monoclonal anti beta actin antibody Millipore Search Results


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  • 97
    Thermo Fisher anti β actin
    The conditional deletion of Cdc42 in the lactating mammary gland stunts nursing pup growth. A , schematic timeline describing the conditional gene deletion strategy used in this study, with illustrations depicting the development of the mammary gland in each developmental stage. B , Western blot of tissue lysates showing whole-gland Cdc42 expression from the stages of virgin to lactation day 20 (L20), with <t>β-actin</t> serving as a loading control. C , growth plot depicting average weight of individual pups ( n = 30) feeding from a CCKO mother ( blue ), or from a control mother ( red ), throughout lactation. Error bars represent the standard deviation to the mean pup mass at each given time point. D , growth plot depicting average weight of individual pups ( n = 30) that were fostered from a control mother to a CCKO mother ( blue ), or from a CCKO mother to a control mother ( red ). Error bars represent the standard deviation to the mean pup mass at each given time point.
    Anti β Actin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 611 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Millipore anti beta actin mab
    Immunoblot analysis of cultured fibroblasts from the normal human control and the proband. Immunoblot analysis of extracts from fibroblasts of the normal control and the proband by using PN643 against the N-terminal actin- binding domain, HD1-121 against the rod domain and C20 against the C-terminal plectin repeats. Rodless plectin (arrows), detected with PN643 and C20, migrates just below full-length plectin (arrowheads) in normal human fibroblasts. Using HD1-121, only full-length plectin is observed in the normal control. In contrast, fibroblasts of the proband contained smaller proteins than 500-kDa full-length plectin, the putatively truncated full-length plectin (asterisks), which was detected with PN643 and HD1-121. C20 did not react with lysates of the proband's fibroblasts. Equal protein loading was confirmed by reprobing with AC 15 <t>(anti-beta-actin</t> antibody).
    Anti Beta Actin Mab, 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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    82
    Millipore mab mouse anti beta actin
    Hyperoxia does not affect astrocyte number, but decreases astrocytic GLAST expression in the immature WM ( A1-5, B1-5 ) Immunofluorescence labeling with antibodies for glial fibrillary acidic protein (GFAP), glutamine synthetase (GS), the glutamate-aspartate transporter (GLAST) and the nuclear fluorescent stain DAPI to determine GLAST expression in GFAP + GS + astrocytes (GFAP + GS + GLAST + cells) in WT mice at P8. Arrowheads indicate cells positive for each respective marker and all four in merged image. ( C1-5 ) Enlarged image of boxed region in A showing three GFAP + GS + GLAST + DAPI + cells from a control mouse. ( D ) Histrogram showing no difference in the number of astrocytes or glutamate transporter GLT-1 positive astrocytes (GFAP + GS + GLT-1 + cells) between the control and hyperoxia experimental groups at P8. However, hyperoxia reduced the number of astrocytes expressing GLAST. ( E ) Data indicating that hyperoxia decreases the percentage of GLAST-expressing astrocytes without changing the number of astrocytes expressing GLT-1 at P8. ( F, G ) Immuno-labeling with antibodies for GFAP, GS, GLT-1 and DAPI to analyze astrocyte numbers and the amount of astrocytes expressing GLT-1 in WT mice at P12. Arrowheads indicate cells positive for each respective marker and all four in merged image. ( H , I ) No change in the total number of GFAP + GS + GLAST + cells or GFAP + GS + GLT-1 + cells was observed at P12. ( J, K ) Densitometric analysis of GLAST and GLT-1 western blots at P8 and P12. Hyperoxia caused a decrease in GLAST protein levels immediately following exposure ( J, ). After 4 days of room air recovery ( K ), WM GLAST protein expression returned to the level of controls. No changes in GLT-1 levels were observed in hyperoxia exposed animals. Values represent standardized mean ratios for the protein of interest (POI) and <t>β-actin.</t> ( L ) Representative western blots of GLAST, GLT-1 and β-actin protein expression using micro-dissected WM tissue from P8 and P12 animals in each experimental group. For each group and time point, n = 3 – 5 brains. An unpaired t-test comparing control vs. hyperoxia, where *P
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    89
    Merck KGaA monoclonal anti beta actin
    Hyperoxia does not affect astrocyte number, but decreases astrocytic GLAST expression in the immature WM ( A1-5, B1-5 ) Immunofluorescence labeling with antibodies for glial fibrillary acidic protein (GFAP), glutamine synthetase (GS), the glutamate-aspartate transporter (GLAST) and the nuclear fluorescent stain DAPI to determine GLAST expression in GFAP + GS + astrocytes (GFAP + GS + GLAST + cells) in WT mice at P8. Arrowheads indicate cells positive for each respective marker and all four in merged image. ( C1-5 ) Enlarged image of boxed region in A showing three GFAP + GS + GLAST + DAPI + cells from a control mouse. ( D ) Histrogram showing no difference in the number of astrocytes or glutamate transporter GLT-1 positive astrocytes (GFAP + GS + GLT-1 + cells) between the control and hyperoxia experimental groups at P8. However, hyperoxia reduced the number of astrocytes expressing GLAST. ( E ) Data indicating that hyperoxia decreases the percentage of GLAST-expressing astrocytes without changing the number of astrocytes expressing GLT-1 at P8. ( F, G ) Immuno-labeling with antibodies for GFAP, GS, GLT-1 and DAPI to analyze astrocyte numbers and the amount of astrocytes expressing GLT-1 in WT mice at P12. Arrowheads indicate cells positive for each respective marker and all four in merged image. ( H , I ) No change in the total number of GFAP + GS + GLAST + cells or GFAP + GS + GLT-1 + cells was observed at P12. ( J, K ) Densitometric analysis of GLAST and GLT-1 western blots at P8 and P12. Hyperoxia caused a decrease in GLAST protein levels immediately following exposure ( J, ). After 4 days of room air recovery ( K ), WM GLAST protein expression returned to the level of controls. No changes in GLT-1 levels were observed in hyperoxia exposed animals. Values represent standardized mean ratios for the protein of interest (POI) and <t>β-actin.</t> ( L ) Representative western blots of GLAST, GLT-1 and β-actin protein expression using micro-dissected WM tissue from P8 and P12 animals in each experimental group. For each group and time point, n = 3 – 5 brains. An unpaired t-test comparing control vs. hyperoxia, where *P
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    99
    Millipore monoclonal anti beta actin antibody
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
    Monoclonal Anti Beta Actin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 26675 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti ß actin mab
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
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    99
    Millipore beta actin
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
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    Millipore anti β actin mab
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
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    Millipore anti beta actin antibody
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
    Anti Beta Actin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 316 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Millipore β actin mab hrp
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
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    83
    Millipore mouse monoclonal anti beta actin actb
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
    Mouse Monoclonal Anti Beta Actin Actb, supplied by Millipore, used in various techniques. Bioz Stars score: 83/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Abcam monoclonal anti beta actin antibody
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
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    Millipore anti beta actin antibody mouse monoclonal
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
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    Millipore monoclonal anti beta actin peroxidase antibody
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
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    96
    Millipore anti beta actin antibody rabbit monoclonal
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
    Anti Beta Actin Antibody Rabbit Monoclonal, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 99 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore mouse monoclonal anti beta actin antibody
    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and <t>β-actin</t> as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).
    Mouse Monoclonal Anti Beta Actin Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore β actin
    miR-27a knockdown promotes autophagy in CRC cells. ( a ) Morphological features of HCT116 CRTL, miR27a_KD and miR27a_OE cells were evaluated by hematoxylin and eosin staining; the arrows point out some remarkable phenotypic characteristics (Scale bar, 20 mm). ( b ) Dose-dependent induction of autophagy in HCT116 CRTL, miR27a_KD and miR27a_OE cells exposed to the lysosomotropic drug chloroquine (CQ). Western blot analysis of the LC3-II mature form, an autophagic marker, is reported along with its relative quantification in the histogram. <t>β</t> -Actin was used as loading control. ( c ) Time-course of autophagy induction in HCT116 CRTL, miR27a_KD and miR27a_OE cells upon MTX treatment at 1 μ M. Immunoblot of LC-3-II was used as a marker. All data are representative of three independent experiments and error bars represent S.D. of technical replicates (mean±S.D.)
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    70
    Millipore anti actin control mab
    miR-27a knockdown promotes autophagy in CRC cells. ( a ) Morphological features of HCT116 CRTL, miR27a_KD and miR27a_OE cells were evaluated by hematoxylin and eosin staining; the arrows point out some remarkable phenotypic characteristics (Scale bar, 20 mm). ( b ) Dose-dependent induction of autophagy in HCT116 CRTL, miR27a_KD and miR27a_OE cells exposed to the lysosomotropic drug chloroquine (CQ). Western blot analysis of the LC3-II mature form, an autophagic marker, is reported along with its relative quantification in the histogram. <t>β</t> -Actin was used as loading control. ( c ) Time-course of autophagy induction in HCT116 CRTL, miR27a_KD and miR27a_OE cells upon MTX treatment at 1 μ M. Immunoblot of LC-3-II was used as a marker. All data are representative of three independent experiments and error bars represent S.D. of technical replicates (mean±S.D.)
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    Millipore β actin mab
    miR-27a knockdown promotes autophagy in CRC cells. ( a ) Morphological features of HCT116 CRTL, miR27a_KD and miR27a_OE cells were evaluated by hematoxylin and eosin staining; the arrows point out some remarkable phenotypic characteristics (Scale bar, 20 mm). ( b ) Dose-dependent induction of autophagy in HCT116 CRTL, miR27a_KD and miR27a_OE cells exposed to the lysosomotropic drug chloroquine (CQ). Western blot analysis of the LC3-II mature form, an autophagic marker, is reported along with its relative quantification in the histogram. <t>β</t> -Actin was used as loading control. ( c ) Time-course of autophagy induction in HCT116 CRTL, miR27a_KD and miR27a_OE cells upon MTX treatment at 1 μ M. Immunoblot of LC-3-II was used as a marker. All data are representative of three independent experiments and error bars represent S.D. of technical replicates (mean±S.D.)
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    Millipore anti actin mab ac 40
    miR-27a knockdown promotes autophagy in CRC cells. ( a ) Morphological features of HCT116 CRTL, miR27a_KD and miR27a_OE cells were evaluated by hematoxylin and eosin staining; the arrows point out some remarkable phenotypic characteristics (Scale bar, 20 mm). ( b ) Dose-dependent induction of autophagy in HCT116 CRTL, miR27a_KD and miR27a_OE cells exposed to the lysosomotropic drug chloroquine (CQ). Western blot analysis of the LC3-II mature form, an autophagic marker, is reported along with its relative quantification in the histogram. <t>β</t> -Actin was used as loading control. ( c ) Time-course of autophagy induction in HCT116 CRTL, miR27a_KD and miR27a_OE cells upon MTX treatment at 1 μ M. Immunoblot of LC-3-II was used as a marker. All data are representative of three independent experiments and error bars represent S.D. of technical replicates (mean±S.D.)
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    Image Search Results


