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Abcam expression levels antibodies
Expression Levels Antibodies, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Article Title: Acute exercise modifies titin phosphorylation and increases cardiac myofilament stiffness
Article Snippet: .. To determine the expression levels antibodies were used against Phospho-PKCα (phospho-T497, Abcam), (Total-) PKCα (Cell Signaling Technology) and Phospho-Phospholamban (phospho-S16, Badrilla). ..

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  • 95
    Abcam drebrin expression levels
    Stable depletion of endogenous <t>drebrin</t> in tumorigenic UMUC-3 urothelial cancer cells inhibits motility and anchorage-independent growth (A) The generation of UMUC-3/pRS-control and UMUC-3/pRS-shDBN cells has been described in Materials and Methods. Drebrin expression in lysates from parental (P), control- (C) or shRNA drebrin-transfected (shDBN) UMUC-3 cells was detected by immunoblot. (B) Migration of the various UMUC-3 cell lines was performed using transwells as described in detail in Materials and Methods. The experiment is the average of three independent experiments run in duplicates ±SD. ** P
    Drebrin Expression Levels, supplied by Abcam, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/drebrin expression levels/product/Abcam
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    94
    Abcam antinucleolin
    Cleavage of AUF1 during poliovirus, human rhinovirus 14, or human rhinovirus 16 infection. HeLa cells were infected with poliovirus (A) (lanes 3 to 7), human rhinovirus 14 (B) (lanes 3 to 11), or human rhinovirus 16 (C) (lanes 3 to 11), and NP-40 lysates were generated at different times after infection. Lysates from mock-infected cells (M0 and M6.5 or M16, lanes 1 and 2) were generated at 0 hpi or at 6.5 hpi (for poliovirus) or 16 hpi (for human rhinovirus). Lysates were subjected to SDS-PAGE and Western blot analysis using anti-AUF1 rabbit polyclonal antibody and <t>antinucleolin</t> rabbit polyclonal antibody (as a loading control) to visualize proteins. For size comparison, a molecular mass marker was included (left side of the autoradiograph of the gel). The electrophoretic mobilities of endogenous AUF1, cleaved and uncleaved, and nucleolin are indicated by the bracket and arrow, respectively, on the right.
    Antinucleolin, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam gata3 expression levels
    <t>GATA3</t> expression stratified by histologic type and nuclear grade The mean GATA3 protein expression for each category is shown using bar plots. The error bars represent the standard error of the mean; n is number of spots. (A) GATA3 expression was significantly increased in ductal hyperplasia (DH, P
    Gata3 Expression Levels, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Abcam rad18 expression levels
    Knockdown of <t>Rad18</t> decreased GFP-Polκ recruitment at laser-induced sites of damage. A) U2OS cells were transfected with shRad18 or shNC and stable cell lines with a reduced Rad18 level were established. Top panel: western blot to show the level of Rad18 in stable cells. Bottom: U2OS cells-depleted of Rad18 were UV irradiated and cell extracts were separated by SDS-PAGE, and incubated with anti-PCNA antibodies.(B) The indicated stable cells were transfected with GFP-Polκ. 24h later, the cells were micro-irradiated with a UVA laser and kinetic analysis of GFP-Polκ intensity at laser-irradiated sites was performed. Error bars represent standard errors based on 10 independent measurements. C) The proportion of cells with Polκ accumulation was quantified.
    Rad18 Expression Levels, supplied by Abcam, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Stable depletion of endogenous drebrin in tumorigenic UMUC-3 urothelial cancer cells inhibits motility and anchorage-independent growth (A) The generation of UMUC-3/pRS-control and UMUC-3/pRS-shDBN cells has been described in Materials and Methods. Drebrin expression in lysates from parental (P), control- (C) or shRNA drebrin-transfected (shDBN) UMUC-3 cells was detected by immunoblot. (B) Migration of the various UMUC-3 cell lines was performed using transwells as described in detail in Materials and Methods. The experiment is the average of three independent experiments run in duplicates ±SD. ** P

    Journal: Oncotarget

    Article Title: A novel role for drebrin in regulating progranulin bioactivity in bladder cancer

    doi:

