1/750); rat-anti-BrdU (Abcam, 1/100), -anti-LN1 α1 chain (clones 198 and 200; a kind gift from Lydia Sorokin, 1/50); sheep anti-BrdU (Abcam, 1/100); anti-rabbit, -mouse, -rat and -sheep secondary antibodies conjugated to Alexa Fluor 488 or 594 (Invitrogen, 1/400).

    Techniques: Sequencing

    PA blocked proper mitophagy activation in macrophage cells. (A) PA stimulated autophagy activation associated proteins LC3II/LC3I, P62, Lamp2, and CTSB expression were analyzed by immunoblotting, β-actin as a control; analysis of Lamp2, LC3II, and P62 levels from macrophage cells were on the right panel (*, p

    Journal: Redox Biology

    Article Title: Defective mitophagy driven by dysregulation of rheb and KIF5B contributes to mitochondrial reactive oxygen species (ROS)-induced nod-like receptor 3 (NLRP3) dependent proinflammatory response and aggravates lipotoxicity

    doi: 10.1016/j.redox.2014.04.001

    Figure Lengend Snippet: PA blocked proper mitophagy activation in macrophage cells. (A) PA stimulated autophagy activation associated proteins LC3II/LC3I, P62, Lamp2, and CTSB expression were analyzed by immunoblotting, β-actin as a control; analysis of Lamp2, LC3II, and P62 levels from macrophage cells were on the right panel (*, p

    Article Snippet: The following primary antibodies were used for Western blots and immunostaining: rabbit anti-LC3 (Sigma, L8918); Rat monoclonal to LAMP2 (Abcam, ab13524); anti-β actin antibody (Abcam, ab3280); rabbit polyclonal anti-Atg7 (Cell Signaling Technology, 2631); Anti-IL-1β antibody (Abcam, ab2105); Anti-IL6 antibody (Abcam, ab6672); Anti-MCP1 antibody (Abcam, ab9669); Anti-TNF alpha antibody (Abcam, ab9635); guinea pig polyclonal anti-p62 (ProGen, GP62-N); anti-Rheb(Abcam, ab2587); anti-Tom20 (SantaCruz, sc-17764); anti-calregulin (SantaCruz, sc-6468-R); anti-Gapdh (Abcam, ab9483); anti-Golgi 58 (Abcam, ab27043); Alexa Fluor-conjugated antibodies (Molecular probes, A21057 , A21076 , A21096 ) were used as secondary antibodies.

    Techniques: Activation Assay, Expressing

    Knock‐down of ADAM 10 is less effective at reducing the shedding of H157Y TREM 2 Western blot of HEK293 cells for ADAM10 (A) or ADAM17 and reprobed for β‐actin (B) confirmed siRNA‐mediated knock‐down of target proteins (arrowheads). siRNA pools, or vehicle, added to cells as indicated. β‐actin (asterisk) was the loading control. Quantitation of WT and H157Y (SEM error bars) TREM2 NTF in the conditioned media of HEK293 cells as compared to untreated cells measured by MSD assay ( N = 8): ADAM10 siRNA reduced shedding whether applied alone or in combination with ADAM17 siRNA. ADAM17 siRNA was ineffective. Fractional inhibition of shedding was greatest for WT TREM2 using ADAM10 siRNA. Source data are available online for this figure.

    Journal: EMBO Molecular Medicine

    Article Title: TREM2 shedding by cleavage at the H157‐S158 bond is accelerated for the Alzheimer's disease‐associated H157Y variant

    doi: 10.15252/emmm.201707673

    Figure Lengend Snippet: Knock‐down of ADAM 10 is less effective at reducing the shedding of H157Y TREM 2 Western blot of HEK293 cells for ADAM10 (A) or ADAM17 and reprobed for β‐actin (B) confirmed siRNA‐mediated knock‐down of target proteins (arrowheads). siRNA pools, or vehicle, added to cells as indicated. β‐actin (asterisk) was the loading control. Quantitation of WT and H157Y (SEM error bars) TREM2 NTF in the conditioned media of HEK293 cells as compared to untreated cells measured by MSD assay ( N = 8): ADAM10 siRNA reduced shedding whether applied alone or in combination with ADAM17 siRNA. ADAM17 siRNA was ineffective. Fractional inhibition of shedding was greatest for WT TREM2 using ADAM10 siRNA. Source data are available online for this figure.

    Article Snippet: Blots in the siRNA experiments were probed with polyclonal rabbit anti‐ADAM10 at 1:500 (14194S, Cell Signaling), rabbit anti‐ADAM17 at 1:500 (AB19027, Millipore) and mouse anti‐β‐actin at 1:1,000 (ab3280, Abcam).

    Techniques: Western Blot, Quantitation Assay, Inhibition

    A PPARα ligand prevents LPS-mediated up-regulation of C3 gene in mouse liver. Mice were intravenously injected with LPS, WY-14643 ( WY ), or DMSO (control), and the level of C3 expression in the liver 24 h after treatment was determined, and β-actin

    Journal: The Journal of Biological Chemistry

    Article Title: Peroxisome Proliferator-activated Receptor ? Positively Regulates Complement C3 Expression but Inhibits Tumor Necrosis Factor ?-mediated Activation of C3 Gene in Mammalian Hepatic-derived Cells *

    doi: 10.1074/jbc.M112.437525

    Figure Lengend Snippet: A PPARα ligand prevents LPS-mediated up-regulation of C3 gene in mouse liver. Mice were intravenously injected with LPS, WY-14643 ( WY ), or DMSO (control), and the level of C3 expression in the liver 24 h after treatment was determined, and β-actin

    Article Snippet: Mouse monoclonal antibodies against human β-actin (catalog no. ab3280), against human PPARα (catalog no. ab2779) were purchased from Abcam.