    The conditional deletion of Cdc42 in the lactating mammary gland stunts nursing pup growth. A , schematic timeline describing the conditional gene deletion strategy used in this study, with illustrations depicting the development of the mammary gland in each developmental stage. B , Western blot of tissue lysates showing whole-gland Cdc42 expression from the stages of virgin to lactation day 20 (L20), with β-actin serving as a loading control. C , growth plot depicting average weight of individual pups ( n = 30) feeding from a CCKO mother ( blue ), or from a control mother ( red ), throughout lactation. Error bars represent the standard deviation to the mean pup mass at each given time point. D , growth plot depicting average weight of individual pups ( n = 30) that were fostered from a control mother to a CCKO mother ( blue ), or from a CCKO mother to a control mother ( red ). Error bars represent the standard deviation to the mean pup mass at each given time point.

    Journal: The Journal of Biological Chemistry

    Article Title: An Essential Role for Cdc42 in the Functioning of the Adult Mammary Gland *

    doi: 10.1074/jbc.M115.694349

    Figure Lengend Snippet: The conditional deletion of Cdc42 in the lactating mammary gland stunts nursing pup growth. A , schematic timeline describing the conditional gene deletion strategy used in this study, with illustrations depicting the development of the mammary gland in each developmental stage. B , Western blot of tissue lysates showing whole-gland Cdc42 expression from the stages of virgin to lactation day 20 (L20), with β-actin serving as a loading control. C , growth plot depicting average weight of individual pups ( n = 30) feeding from a CCKO mother ( blue ), or from a control mother ( red ), throughout lactation. Error bars represent the standard deviation to the mean pup mass at each given time point. D , growth plot depicting average weight of individual pups ( n = 30) that were fostered from a control mother to a CCKO mother ( blue ), or from a CCKO mother to a control mother ( red ). Error bars represent the standard deviation to the mean pup mass at each given time point.

    Article Snippet: Anti-cleaved caspase-3 (AB3623) antibody was purchased from EMD Millipore, anti-β-actin (MA5–15739) was purchased from ThermoFisher Scientific, and anti-Par 6 (25525) antibody was obtained from Santa Cruz Biotechnology.

    Techniques: Western Blot, Expressing, Standard Deviation

    Immunoblot analysis of cultured fibroblasts from the normal human control and the proband. Immunoblot analysis of extracts from fibroblasts of the normal control and the proband by using PN643 against the N-terminal actin- binding domain, HD1-121 against the rod domain and C20 against the C-terminal plectin repeats. Rodless plectin (arrows), detected with PN643 and C20, migrates just below full-length plectin (arrowheads) in normal human fibroblasts. Using HD1-121, only full-length plectin is observed in the normal control. In contrast, fibroblasts of the proband contained smaller proteins than 500-kDa full-length plectin, the putatively truncated full-length plectin (asterisks), which was detected with PN643 and HD1-121. C20 did not react with lysates of the proband's fibroblasts. Equal protein loading was confirmed by reprobing with AC 15 (anti-beta-actin antibody).