    Figure Lengend Snippet: Stable depletion of endogenous drebrin in tumorigenic UMUC-3 urothelial cancer cells inhibits motility and anchorage-independent growth (A) The generation of UMUC-3/pRS-control and UMUC-3/pRS-shDBN cells has been described in Materials and Methods. Drebrin expression in lysates from parental (P), control- (C) or shRNA drebrin-transfected (shDBN) UMUC-3 cells was detected by immunoblot. (B) Migration of the various UMUC-3 cell lines was performed using transwells as described in detail in Materials and Methods. The experiment is the average of three independent experiments run in duplicates ±SD. ** P

    Article Snippet: After selection, pools of drebrin-depleted UMUC-3 cells were tested for drebrin expression levels by immunoblot using anti-drebrin monoclonal antibodies (Abcam).

    Techniques: Expressing, shRNA, Transfection, Migration

    Drebrin is upregulated in bladder cancer tissues (A–H) , Panels of light micrographs depicting the distribution of immunoreactive drebrin in normal bladder (A and B) and various types of urinary cancers as indicated (C–H) Notice that in normal bladder, drebrin is essentially not expressed in the mucosa (Mu, a) but is expressed in the submucosal blood vessels and nerves (arrows and arrowheads, respectively, panel B). Drebrin is expressed at high levels in the epithelial components of all cancers (Ca) studied and often in the tumor vasculature (arrows in panels f and g). Bars = 100 μm. (I) Quantification of the drebrin staining was done using ImageJ software. Various images of normal ( n = 9); Ta, T1 ( n = 10) and T2, T3, T4 ( n = 13) urothelial carcinoma tissues were analyzed. Briefly, the threshold of each image was adjusted in order to show only the specific staining. The representative areas of staining were then quantified and plot using SigmaPlot. (L–J) Drebrin and progranulin expression in frozen high grade urothelial carcinoma tissues was analyzed by immunofluorescence analysis. Arrows (L) indicate some areas of colocalization. Three-dimensional surface plots are indicative of progranulin (M) and drebrin (N) expression levels in the relative fluorescence images.

    Journal: Oncotarget

    Article Title: A novel role for drebrin in regulating progranulin bioactivity in bladder cancer

    doi:

    Figure Lengend Snippet: Drebrin is upregulated in bladder cancer tissues (A–H) , Panels of light micrographs depicting the distribution of immunoreactive drebrin in normal bladder (A and B) and various types of urinary cancers as indicated (C–H) Notice that in normal bladder, drebrin is essentially not expressed in the mucosa (Mu, a) but is expressed in the submucosal blood vessels and nerves (arrows and arrowheads, respectively, panel B). Drebrin is expressed at high levels in the epithelial components of all cancers (Ca) studied and often in the tumor vasculature (arrows in panels f and g). Bars = 100 μm. (I) Quantification of the drebrin staining was done using ImageJ software. Various images of normal ( n = 9); Ta, T1 ( n = 10) and T2, T3, T4 ( n = 13) urothelial carcinoma tissues were analyzed. Briefly, the threshold of each image was adjusted in order to show only the specific staining. The representative areas of staining were then quantified and plot using SigmaPlot. (L–J) Drebrin and progranulin expression in frozen high grade urothelial carcinoma tissues was analyzed by immunofluorescence analysis. Arrows (L) indicate some areas of colocalization. Three-dimensional surface plots are indicative of progranulin (M) and drebrin (N) expression levels in the relative fluorescence images.

    Article Snippet: After selection, pools of drebrin-depleted UMUC-3 cells were tested for drebrin expression levels by immunoblot using anti-drebrin monoclonal antibodies (Abcam).

    Techniques: Staining, Software, Expressing, Immunofluorescence, Fluorescence

    Progranulin coprecipitates with drebrin in 5637 and T24 urothelial cancer cells (A) Serum-starved (SFM) 5637 and (B) T24 cells were stimulated with recombinant progranulin (80 nM) for 5 and 30 min (5′ and 30′). progranulin interaction with drebrin was assesses by coimmmunoprecipitation experiments. 3 mg of lysates from 5637 (A) and T24 (B) cells were immunoprecipitated with anti-progranulin polyclonal antibodies. Unrelated IgG (IgG) was used as control (A) Drebrin was detected by immunoblot using anti-drebrin monoclonal antibodies. Blots are representative of two independent experiments.