    Techniques: Mouse Assay, Injection, Expressing

    (A) Amounts of DNMT3A and DNMT1 in U937 cells and HL-60 cells after treatment with the indicated agent for 48 h. Values indicate the relative amounts of DNMT3A and DNMT1 normalized with β-ACTIN. (B) Amounts of DNMT3A and DNMT1 in R-U937 and R-HL-60 cells after treatment with the indicated agent for 48 h. Values indicate the relative amounts of DNMT3A and DNMT1 normalized with β-ACTIN.

    Journal: Oncotarget

    Article Title: Teriflunomide restores 5-azacytidine sensitivity via activation of pyrimidine salvage in 5-azacytidine-resistant leukemia cells

    doi: 10.18632/oncotarget.19436

    Figure Lengend Snippet: (A) Amounts of DNMT3A and DNMT1 in U937 cells and HL-60 cells after treatment with the indicated agent for 48 h. Values indicate the relative amounts of DNMT3A and DNMT1 normalized with β-ACTIN. (B) Amounts of DNMT3A and DNMT1 in R-U937 and R-HL-60 cells after treatment with the indicated agent for 48 h. Values indicate the relative amounts of DNMT3A and DNMT1 normalized with β-ACTIN.

    Article Snippet: The anti-DNMT1 antibody 4H80, the anti-DNMT3A antibody H-295, and the anti-β-ACTIN antibody C4 were purchased from Santa Cruz Biotechnology (Dallas, TX, USA).

    Techniques:

    p300 is a transcriptional coactivator for GR-regulated DUSP1 gene transcription. A Glucocorticoid treatment increased the level of p300 and CBP at the DUSP1 GLS2 region. A549 cells were treated with DMSO or DEX (0.5 µM) for 10 min, and ChIP was performed with antibodies against p300, CBP and IgG (control). Data is shown from qPCR analyses with primers specific to the DUSP1 GLS2. B RNAi knockdown causes substantial reduction of p300 protein and CBP protein. A549 cells reverse transfected with p300, CBP or scramble siRNA were harvested 48 h post-transfection, then probed by Western blot using an antibody against p300 or CBP, with β-actin as a loading control. C RNAi against p300 but not CBP decreased DEX-induced DUSP1 gene expression. p300, CBP or scramble (control) siRNA was transfected into A549 cells. 48 h post-transfection, cells were treated with DMSO or DEX (0.5 µM) for 5 h. Total RNA was isolated and converted to cDNA. qPCR was used to monitor the expression of DUSP1 gene. The expression of Rpl19 gene was used as an internal control. Data represents the SEM of DEX-induced DUSP1 gene expression (DEX-treated cells divided by DMSO-treated cells), as a percent of the control siRNA response from at least three experiments.

    Journal: PLoS ONE

    Article Title: Transcriptional Regulation of Human Dual Specificity Protein Phosphatase 1 (DUSP1) Gene by Glucocorticoids

    doi: 10.1371/journal.pone.0013754

    Figure Lengend Snippet: p300 is a transcriptional coactivator for GR-regulated DUSP1 gene transcription. A Glucocorticoid treatment increased the level of p300 and CBP at the DUSP1 GLS2 region. A549 cells were treated with DMSO or DEX (0.5 µM) for 10 min, and ChIP was performed with antibodies against p300, CBP and IgG (control). Data is shown from qPCR analyses with primers specific to the DUSP1 GLS2. B RNAi knockdown causes substantial reduction of p300 protein and CBP protein. A549 cells reverse transfected with p300, CBP or scramble siRNA were harvested 48 h post-transfection, then probed by Western blot using an antibody against p300 or CBP, with β-actin as a loading control. C RNAi against p300 but not CBP decreased DEX-induced DUSP1 gene expression. p300, CBP or scramble (control) siRNA was transfected into A549 cells. 48 h post-transfection, cells were treated with DMSO or DEX (0.5 µM) for 5 h. Total RNA was isolated and converted to cDNA. qPCR was used to monitor the expression of DUSP1 gene. The expression of Rpl19 gene was used as an internal control. Data represents the SEM of DEX-induced DUSP1 gene expression (DEX-treated cells divided by DMSO-treated cells), as a percent of the control siRNA response from at least three experiments.

    Article Snippet: The following antibodies were used: p300 rabbit polyclonal IgG (sc-584; Santa Cruz Biotechnology), CBP mouse monoclonal IgG1 (sc-7300, Santa Cruz Biotechnology), β-Actin (C4) mouse monoclonal IgG1 (sc-47778; Santa Cruz Biotechnology), anti-rabbit IgG1 -HRP (Cell Signaling), and anti-mouse IgG1 -HRP (sc-2060; Santa Cruz Biotechnology).

    Techniques: Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction, Transfection, Western Blot, Expressing, Isolation