    Journal: Human Mutation

    Article Title: Plectin Deficiency Leads to Both Muscular Dystrophy and Pyloric Atresia in Epidermolysis Bullosa Simplex

    doi: 10.1002/humu.21330

    Figure Lengend Snippet: Immunoblot analysis of cultured fibroblasts from the normal human control and the proband. Immunoblot analysis of extracts from fibroblasts of the normal control and the proband by using PN643 against the N-terminal actin- binding domain, HD1-121 against the rod domain and C20 against the C-terminal plectin repeats. Rodless plectin (arrows), detected with PN643 and C20, migrates just below full-length plectin (arrowheads) in normal human fibroblasts. Using HD1-121, only full-length plectin is observed in the normal control. In contrast, fibroblasts of the proband contained smaller proteins than 500-kDa full-length plectin, the putatively truncated full-length plectin (asterisks), which was detected with PN643 and HD1-121. C20 did not react with lysates of the proband's fibroblasts. Equal protein loading was confirmed by reprobing with AC 15 (anti-beta-actin antibody).

    Article Snippet: Anti-beta-actin mAb (AC15, Sigma, St. Louis, MO) was used to confirm equal protein loading.

    Techniques: Cell Culture, Binding Assay

    Hyperoxia does not affect astrocyte number, but decreases astrocytic GLAST expression in the immature WM ( A1-5, B1-5 ) Immunofluorescence labeling with antibodies for glial fibrillary acidic protein (GFAP), glutamine synthetase (GS), the glutamate-aspartate transporter (GLAST) and the nuclear fluorescent stain DAPI to determine GLAST expression in GFAP + GS + astrocytes (GFAP + GS + GLAST + cells) in WT mice at P8. Arrowheads indicate cells positive for each respective marker and all four in merged image. ( C1-5 ) Enlarged image of boxed region in A showing three GFAP + GS + GLAST + DAPI + cells from a control mouse. ( D ) Histrogram showing no difference in the number of astrocytes or glutamate transporter GLT-1 positive astrocytes (GFAP + GS + GLT-1 + cells) between the control and hyperoxia experimental groups at P8. However, hyperoxia reduced the number of astrocytes expressing GLAST. ( E ) Data indicating that hyperoxia decreases the percentage of GLAST-expressing astrocytes without changing the number of astrocytes expressing GLT-1 at P8. ( F, G ) Immuno-labeling with antibodies for GFAP, GS, GLT-1 and DAPI to analyze astrocyte numbers and the amount of astrocytes expressing GLT-1 in WT mice at P12. Arrowheads indicate cells positive for each respective marker and all four in merged image. ( H , I ) No change in the total number of GFAP + GS + GLAST + cells or GFAP + GS + GLT-1 + cells was observed at P12. ( J, K ) Densitometric analysis of GLAST and GLT-1 western blots at P8 and P12. Hyperoxia caused a decrease in GLAST protein levels immediately following exposure ( J, ). After 4 days of room air recovery ( K ), WM GLAST protein expression returned to the level of controls. No changes in GLT-1 levels were observed in hyperoxia exposed animals. Values represent standardized mean ratios for the protein of interest (POI) and β-actin. ( L ) Representative western blots of GLAST, GLT-1 and β-actin protein expression using micro-dissected WM tissue from P8 and P12 animals in each experimental group. For each group and time point, n = 3 – 5 brains. An unpaired t-test comparing control vs. hyperoxia, where *P

    Journal: The Journal of neuroscience : the official journal of the Society for Neuroscience

    Article Title: Cellular Changes Underlying Hyperoxia-induced Delay of White Matter Development

    doi: 10.1523/JNEUROSCI.3942-10.2011

    Figure Lengend Snippet: Hyperoxia does not affect astrocyte number, but decreases astrocytic GLAST expression in the immature WM ( A1-5, B1-5 ) Immunofluorescence labeling with antibodies for glial fibrillary acidic protein (GFAP), glutamine synthetase (GS), the glutamate-aspartate transporter (GLAST) and the nuclear fluorescent stain DAPI to determine GLAST expression in GFAP + GS + astrocytes (GFAP + GS + GLAST + cells) in WT mice at P8. Arrowheads indicate cells positive for each respective marker and all four in merged image. ( C1-5 ) Enlarged image of boxed region in A showing three GFAP + GS + GLAST + DAPI + cells from a control mouse. ( D ) Histrogram showing no difference in the number of astrocytes or glutamate transporter GLT-1 positive astrocytes (GFAP + GS + GLT-1 + cells) between the control and hyperoxia experimental groups at P8. However, hyperoxia reduced the number of astrocytes expressing GLAST. ( E ) Data indicating that hyperoxia decreases the percentage of GLAST-expressing astrocytes without changing the number of astrocytes expressing GLT-1 at P8. ( F, G ) Immuno-labeling with antibodies for GFAP, GS, GLT-1 and DAPI to analyze astrocyte numbers and the amount of astrocytes expressing GLT-1 in WT mice at P12. Arrowheads indicate cells positive for each respective marker and all four in merged image. ( H , I ) No change in the total number of GFAP + GS + GLAST + cells or GFAP + GS + GLT-1 + cells was observed at P12. ( J, K ) Densitometric analysis of GLAST and GLT-1 western blots at P8 and P12. Hyperoxia caused a decrease in GLAST protein levels immediately following exposure ( J, ). After 4 days of room air recovery ( K ), WM GLAST protein expression returned to the level of controls. No changes in GLT-1 levels were observed in hyperoxia exposed animals. Values represent standardized mean ratios for the protein of interest (POI) and β-actin. ( L ) Representative western blots of GLAST, GLT-1 and β-actin protein expression using micro-dissected WM tissue from P8 and P12 animals in each experimental group. For each group and time point, n = 3 – 5 brains. An unpaired t-test comparing control vs. hyperoxia, where *P

    Article Snippet: The antibodies used were as follows: monoclonal mouse MBP 1:1000 (Covance VA), polyclonal mouse GFAP 1:1000 (Sigma-Aldrich, St. Louis MO), polyclonal rabbit GLAST/EAAT1 1:250 (Abcam, Cambridge MA), polyclonal guinea pig GLT-1/EAAT2 1:250 (Millipore/Chemicon, Temecula CA), monoclonal mouse β-actin 1:1,250 (Millipore/Chemicon, Temecula CA).

    Techniques: Expressing, Immunofluorescence, Labeling, Staining, Mouse Assay, Marker, Immunolabeling, Western Blot

    Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and β-actin as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HLA-B35 Upregulates Endothelin-1 and Downregulates Endothelial Nitric Oxide Synthase via Endoplasmic Reticulum Stress Response in Endothelial Cells

    doi: 10.4049/jimmunol.0903188

    Figure Lengend Snippet: Expression of HSPs in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h. Quantitative RT-PCR was performed with SYBR Green and β-actin as an internal control. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).