    Journal: Oncotarget

    Article Title: A novel role for drebrin in regulating progranulin bioactivity in bladder cancer

    doi:

    Figure Lengend Snippet: Progranulin coprecipitates with drebrin in 5637 and T24 urothelial cancer cells (A) Serum-starved (SFM) 5637 and (B) T24 cells were stimulated with recombinant progranulin (80 nM) for 5 and 30 min (5′ and 30′). progranulin interaction with drebrin was assesses by coimmmunoprecipitation experiments. 3 mg of lysates from 5637 (A) and T24 (B) cells were immunoprecipitated with anti-progranulin polyclonal antibodies. Unrelated IgG (IgG) was used as control (A) Drebrin was detected by immunoblot using anti-drebrin monoclonal antibodies. Blots are representative of two independent experiments.

    Article Snippet: After selection, pools of drebrin-depleted UMUC-3 cells were tested for drebrin expression levels by immunoblot using anti-drebrin monoclonal antibodies (Abcam).

    Techniques: Recombinant, Immunoprecipitation

    Drebrin modulates progranulin-induced motility and signaling of urothelial cancer cells (A and B) 5637 and T24 cells were transiently transfected with vehicle, control oligos or On-Target siGenome pool of drebrin-specific oligos. 48 h post-transfection cells were transferred to SFM or SFM supplemented with progranulin (40 nM) and counted for migration after 18 h. Data are the average of three independent experiments ±SD. * P

    Journal: Oncotarget

    Article Title: A novel role for drebrin in regulating progranulin bioactivity in bladder cancer

    doi:

    Figure Lengend Snippet: Drebrin modulates progranulin-induced motility and signaling of urothelial cancer cells (A and B) 5637 and T24 cells were transiently transfected with vehicle, control oligos or On-Target siGenome pool of drebrin-specific oligos. 48 h post-transfection cells were transferred to SFM or SFM supplemented with progranulin (40 nM) and counted for migration after 18 h. Data are the average of three independent experiments ±SD. * P

    Article Snippet: After selection, pools of drebrin-depleted UMUC-3 cells were tested for drebrin expression levels by immunoblot using anti-drebrin monoclonal antibodies (Abcam).

    Techniques: Transfection, Migration

    Drebrin is critical for progranulin-mediated F-actin remodeling (A) GFP-tagged wild type drebrin construct has been previously described [ 23 ]. (ADF-H) actin-depolymerizing factor homology domain. AB: actin binding domain. AE: adult specific exon. 5637 cells were transiently transfected with the GFP-tagged drebrin construct, serum-starved for 24 h and then stimulated with progranulin (40 nM) for 30 min. F-actin structures were assesses by immunofluorescence analysis as described in Material and Methods using Rhodamine-phalloidin. Pictures are representative of at least 10 independent fields from three independent experiments. An average of 300 cells was examined for each condition. Arrows indicate various F-actin structures. 5637 cells were transiently transfected with control oligos (B) or On-Target siGenome pool of drebrin-specific oligos (Dharmacon) (C) serum-starved for 24 h and stimulated with progranulin (40 nM) for 30 min. Immunofluorescence analysis was performed as described in Material and Methods. F-actin was detected using anti-phalloidin staining. Drebrin levels were analyzed using anti-drebrin monoclonal antibodies. Pictures are representative of at least 10 independent fields from three independent experiments. An average of 300 cells was examined for each condition. Arrows indicate F-actin networks while arrowheads identify cortical actin.

    Journal: Oncotarget

    Article Title: A novel role for drebrin in regulating progranulin bioactivity in bladder cancer

    doi:

    Figure Lengend Snippet: Drebrin is critical for progranulin-mediated F-actin remodeling (A) GFP-tagged wild type drebrin construct has been previously described [ 23 ]. (ADF-H) actin-depolymerizing factor homology domain. AB: actin binding domain. AE: adult specific exon. 5637 cells were transiently transfected with the GFP-tagged drebrin construct, serum-starved for 24 h and then stimulated with progranulin (40 nM) for 30 min. F-actin structures were assesses by immunofluorescence analysis as described in Material and Methods using Rhodamine-phalloidin. Pictures are representative of at least 10 independent fields from three independent experiments. An average of 300 cells was examined for each condition. Arrows indicate various F-actin structures. 5637 cells were transiently transfected with control oligos (B) or On-Target siGenome pool of drebrin-specific oligos (Dharmacon) (C) serum-starved for 24 h and stimulated with progranulin (40 nM) for 30 min. Immunofluorescence analysis was performed as described in Material and Methods. F-actin was detected using anti-phalloidin staining. Drebrin levels were analyzed using anti-drebrin monoclonal antibodies. Pictures are representative of at least 10 independent fields from three independent experiments. An average of 300 cells was examined for each condition. Arrows indicate F-actin networks while arrowheads identify cortical actin.

    Article Snippet: After selection, pools of drebrin-depleted UMUC-3 cells were tested for drebrin expression levels by immunoblot using anti-drebrin monoclonal antibodies (Abcam).

    Techniques: Construct, Binding Assay, Transfection, Immunofluorescence, Staining

    Drebrin regulates tumor formation in vivo (A) Tumor growth plot of mice ( n = 18) injected with UMUC-3/sh-control (shCon) and UMUC-3/sh-drebrin (shDBN) cells at day 52. *** P

    Journal: Oncotarget

    Article Title: A novel role for drebrin in regulating progranulin bioactivity in bladder cancer

    doi:

    Figure Lengend Snippet: Drebrin regulates tumor formation in vivo (A) Tumor growth plot of mice ( n = 18) injected with UMUC-3/sh-control (shCon) and UMUC-3/sh-drebrin (shDBN) cells at day 52. *** P

    Article Snippet: After selection, pools of drebrin-depleted UMUC-3 cells were tested for drebrin expression levels by immunoblot using anti-drebrin monoclonal antibodies (Abcam).

    Techniques: In Vivo, Mouse Assay, Injection

    Progranulin interacts with the F-acting-binding protein drebrin (A) Proteomic identification of drebrin from 5637 cell extract pulled-down with recombinant His-tagged progranulin. Samples were separated by SDS-PAGE, visualized with Coomassie blue staining and processed for mass spectrometry. Bands isolated from gel and analyzed are identified by the arrow. Drebrin identity was confirmed on a local Mascot server against the Swissprot database. (B) Drebrin immunodetection from lysates of various urothelial-carcinoma cell lines (Upper panel). B-actin was used as a loading control (lower panel). The blot is representative of two independent experiments. (C) Representative images of immunofluorescence analysis of drebrin expression in 5637 cells. Arrows show drebrin localization at the membrane. DAPI staining was used to label cell nuclei. (D) Drebrin colocalizes with progranulin after 5 min of stimulation as determined by confocal microscopy. Notice the distinct co-localization of drebrin and progranulin in the Z stacks (yellow staining, bottom right panel). The line-scanned profiles at the bottom of the fluorescence images show the distribution of the fluorescence signals of each channel between the white arrows in the corresponding confocal images. Pictures are representative of at least 10 independent fields from three independent experiments. An average of 300 cells was examined for each condition.

    Journal: Oncotarget

    Article Title: A novel role for drebrin in regulating progranulin bioactivity in bladder cancer

    doi:

    Figure Lengend Snippet: Progranulin interacts with the F-acting-binding protein drebrin (A) Proteomic identification of drebrin from 5637 cell extract pulled-down with recombinant His-tagged progranulin. Samples were separated by SDS-PAGE, visualized with Coomassie blue staining and processed for mass spectrometry. Bands isolated from gel and analyzed are identified by the arrow. Drebrin identity was confirmed on a local Mascot server against the Swissprot database. (B) Drebrin immunodetection from lysates of various urothelial-carcinoma cell lines (Upper panel). B-actin was used as a loading control (lower panel). The blot is representative of two independent experiments. (C) Representative images of immunofluorescence analysis of drebrin expression in 5637 cells. Arrows show drebrin localization at the membrane. DAPI staining was used to label cell nuclei. (D) Drebrin colocalizes with progranulin after 5 min of stimulation as determined by confocal microscopy. Notice the distinct co-localization of drebrin and progranulin in the Z stacks (yellow staining, bottom right panel). The line-scanned profiles at the bottom of the fluorescence images show the distribution of the fluorescence signals of each channel between the white arrows in the corresponding confocal images. Pictures are representative of at least 10 independent fields from three independent experiments. An average of 300 cells was examined for each condition.