    Article Snippet: Abs used were as followed: goat ET-1 Ab (Santa Cruz Biotechnology, Santa Clara, CA) at a 1:500 dilution; endothelial NO synthase (eNOS) Ab (Santa Cruz Biotechnology) at a 1:1000 dilution; heat shock protein 70 (HSP70) and HSP40 Ab (Cell Signaling, Danvers, MA) at 1:1000 dilution; H chain binding protein (BiP) and C/Ebp homologous protein (CHOP) Ab (Abcam, Cambridge, MA) at 1:1000 dilution; monoclonal β-actin Ab (Sigma-Aldrich) at 1:5000 diluition.

    Techniques: Expressing, Transduction, Isolation, Quantitative RT-PCR, SYBR Green Assay

    Expression of ET-1 and eNOS protein levels in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 or HLA-B8 Ads. ECs were transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h; 20 μg of total cellular proteins were separated via 15% SDS-PAGE for ET-1 (7.5% for eNOS) and transferred to a nitrocellulose membrane. The blots were probed overnight with primary Abs at 4°C. As a control for equal protein loading, membranes were stripped and reprobed for β-actin using a mAb to β-actin. Representative blots of at least three experiments are shown.

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HLA-B35 Upregulates Endothelin-1 and Downregulates Endothelial Nitric Oxide Synthase via Endoplasmic Reticulum Stress Response in Endothelial Cells

    doi: 10.4049/jimmunol.0903188

    Figure Lengend Snippet: Expression of ET-1 and eNOS protein levels in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 or HLA-B8 Ads. ECs were transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad-B35/GFP or Ad-B8/GFP for 48 h; 20 μg of total cellular proteins were separated via 15% SDS-PAGE for ET-1 (7.5% for eNOS) and transferred to a nitrocellulose membrane. The blots were probed overnight with primary Abs at 4°C. As a control for equal protein loading, membranes were stripped and reprobed for β-actin using a mAb to β-actin. Representative blots of at least three experiments are shown.

    Article Snippet: Abs used were as followed: goat ET-1 Ab (Santa Cruz Biotechnology, Santa Clara, CA) at a 1:500 dilution; endothelial NO synthase (eNOS) Ab (Santa Cruz Biotechnology) at a 1:1000 dilution; heat shock protein 70 (HSP70) and HSP40 Ab (Cell Signaling, Danvers, MA) at 1:1000 dilution; H chain binding protein (BiP) and C/Ebp homologous protein (CHOP) Ab (Abcam, Cambridge, MA) at 1:1000 dilution; monoclonal β-actin Ab (Sigma-Aldrich) at 1:5000 diluition.

    Techniques: Expressing, Transduction, SDS Page

    Expression of UPR genes in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10–15 (ECV304) or 5–10 (HUVECs and HDMECs) MOI of Ad-B35/GFP (Ad-B8/GFP) after 48 h. Quantitative RT-PCR was performed with SYBR Green and β-actin as an internal control. * p = 0.05 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HLA-B35 Upregulates Endothelin-1 and Downregulates Endothelial Nitric Oxide Synthase via Endoplasmic Reticulum Stress Response in Endothelial Cells

    doi: 10.4049/jimmunol.0903188

    Figure Lengend Snippet: Expression of UPR genes in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. Total RNA was isolated from ECs transduced with 10–15 (ECV304) or 5–10 (HUVECs and HDMECs) MOI of Ad-B35/GFP (Ad-B8/GFP) after 48 h. Quantitative RT-PCR was performed with SYBR Green and β-actin as an internal control. * p = 0.05 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).

    Article Snippet: Abs used were as followed: goat ET-1 Ab (Santa Cruz Biotechnology, Santa Clara, CA) at a 1:500 dilution; endothelial NO synthase (eNOS) Ab (Santa Cruz Biotechnology) at a 1:1000 dilution; heat shock protein 70 (HSP70) and HSP40 Ab (Cell Signaling, Danvers, MA) at 1:1000 dilution; H chain binding protein (BiP) and C/Ebp homologous protein (CHOP) Ab (Abcam, Cambridge, MA) at 1:1000 dilution; monoclonal β-actin Ab (Sigma-Aldrich) at 1:5000 diluition.

    Techniques: Expressing, Transduction, Isolation, Quantitative RT-PCR, SYBR Green Assay

    Expression of HSP70 and HSP40 protein levels in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. The 30 μg total cellular proteins were separated via 10% SDS-PAGE and transferred to a nitrocellulose membrane. The blots were probed overnight with 1:1000 dilutions of primary Abs in 3% milk/Tween-Tris buffered saline at 4°C. As a control for equal protein loading, membranes were stripped and reprobed for β-actin using a mAb to β-actin. Representative blots of at least three experiments are shown.

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HLA-B35 Upregulates Endothelin-1 and Downregulates Endothelial Nitric Oxide Synthase via Endoplasmic Reticulum Stress Response in Endothelial Cells

    doi: 10.4049/jimmunol.0903188

    Figure Lengend Snippet: Expression of HSP70 and HSP40 protein levels in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. The 30 μg total cellular proteins were separated via 10% SDS-PAGE and transferred to a nitrocellulose membrane. The blots were probed overnight with 1:1000 dilutions of primary Abs in 3% milk/Tween-Tris buffered saline at 4°C. As a control for equal protein loading, membranes were stripped and reprobed for β-actin using a mAb to β-actin. Representative blots of at least three experiments are shown.

    Article Snippet: Abs used were as followed: goat ET-1 Ab (Santa Cruz Biotechnology, Santa Clara, CA) at a 1:500 dilution; endothelial NO synthase (eNOS) Ab (Santa Cruz Biotechnology) at a 1:1000 dilution; heat shock protein 70 (HSP70) and HSP40 Ab (Cell Signaling, Danvers, MA) at 1:1000 dilution; H chain binding protein (BiP) and C/Ebp homologous protein (CHOP) Ab (Abcam, Cambridge, MA) at 1:1000 dilution; monoclonal β-actin Ab (Sigma-Aldrich) at 1:5000 diluition.

    Techniques: Expressing, Transduction, SDS Page

    Expression of BiP and CHOP protein levels in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. The 30 μg total cellular proteins were separated via 10% SDS-PAGE and transferred to a nitrocellulose membrane. The blots were probed overnight with 1:1000 dilutions of primary Abs in 3% milk/Tween-Tris buffered saline at 4°C. As a control for equal protein loading, membranes were stripped and reprobed for β-actin using a mAb to β-actin. Representative blots of at least three experiments are shown.

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HLA-B35 Upregulates Endothelin-1 and Downregulates Endothelial Nitric Oxide Synthase via Endoplasmic Reticulum Stress Response in Endothelial Cells

    doi: 10.4049/jimmunol.0903188

    Figure Lengend Snippet: Expression of BiP and CHOP protein levels in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells transduced with HLA-B35 (HLA-B8) Ads. The 30 μg total cellular proteins were separated via 10% SDS-PAGE and transferred to a nitrocellulose membrane. The blots were probed overnight with 1:1000 dilutions of primary Abs in 3% milk/Tween-Tris buffered saline at 4°C. As a control for equal protein loading, membranes were stripped and reprobed for β-actin using a mAb to β-actin. Representative blots of at least three experiments are shown.