    Article Snippet: After selection, pools of drebrin-depleted UMUC-3 cells were tested for drebrin expression levels by immunoblot using anti-drebrin monoclonal antibodies (Abcam).

    Techniques: Binding Assay, Recombinant, SDS Page, Staining, Mass Spectrometry, Isolation, Immunodetection, Immunofluorescence, Expressing, Confocal Microscopy, Fluorescence

    Cleavage of AUF1 during poliovirus, human rhinovirus 14, or human rhinovirus 16 infection. HeLa cells were infected with poliovirus (A) (lanes 3 to 7), human rhinovirus 14 (B) (lanes 3 to 11), or human rhinovirus 16 (C) (lanes 3 to 11), and NP-40 lysates were generated at different times after infection. Lysates from mock-infected cells (M0 and M6.5 or M16, lanes 1 and 2) were generated at 0 hpi or at 6.5 hpi (for poliovirus) or 16 hpi (for human rhinovirus). Lysates were subjected to SDS-PAGE and Western blot analysis using anti-AUF1 rabbit polyclonal antibody and antinucleolin rabbit polyclonal antibody (as a loading control) to visualize proteins. For size comparison, a molecular mass marker was included (left side of the autoradiograph of the gel). The electrophoretic mobilities of endogenous AUF1, cleaved and uncleaved, and nucleolin are indicated by the bracket and arrow, respectively, on the right.

    Journal: mBio

    Article Title: Picornavirus Modification of a Host mRNA Decay Protein

    doi: 10.1128/mBio.00431-12

    Figure Lengend Snippet: Cleavage of AUF1 during poliovirus, human rhinovirus 14, or human rhinovirus 16 infection. HeLa cells were infected with poliovirus (A) (lanes 3 to 7), human rhinovirus 14 (B) (lanes 3 to 11), or human rhinovirus 16 (C) (lanes 3 to 11), and NP-40 lysates were generated at different times after infection. Lysates from mock-infected cells (M0 and M6.5 or M16, lanes 1 and 2) were generated at 0 hpi or at 6.5 hpi (for poliovirus) or 16 hpi (for human rhinovirus). Lysates were subjected to SDS-PAGE and Western blot analysis using anti-AUF1 rabbit polyclonal antibody and antinucleolin rabbit polyclonal antibody (as a loading control) to visualize proteins. For size comparison, a molecular mass marker was included (left side of the autoradiograph of the gel). The electrophoretic mobilities of endogenous AUF1, cleaved and uncleaved, and nucleolin are indicated by the bracket and arrow, respectively, on the right.

    Article Snippet: Cellular extracts were subjected to SDS-PAGE, and proteins were electroblotted to a PVDF membrane that was then probed using anti-AUF1 (Millipore) and antinucleolin (Abcam) antibodies (with expression levels of nucleolin serving as a loading control).

    Techniques: Infection, Generated, SDS Page, Western Blot, Marker, Autoradiography

    Guanidine HCl prevents cleavage and relocalization of AUF1 during poliovirus infection. (A) HeLa cells were mock treated (lanes 1 to 6) or treated with 2 mM guanidine HCl (GuaHCl; lanes 7 to 12) during mock infection (lanes 1 and 7) or poliovirus infection (lanes 2 to 6 and lanes 8 to 12). Lysates were collected at indicated hours postinfection (hpi) and subjected to SDS-PAGE and Western blot analysis using anti-AUF1 and antinucleolin (as a loading control) antibodies to visualize proteins. Electrophoretic mobilities of nucleolin and AUF1 are indicated to the right by an arrow and a bracket, respectively. (B) HeLa cells seeded on coverslips were mock infected or infected with poliovirus and treated with 2 mM guanidine HCl. Cells were fixed at either 0 or 5 hpi, immunostained with anti-AUF1 antibody (in red) and anti-3A antibody (in green), and stained with DAPI (blue) to visualize the nucleus. Proteins were visualized using a Zeiss Axiovert 200 M inverted microscope.

    Journal: mBio

    Article Title: Picornavirus Modification of a Host mRNA Decay Protein

    doi: 10.1128/mBio.00431-12

    Figure Lengend Snippet: Guanidine HCl prevents cleavage and relocalization of AUF1 during poliovirus infection. (A) HeLa cells were mock treated (lanes 1 to 6) or treated with 2 mM guanidine HCl (GuaHCl; lanes 7 to 12) during mock infection (lanes 1 and 7) or poliovirus infection (lanes 2 to 6 and lanes 8 to 12). Lysates were collected at indicated hours postinfection (hpi) and subjected to SDS-PAGE and Western blot analysis using anti-AUF1 and antinucleolin (as a loading control) antibodies to visualize proteins. Electrophoretic mobilities of nucleolin and AUF1 are indicated to the right by an arrow and a bracket, respectively. (B) HeLa cells seeded on coverslips were mock infected or infected with poliovirus and treated with 2 mM guanidine HCl. Cells were fixed at either 0 or 5 hpi, immunostained with anti-AUF1 antibody (in red) and anti-3A antibody (in green), and stained with DAPI (blue) to visualize the nucleus. Proteins were visualized using a Zeiss Axiovert 200 M inverted microscope.

    Article Snippet: Cellular extracts were subjected to SDS-PAGE, and proteins were electroblotted to a PVDF membrane that was then probed using anti-AUF1 (Millipore) and antinucleolin (Abcam) antibodies (with expression levels of nucleolin serving as a loading control).

    Techniques: Infection, SDS Page, Western Blot, Staining, Inverted Microscopy

    Full-length and virally truncated forms of AUF1 interact with the 5′ NCR of poliovirus and human rhinovirus 16. Transcripts of the poliovirus 5′ NCR (A) or human rhinovirus 16 5′ NCR (B) were biotinylated with biotin-CTP. Streptavidin agarose resin was first incubated with either tRNA alone (lanes 3 and 4) or biotinylated 5′-NCR transcripts (lanes 5 and 6). All experiments were carried out in the presence of a molar excess of tRNA. Lysates from mock-infected or poliovirus-infected (A) or human rhinovirus 16-infected (B) HeLa cells were incubated with streptavidin-bound RNA in RNA affinity assays. Bound complexes were analyzed by SDS-PAGE and Western blot analysis using anti-AUF1 antibody (A) or anti-AUF1 and antinucleolin (as a loading control) antibodies (B). In lanes 1 and 2, 20% of the experimental input sample was loaded from mock or infected lysates, respectively. Electrophoretic mobilities of AUF1 and nucleolin are indicated by a bracket or arrow, respectively.

    Journal: mBio

    Article Title: Picornavirus Modification of a Host mRNA Decay Protein

    doi: 10.1128/mBio.00431-12

    Figure Lengend Snippet: Full-length and virally truncated forms of AUF1 interact with the 5′ NCR of poliovirus and human rhinovirus 16. Transcripts of the poliovirus 5′ NCR (A) or human rhinovirus 16 5′ NCR (B) were biotinylated with biotin-CTP. Streptavidin agarose resin was first incubated with either tRNA alone (lanes 3 and 4) or biotinylated 5′-NCR transcripts (lanes 5 and 6). All experiments were carried out in the presence of a molar excess of tRNA. Lysates from mock-infected or poliovirus-infected (A) or human rhinovirus 16-infected (B) HeLa cells were incubated with streptavidin-bound RNA in RNA affinity assays. Bound complexes were analyzed by SDS-PAGE and Western blot analysis using anti-AUF1 antibody (A) or anti-AUF1 and antinucleolin (as a loading control) antibodies (B). In lanes 1 and 2, 20% of the experimental input sample was loaded from mock or infected lysates, respectively. Electrophoretic mobilities of AUF1 and nucleolin are indicated by a bracket or arrow, respectively.

    Article Snippet: Cellular extracts were subjected to SDS-PAGE, and proteins were electroblotted to a PVDF membrane that was then probed using anti-AUF1 (Millipore) and antinucleolin (Abcam) antibodies (with expression levels of nucleolin serving as a loading control).