    Article Snippet: Abs used were as followed: goat ET-1 Ab (Santa Cruz Biotechnology, Santa Clara, CA) at a 1:500 dilution; endothelial NO synthase (eNOS) Ab (Santa Cruz Biotechnology) at a 1:1000 dilution; heat shock protein 70 (HSP70) and HSP40 Ab (Cell Signaling, Danvers, MA) at 1:1000 dilution; H chain binding protein (BiP) and C/Ebp homologous protein (CHOP) Ab (Abcam, Cambridge, MA) at 1:1000 dilution; monoclonal β-actin Ab (Sigma-Aldrich) at 1:5000 diluition.

    Techniques: Expressing, Transduction, SDS Page

    Upregulation of PPET1 and dowregulation of eNOS mRNA after HLA-B35 (and HLA-B8) over-expression in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells. In the top panel , we show the dose of Ad that expresses HLA-B35 at the physiological levels corresponding to those found in HLA-B35+ individual (gray column) in ECV304 ( A ), HUVECs ( B ), and HDMECs ( C ). Confluent dishes of ECs were transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad encoding HLA-B35 and HLA-B8 for 48 h. Total RNA was extracted and mRNA levels of PPET1 ( middle row ) and eNOS ( bottom row ) were quantified by quantitative RT-PCR. Expression of the housekeeping gene β-actin served as an internal positive control in each assay performed. After measurement of the relative fluorescence intensity for each sample, the amount of each mRNA transcript was expressed as a threshold cycle value. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HLA-B35 Upregulates Endothelin-1 and Downregulates Endothelial Nitric Oxide Synthase via Endoplasmic Reticulum Stress Response in Endothelial Cells

    doi: 10.4049/jimmunol.0903188

    Figure Lengend Snippet: Upregulation of PPET1 and dowregulation of eNOS mRNA after HLA-B35 (and HLA-B8) over-expression in ECV304 ( A ), HUVEC ( B ), and HDMEC ( C ) cells. In the top panel , we show the dose of Ad that expresses HLA-B35 at the physiological levels corresponding to those found in HLA-B35+ individual (gray column) in ECV304 ( A ), HUVECs ( B ), and HDMECs ( C ). Confluent dishes of ECs were transduced with 10 and 15 MOI (ECV304) or 5 and 10 MOI (HUVECs and HDMECs) of Ad encoding HLA-B35 and HLA-B8 for 48 h. Total RNA was extracted and mRNA levels of PPET1 ( middle row ) and eNOS ( bottom row ) were quantified by quantitative RT-PCR. Expression of the housekeeping gene β-actin served as an internal positive control in each assay performed. After measurement of the relative fluorescence intensity for each sample, the amount of each mRNA transcript was expressed as a threshold cycle value. * p = 0.05; ** p = 0.001 Ad-B35/GFP (black column) versus Ad-B8/GFP (white column).

    Article Snippet: Abs used were as followed: goat ET-1 Ab (Santa Cruz Biotechnology, Santa Clara, CA) at a 1:500 dilution; endothelial NO synthase (eNOS) Ab (Santa Cruz Biotechnology) at a 1:1000 dilution; heat shock protein 70 (HSP70) and HSP40 Ab (Cell Signaling, Danvers, MA) at 1:1000 dilution; H chain binding protein (BiP) and C/Ebp homologous protein (CHOP) Ab (Abcam, Cambridge, MA) at 1:1000 dilution; monoclonal β-actin Ab (Sigma-Aldrich) at 1:5000 diluition.

    Techniques: Over Expression, Transduction, Quantitative RT-PCR, Expressing, Positive Control, Fluorescence

    Upregulation of ET-1 and HSPA1A in ECV304 ( A ) and HDMEC ( B ) cells after TG treatment, total RNA was isolated from ECV304 and HDMEC cells and treated with TG for 24 h (1–5– 10 pM). Quantitative RT-PCR was performed with SYBR Green and β-actin as an internal control. The 30 μg total cellular proteins were separated via SDS-PAGE and transferred to a nitrocellulose membrane. The blots were probed overnight with primary Abs at 4°C. As a control for equal protein loading, membranes were stripped and reprobed for β-actin using a mAb to β-actin. * p = 0.05 cells after TG treatment versus untreated cells.

    Journal: Journal of immunology (Baltimore, Md. : 1950)

    Article Title: HLA-B35 Upregulates Endothelin-1 and Downregulates Endothelial Nitric Oxide Synthase via Endoplasmic Reticulum Stress Response in Endothelial Cells

    doi: 10.4049/jimmunol.0903188

    Figure Lengend Snippet: Upregulation of ET-1 and HSPA1A in ECV304 ( A ) and HDMEC ( B ) cells after TG treatment, total RNA was isolated from ECV304 and HDMEC cells and treated with TG for 24 h (1–5– 10 pM). Quantitative RT-PCR was performed with SYBR Green and β-actin as an internal control. The 30 μg total cellular proteins were separated via SDS-PAGE and transferred to a nitrocellulose membrane. The blots were probed overnight with primary Abs at 4°C. As a control for equal protein loading, membranes were stripped and reprobed for β-actin using a mAb to β-actin. * p = 0.05 cells after TG treatment versus untreated cells.

    Article Snippet: Abs used were as followed: goat ET-1 Ab (Santa Cruz Biotechnology, Santa Clara, CA) at a 1:500 dilution; endothelial NO synthase (eNOS) Ab (Santa Cruz Biotechnology) at a 1:1000 dilution; heat shock protein 70 (HSP70) and HSP40 Ab (Cell Signaling, Danvers, MA) at 1:1000 dilution; H chain binding protein (BiP) and C/Ebp homologous protein (CHOP) Ab (Abcam, Cambridge, MA) at 1:1000 dilution; monoclonal β-actin Ab (Sigma-Aldrich) at 1:5000 diluition.

    Techniques: Isolation, Quantitative RT-PCR, SYBR Green Assay, SDS Page

    CSPα HPD-AAA increases BK channel levels in stably-transfected, BK channel expressing CAD cells. A schematic of wild-type CSPα, CSPα HPD-AAA , wild-type Hsp40 and Hsp40 HPD-AAA is shown at the top of the Figure, in which the J domain and the cysteine string regions are indicated. (A) Western blot analysis of BKα subunit expression in BK stable, CAD cells transiently transfected with either myc-tagged CSPα or CSPα HPD-AAA (0.75 μg cDNA each), or 1 μg cDNA encoding either myc-tagged Hsp40 or Hsp40 HPD-AAA . pCMV plasmid (1 μg cDNA) was used as a transfection control. 48 h post-transfection, transfected cells were harvested and 30 μg of cell lysate were separated by SDS-PAGE, and probed with either an anti-BKα subunit antibody (upper) or an anti-myc antibody (middle). Detection of endogenous β-actin (lower) was used to verify similar sample loading. The BKα subunit data shown in the upper image of this panel were selected from a full-length western blot, which is displayed in Supplementary Figure 2A . The histogram (panel B) quantifies the relative changes in cellular BKα subunit expression in the presence of WT and HPD-AAA mutant forms of CSPα and Hsp40. (Panel C) shows a series of representative western blots of proteins reported to undergo palmitoylation. Soluble lysates were prepared from BK stable CAD cells transiently transfected with either wild-type CSPα or the HPD-AAA mutant, as indicated at the top of the panel. eGFP was used as a transfection control. Samples in the left hand column (denoted by the minus sign) are lysates from non-transfected cells. Detection of β-actin was used as a loading control. Results are representative of 4 independent experiments that all provided qualitatively similar data. Statistically significant differences between values were determined by -ANOVA, * p

    Journal: Scientific Reports

    Article Title: The Large Conductance, Calcium-activated K+ (BK) Channel is regulated by Cysteine String Protein

    doi: 10.1038/srep02447

    Figure Lengend Snippet: CSPα HPD-AAA increases BK channel levels in stably-transfected, BK channel expressing CAD cells. A schematic of wild-type CSPα, CSPα HPD-AAA , wild-type Hsp40 and Hsp40 HPD-AAA is shown at the top of the Figure, in which the J domain and the cysteine string regions are indicated. (A) Western blot analysis of BKα subunit expression in BK stable, CAD cells transiently transfected with either myc-tagged CSPα or CSPα HPD-AAA (0.75 μg cDNA each), or 1 μg cDNA encoding either myc-tagged Hsp40 or Hsp40 HPD-AAA . pCMV plasmid (1 μg cDNA) was used as a transfection control. 48 h post-transfection, transfected cells were harvested and 30 μg of cell lysate were separated by SDS-PAGE, and probed with either an anti-BKα subunit antibody (upper) or an anti-myc antibody (middle). Detection of endogenous β-actin (lower) was used to verify similar sample loading. The BKα subunit data shown in the upper image of this panel were selected from a full-length western blot, which is displayed in Supplementary Figure 2A . The histogram (panel B) quantifies the relative changes in cellular BKα subunit expression in the presence of WT and HPD-AAA mutant forms of CSPα and Hsp40. (Panel C) shows a series of representative western blots of proteins reported to undergo palmitoylation. Soluble lysates were prepared from BK stable CAD cells transiently transfected with either wild-type CSPα or the HPD-AAA mutant, as indicated at the top of the panel. eGFP was used as a transfection control. Samples in the left hand column (denoted by the minus sign) are lysates from non-transfected cells. Detection of β-actin was used as a loading control. Results are representative of 4 independent experiments that all provided qualitatively similar data. Statistically significant differences between values were determined by -ANOVA, * p

    Article Snippet: Primary antibodies were obtained as follows: BK polyclonal and Cav 2.2 polyclonal (Millipore), BK monoclonal, c-myc monoclonal and flotillin monoclonal (BD Biosciences), Kv 1.1 monoclonal and Kv 1.2 monoclonal (NeuroMab), SNAP25 monoclonal (Sternberger monoclonals), syntaxin monoclonal, GAP43 monoclonal, and β-actin monoclonal (Sigma-Aldrich).

    Techniques: Stable Transfection, Transfection, Expressing, Western Blot, Plasmid Preparation, SDS Page, Mutagenesis

    CSPα HPD-AAA increases cell surface expression of BK channel stably-transfected CAD cells. (A) CAD cells stably-expressing BK channels were transiently-transfected with 0.75 μg CSPα, CSPα HPD-AAA and pCMV (negative control). 48 h post-transfection, the cells were labeled for 30 min at 4°C with bath applied Biotin. Following lysis, 1 mg of soluble protein lysate was subjected to overnight streptavidin pull-down at 4°C. Proteins isolated by streptavidin pull down (panel A, left) and 30 μg of soluble cellular lysate (panel A, right) were analyzed by Western Blot with an anti-BKα subunit antibody. β-actin (lower) is shown as a sample loading control. The BKα subunit data shown in the upper image of panel A were selected from a full-length western blot, which is displayed in Supplementary Figure 2B . The histogram in (panel B) quantifies the relative changes in cellular BK channel expression in the presence of WT and various mutant forms of CSPα (i.e. HPD-AAA, CSPα L115R and CSPα Δ116 ), as depicted in panel C. Data are presented as mean ± SE; the number of cells analyzed under each condition is indicated in parentheses. Statistically significant differences were determined using a one-way ANOVA and a Dunnett post-hoc test (vs. GFP alone); * (p

    Journal: Scientific Reports

    Article Title: The Large Conductance, Calcium-activated K+ (BK) Channel is regulated by Cysteine String Protein

    doi: 10.1038/srep02447

    Figure Lengend Snippet: CSPα HPD-AAA increases cell surface expression of BK channel stably-transfected CAD cells. (A) CAD cells stably-expressing BK channels were transiently-transfected with 0.75 μg CSPα, CSPα HPD-AAA and pCMV (negative control). 48 h post-transfection, the cells were labeled for 30 min at 4°C with bath applied Biotin. Following lysis, 1 mg of soluble protein lysate was subjected to overnight streptavidin pull-down at 4°C. Proteins isolated by streptavidin pull down (panel A, left) and 30 μg of soluble cellular lysate (panel A, right) were analyzed by Western Blot with an anti-BKα subunit antibody. β-actin (lower) is shown as a sample loading control. The BKα subunit data shown in the upper image of panel A were selected from a full-length western blot, which is displayed in Supplementary Figure 2B . The histogram in (panel B) quantifies the relative changes in cellular BK channel expression in the presence of WT and various mutant forms of CSPα (i.e. HPD-AAA, CSPα L115R and CSPα Δ116 ), as depicted in panel C. Data are presented as mean ± SE; the number of cells analyzed under each condition is indicated in parentheses. Statistically significant differences were determined using a one-way ANOVA and a Dunnett post-hoc test (vs. GFP alone); * (p

    Article Snippet: Primary antibodies were obtained as follows: BK polyclonal and Cav 2.2 polyclonal (Millipore), BK monoclonal, c-myc monoclonal and flotillin monoclonal (BD Biosciences), Kv 1.1 monoclonal and Kv 1.2 monoclonal (NeuroMab), SNAP25 monoclonal (Sternberger monoclonals), syntaxin monoclonal, GAP43 monoclonal, and β-actin monoclonal (Sigma-Aldrich).