    Techniques: Incubation, Infection, SDS Page, Western Blot

    GATA3 expression stratified by histologic type and nuclear grade The mean GATA3 protein expression for each category is shown using bar plots. The error bars represent the standard error of the mean; n is number of spots. (A) GATA3 expression was significantly increased in ductal hyperplasia (DH, P

    Journal: Human pathology

    Article Title: Higher Levels of GATA3 Predict Better Survival in Women with Breast Cancer

    doi: 10.1016/j.humpath.2010.06.010

    Figure Lengend Snippet: GATA3 expression stratified by histologic type and nuclear grade The mean GATA3 protein expression for each category is shown using bar plots. The error bars represent the standard error of the mean; n is number of spots. (A) GATA3 expression was significantly increased in ductal hyperplasia (DH, P

    Article Snippet: Identical results were observed for GATA3 expression levels in breast cancer using the antibodies from either Abcam or Santa Cruz.

    Techniques: Expressing

    Representative images of GATA3 expression in breast tissues Staining was observed predominantly in the nuclei of glandular epithelial cells, as shown using a 20x objective in spots containing (A) normal ductal epithelium, (B) ductal hyperplasia without atypia, (C) ductal carcinoma in situ , and (D) invasive ductal carcinoma.

    Journal: Human pathology

    Article Title: Higher Levels of GATA3 Predict Better Survival in Women with Breast Cancer

    doi: 10.1016/j.humpath.2010.06.010

    Figure Lengend Snippet: Representative images of GATA3 expression in breast tissues Staining was observed predominantly in the nuclei of glandular epithelial cells, as shown using a 20x objective in spots containing (A) normal ductal epithelium, (B) ductal hyperplasia without atypia, (C) ductal carcinoma in situ , and (D) invasive ductal carcinoma.

    Article Snippet: Identical results were observed for GATA3 expression levels in breast cancer using the antibodies from either Abcam or Santa Cruz.

    Techniques: Expressing, Staining, In Situ

    Knockdown of Rad18 decreased GFP-Polκ recruitment at laser-induced sites of damage. A) U2OS cells were transfected with shRad18 or shNC and stable cell lines with a reduced Rad18 level were established. Top panel: western blot to show the level of Rad18 in stable cells. Bottom: U2OS cells-depleted of Rad18 were UV irradiated and cell extracts were separated by SDS-PAGE, and incubated with anti-PCNA antibodies.(B) The indicated stable cells were transfected with GFP-Polκ. 24h later, the cells were micro-irradiated with a UVA laser and kinetic analysis of GFP-Polκ intensity at laser-irradiated sites was performed. Error bars represent standard errors based on 10 independent measurements. C) The proportion of cells with Polκ accumulation was quantified.

    Journal: DNA repair

    Article Title: Mouse DNA Polymerase Kappa Has A Functional Role In the Repair of DNA Strand Breaks

    doi: 10.1016/j.dnarep.2013.02.008

    Figure Lengend Snippet: Knockdown of Rad18 decreased GFP-Polκ recruitment at laser-induced sites of damage. A) U2OS cells were transfected with shRad18 or shNC and stable cell lines with a reduced Rad18 level were established. Top panel: western blot to show the level of Rad18 in stable cells. Bottom: U2OS cells-depleted of Rad18 were UV irradiated and cell extracts were separated by SDS-PAGE, and incubated with anti-PCNA antibodies.(B) The indicated stable cells were transfected with GFP-Polκ. 24h later, the cells were micro-irradiated with a UVA laser and kinetic analysis of GFP-Polκ intensity at laser-irradiated sites was performed. Error bars represent standard errors based on 10 independent measurements. C) The proportion of cells with Polκ accumulation was quantified.

    Article Snippet: Individual clones were isolated by limiting dilution in media containing puromycin (1 μg/mL) and screened for Rad18 expression levels with antibodies against Rad18 (Abcam).