    Techniques: Expressing, Stable Transfection, Transfection, Negative Control, Labeling, Lysis, Isolation, Western Blot, Mutagenesis

    Comparison of protein levels for BK, Ca v 2.2, K v 1.1 and K v 1.2 channels in whole brain tissue from CSPα wild-type, heterozygous and null mice. (A) Representative western blot data of the pore-forming α subunits of BK channel, Ca v 2.2 channel, K v 1.1 and K v 1.2 channels detected in synaptosome-enriched membrane fractions prepared from whole brain (age P23–27). The total protein loaded per lane was 40 μg; detection of β-actin on the same blots was used to verify equal loading amongst the various lanes. The data shown in panel A were selected from full-length western blot images, which are displayed in Supplementary Figure 1 . (B) Histogram showing average data for BK, Ca v 2.2, K v 1.1 and K v 1.2 channel protein in the wild-type, heterozygous and null brain samples quantified by camera-based detection of emitted chemiluminescence. To perform quantification, the ratio of detected channel protein to β-actin for a given sample was calculated for all three genetic backgrounds. Channel density data for the heterozygote and null tissues were then normalized to the wild-type tissue by dividing all calculated ratios by the wild-type ratio for a given channel species. (C) Histogram showing BK channel expression detected in aorta from CSPα heterozygous and null mice relative to wild-type mice. Quantification of BKα subunit detection was performed as described in panel B. Averaged Western blot data were derived from 5–6 animals (panel B) and 3–4 animals (panel C) of each genetic background (2–3 litters). * indicates a statistically significant difference from the heterozygote and wild-type values, as determined by one-way ANOVA and a Tukey's post-hoc test; p

    Journal: Scientific Reports

    Article Title: The Large Conductance, Calcium-activated K+ (BK) Channel is regulated by Cysteine String Protein

    doi: 10.1038/srep02447

    Figure Lengend Snippet: Comparison of protein levels for BK, Ca v 2.2, K v 1.1 and K v 1.2 channels in whole brain tissue from CSPα wild-type, heterozygous and null mice. (A) Representative western blot data of the pore-forming α subunits of BK channel, Ca v 2.2 channel, K v 1.1 and K v 1.2 channels detected in synaptosome-enriched membrane fractions prepared from whole brain (age P23–27). The total protein loaded per lane was 40 μg; detection of β-actin on the same blots was used to verify equal loading amongst the various lanes. The data shown in panel A were selected from full-length western blot images, which are displayed in Supplementary Figure 1 . (B) Histogram showing average data for BK, Ca v 2.2, K v 1.1 and K v 1.2 channel protein in the wild-type, heterozygous and null brain samples quantified by camera-based detection of emitted chemiluminescence. To perform quantification, the ratio of detected channel protein to β-actin for a given sample was calculated for all three genetic backgrounds. Channel density data for the heterozygote and null tissues were then normalized to the wild-type tissue by dividing all calculated ratios by the wild-type ratio for a given channel species. (C) Histogram showing BK channel expression detected in aorta from CSPα heterozygous and null mice relative to wild-type mice. Quantification of BKα subunit detection was performed as described in panel B. Averaged Western blot data were derived from 5–6 animals (panel B) and 3–4 animals (panel C) of each genetic background (2–3 litters). * indicates a statistically significant difference from the heterozygote and wild-type values, as determined by one-way ANOVA and a Tukey's post-hoc test; p

    Article Snippet: Primary antibodies were obtained as follows: BK polyclonal and Cav 2.2 polyclonal (Millipore), BK monoclonal, c-myc monoclonal and flotillin monoclonal (BD Biosciences), Kv 1.1 monoclonal and Kv 1.2 monoclonal (NeuroMab), SNAP25 monoclonal (Sternberger monoclonals), syntaxin monoclonal, GAP43 monoclonal, and β-actin monoclonal (Sigma-Aldrich).

    Techniques: Mouse Assay, Western Blot, Expressing, Derivative Assay

    Mechanism of NVP-AEW541 drug action. A: Protein expression of IGF-1R in tested human biliary tract cancer cell lines was determined by immunoblot; B: p-IGF-1R, IGF-1R, p-AKT, AKT, p-p42/44, p42/44, p-Stat-3, Stat-3, and Bcl-xL protein levels were examined by immunoblot for selected cell lines EGI-1 and Mz-ChA-1. After 24 h of starvation, cell lines EGI-1 and Mz-ChA-1 were treated with NVP-AEW541 (12 h prior to lysis) and stimulated with ligand IGF-1 (30 min prior to lysis). β-actin served as loading control in all experiments. Densitometry was performed to analyze results which are shown relative to lane 2 as standard.

    Journal: World Journal of Gastroenterology : WJG

    Article Title: Treatment of biliary tract cancer with NVP-AEW541: Mechanisms of action and resistance

    doi: 10.3748/wjg.v16.i2.156

    Figure Lengend Snippet: Mechanism of NVP-AEW541 drug action. A: Protein expression of IGF-1R in tested human biliary tract cancer cell lines was determined by immunoblot; B: p-IGF-1R, IGF-1R, p-AKT, AKT, p-p42/44, p42/44, p-Stat-3, Stat-3, and Bcl-xL protein levels were examined by immunoblot for selected cell lines EGI-1 and Mz-ChA-1. After 24 h of starvation, cell lines EGI-1 and Mz-ChA-1 were treated with NVP-AEW541 (12 h prior to lysis) and stimulated with ligand IGF-1 (30 min prior to lysis). β-actin served as loading control in all experiments. Densitometry was performed to analyze results which are shown relative to lane 2 as standard.

    Article Snippet: Monoclonal (mc) β-actin antibody was purchased from Sigma (Sigma-Aldrich Chemie GmbH Munich, Germany), polyclonal IGF-1Rβantibody from Santa Cruz (Santa Cruz Biotechnology Inc., Santa Cruz, USA), mc p-IGF-1R, mc p-p42/44 (p-Erk1/2, p-MAPK), mc p42/44, mc p-AKT, mc AKT, mc p-Stat3, mc Stat3 and mc Bcl-xL antibodies were all from Cell Signaling (Cell Signaling Technology, Beverly, USA).

    Techniques: Expressing, Lysis

    miR-27a knockdown promotes autophagy in CRC cells. ( a ) Morphological features of HCT116 CRTL, miR27a_KD and miR27a_OE cells were evaluated by hematoxylin and eosin staining; the arrows point out some remarkable phenotypic characteristics (Scale bar, 20 mm). ( b ) Dose-dependent induction of autophagy in HCT116 CRTL, miR27a_KD and miR27a_OE cells exposed to the lysosomotropic drug chloroquine (CQ). Western blot analysis of the LC3-II mature form, an autophagic marker, is reported along with its relative quantification in the histogram. β -Actin was used as loading control. ( c ) Time-course of autophagy induction in HCT116 CRTL, miR27a_KD and miR27a_OE cells upon MTX treatment at 1 μ M. Immunoblot of LC-3-II was used as a marker. All data are representative of three independent experiments and error bars represent S.D. of technical replicates (mean±S.D.)

    Journal: Cell Death & Disease

    Article Title: The miR-27a-calreticulin axis affects drug-induced immunogenic cell death in human colorectal cancer cells

    doi: 10.1038/cddis.2016.29

    Figure Lengend Snippet: miR-27a knockdown promotes autophagy in CRC cells. ( a ) Morphological features of HCT116 CRTL, miR27a_KD and miR27a_OE cells were evaluated by hematoxylin and eosin staining; the arrows point out some remarkable phenotypic characteristics (Scale bar, 20 mm). ( b ) Dose-dependent induction of autophagy in HCT116 CRTL, miR27a_KD and miR27a_OE cells exposed to the lysosomotropic drug chloroquine (CQ). Western blot analysis of the LC3-II mature form, an autophagic marker, is reported along with its relative quantification in the histogram. β -Actin was used as loading control. ( c ) Time-course of autophagy induction in HCT116 CRTL, miR27a_KD and miR27a_OE cells upon MTX treatment at 1 μ M. Immunoblot of LC-3-II was used as a marker. All data are representative of three independent experiments and error bars represent S.D. of technical replicates (mean±S.D.)

    Article Snippet: Antibodies against calreticulin (ab2907), HMGB1 (ab79823) were from Abcam (Cambridge, MA, USA); GRP78 (sc-13968), PERK (sc-377400), p-PERK (sc-32577), Caspase-3 (sc-7148), anti-mouse (sc-2031), anti rabbit (sc-2004) from Santa Cruz Biotechnology (Dallas, TX, USA), LC3 (GTX 82986) from Genetex (Irvine, CA, USA); β -actin (F-3022) from Sigma-Aldrich (Milan, Italy); E-cadherin (BD 610405) from BD transduction (BD Biosciences, San Jose, CA, USA); AKT (Y058027) and p-AKT (Y080084) from abm (Richmond, BC, Canada); eIF2a (#9722), p-eIF2a(#3597) and PARP (#9542 S) from Cell Signaling (Danvers, MA, USA).

    Techniques: Staining, Western Blot, Marker

    miR-27a counteracts mitoxantrone-induced ICD through the same UPR pathway. ( a ) Immunoblot analysis of PERK, p-PERK, eIF2 α , p-eIF2 α and GRP78 in time-course experiments of HCT116 CRTL, miR27a_KD and miR27a_OE cells treated with 1 μ M MTX; phosphorylation was referred to equivalent amounts of the non-phosphorylated forms of the proteins in all cells and then to β -actin used as a loading control. Quantification of the bands in basal and in the kinetic conditions is reported. ( b ) CRT cell surface expression in HCT116 CRTL, miR27a_KD and miR27a_OE cells untreated or treated for 12 h with 20 mM LY-294002, alone or in combination with 1 μ M MTX for the last 6 h. Densitometric analysis was carried out after normalization to E-cadherin. * P ⩽0.05; ** P ⩽0.01 (two-tailed Student's t -test) versus HCT116 CRTL cells; # P ⩽0.05; ## P ⩽0.01 (two-tailed Student's t -test) versus MTX-untreated cells. The values are representative of five experiments

    Journal: Cell Death & Disease

    Article Title: The miR-27a-calreticulin axis affects drug-induced immunogenic cell death in human colorectal cancer cells

    doi: 10.1038/cddis.2016.29

    Figure Lengend Snippet: miR-27a counteracts mitoxantrone-induced ICD through the same UPR pathway. ( a ) Immunoblot analysis of PERK, p-PERK, eIF2 α , p-eIF2 α and GRP78 in time-course experiments of HCT116 CRTL, miR27a_KD and miR27a_OE cells treated with 1 μ M MTX; phosphorylation was referred to equivalent amounts of the non-phosphorylated forms of the proteins in all cells and then to β -actin used as a loading control. Quantification of the bands in basal and in the kinetic conditions is reported. ( b ) CRT cell surface expression in HCT116 CRTL, miR27a_KD and miR27a_OE cells untreated or treated for 12 h with 20 mM LY-294002, alone or in combination with 1 μ M MTX for the last 6 h. Densitometric analysis was carried out after normalization to E-cadherin. * P ⩽0.05; ** P ⩽0.01 (two-tailed Student's t -test) versus HCT116 CRTL cells; # P ⩽0.05; ## P ⩽0.01 (two-tailed Student's t -test) versus MTX-untreated cells. The values are representative of five experiments

    Article Snippet: Antibodies against calreticulin (ab2907), HMGB1 (ab79823) were from Abcam (Cambridge, MA, USA); GRP78 (sc-13968), PERK (sc-377400), p-PERK (sc-32577), Caspase-3 (sc-7148), anti-mouse (sc-2031), anti rabbit (sc-2004) from Santa Cruz Biotechnology (Dallas, TX, USA), LC3 (GTX 82986) from Genetex (Irvine, CA, USA); β -actin (F-3022) from Sigma-Aldrich (Milan, Italy); E-cadherin (BD 610405) from BD transduction (BD Biosciences, San Jose, CA, USA); AKT (Y058027) and p-AKT (Y080084) from abm (Richmond, BC, Canada); eIF2a (#9722), p-eIF2a(#3597) and PARP (#9542 S) from Cell Signaling (Danvers, MA, USA).

    Techniques: Expressing, Two Tailed Test

    miR-27a impairs the kinetics of apoptosis execution in drug-induced ICD. ( a ) Western blot analysis of the apoptosis markers, PARP and caspase 3, in time-course experiments of HCT116 CRTL, miR27a_KD and miR27a_OE cells treated or not with mitoxantrone (1 μ M). β -Actin was used as loading control and quantification of the cleaved protein forms is reported in ( b ). ( c ) Flow cytometry analysis of pre-apoptotic (annexin V-PE + and 7-AAD - ) and apoptotic (annexin V-PE + and 7-AAD + ) HCT116 CRTL, miR27a_KD and miR27a_OE cells treated with OXP (100 μ M) in kinetics experiments. One representative experiment out of three is shown

    Journal: Cell Death & Disease

    Article Title: The miR-27a-calreticulin axis affects drug-induced immunogenic cell death in human colorectal cancer cells

    doi: 10.1038/cddis.2016.29

    Figure Lengend Snippet: miR-27a impairs the kinetics of apoptosis execution in drug-induced ICD. ( a ) Western blot analysis of the apoptosis markers, PARP and caspase 3, in time-course experiments of HCT116 CRTL, miR27a_KD and miR27a_OE cells treated or not with mitoxantrone (1 μ M). β -Actin was used as loading control and quantification of the cleaved protein forms is reported in ( b ). ( c ) Flow cytometry analysis of pre-apoptotic (annexin V-PE + and 7-AAD - ) and apoptotic (annexin V-PE + and 7-AAD + ) HCT116 CRTL, miR27a_KD and miR27a_OE cells treated with OXP (100 μ M) in kinetics experiments. One representative experiment out of three is shown

    Article Snippet: Antibodies against calreticulin (ab2907), HMGB1 (ab79823) were from Abcam (Cambridge, MA, USA); GRP78 (sc-13968), PERK (sc-377400), p-PERK (sc-32577), Caspase-3 (sc-7148), anti-mouse (sc-2031), anti rabbit (sc-2004) from Santa Cruz Biotechnology (Dallas, TX, USA), LC3 (GTX 82986) from Genetex (Irvine, CA, USA); β -actin (F-3022) from Sigma-Aldrich (Milan, Italy); E-cadherin (BD 610405) from BD transduction (BD Biosciences, San Jose, CA, USA); AKT (Y058027) and p-AKT (Y080084) from abm (Richmond, BC, Canada); eIF2a (#9722), p-eIF2a(#3597) and PARP (#9542 S) from Cell Signaling (Danvers, MA, USA).

    Techniques: Western Blot, Flow Cytometry, Cytometry