    Techniques: Transfection, Stable Transfection, Western Blot, Irradiation, SDS Page, Incubation

    Loss of Polκ resulted in reduced rates of global strand break repair. (A) Polκ +/+ Xpc −/− and Polκ −/− Xpc −/− MEFs were treated with 200 μM H 2 O 2 for 10 min. At indicated time points cells were analyzed with alkaline comet assay. Representative images of cells for each time point are shown. (B) The quantitative distribution of tail moments for each time point is shown. (C) Polκ −/− MEFs complemented with GFP or GFP-Polκ were treated with 600 μM H 2 O 2 at 4°C for 30 min. (D) Rad18-depleted U2OS cells were transfected with siPolκ, 48 h later, the cells were treated with 1 mM H 2 O 2 at 4°C for 10 min. (E) Polκ +/+ Xpc −/− and Polκ −/− Xpc −/− MEFs were treated with 300 μM MMS for 1h. At indicated time points cells were analyzed with alkaline comet assay. The quantitative distribution of tail moments for each time point is shown. At least 100 cells were scored in each sample and experiment. Data represent the mean of three independent experiments (+/− SE).

    Journal: DNA repair

    Article Title: Mouse DNA Polymerase Kappa Has A Functional Role In the Repair of DNA Strand Breaks

    doi: 10.1016/j.dnarep.2013.02.008

    Figure Lengend Snippet: Loss of Polκ resulted in reduced rates of global strand break repair. (A) Polκ +/+ Xpc −/− and Polκ −/− Xpc −/− MEFs were treated with 200 μM H 2 O 2 for 10 min. At indicated time points cells were analyzed with alkaline comet assay. Representative images of cells for each time point are shown. (B) The quantitative distribution of tail moments for each time point is shown. (C) Polκ −/− MEFs complemented with GFP or GFP-Polκ were treated with 600 μM H 2 O 2 at 4°C for 30 min. (D) Rad18-depleted U2OS cells were transfected with siPolκ, 48 h later, the cells were treated with 1 mM H 2 O 2 at 4°C for 10 min. (E) Polκ +/+ Xpc −/− and Polκ −/− Xpc −/− MEFs were treated with 300 μM MMS for 1h. At indicated time points cells were analyzed with alkaline comet assay. The quantitative distribution of tail moments for each time point is shown. At least 100 cells were scored in each sample and experiment. Data represent the mean of three independent experiments (+/− SE).

    Article Snippet: Individual clones were isolated by limiting dilution in media containing puromycin (1 μg/mL) and screened for Rad18 expression levels with antibodies against Rad18 (Abcam).

    Techniques: Alkaline Single Cell Gel Electrophoresis, Transfection

    The sensitivity of Polκ-deficient MEFs to DNA damage agent H 2 O 2 . Polκ −/− MEFs were treated with X-rays (A) or H 2 O 2 at 4°C for 1 h (B) and further incubated in fresh medium for 7–10 days. (C) Cell lysates of Polκ −/− MEFs complemented with GFPor GFP-Polκ were separated by SDS-PAGE and then incubated with anti-GFP or anti-β-actin antibodies. “+” represents a positive control. “#1”and “#2” are two different stable clones. (D) Polκ −/− MEFs complemented with GFP or GFP-Polκ were treated with H 2 O 2 at 4°C for 1 h and further incubated in fresh medium for 7–10 days. (E) Polκ and XPC double knockout MEFs were treated with H 2 O 2 as in (D). (F) Polκ in Rad18-depleted U2OS cells was transiently knocked down and the sensitivity of the cells to H 2 O 2 treatment were examined as in (D). Surviving fraction was expressed as a percentage of mock-treated cells. Values are the mean of three independent experiments (+/− SE).

    Journal: DNA repair

    Article Title: Mouse DNA Polymerase Kappa Has A Functional Role In the Repair of DNA Strand Breaks

    doi: 10.1016/j.dnarep.2013.02.008

    Figure Lengend Snippet: The sensitivity of Polκ-deficient MEFs to DNA damage agent H 2 O 2 . Polκ −/− MEFs were treated with X-rays (A) or H 2 O 2 at 4°C for 1 h (B) and further incubated in fresh medium for 7–10 days. (C) Cell lysates of Polκ −/− MEFs complemented with GFPor GFP-Polκ were separated by SDS-PAGE and then incubated with anti-GFP or anti-β-actin antibodies. “+” represents a positive control. “#1”and “#2” are two different stable clones. (D) Polκ −/− MEFs complemented with GFP or GFP-Polκ were treated with H 2 O 2 at 4°C for 1 h and further incubated in fresh medium for 7–10 days. (E) Polκ and XPC double knockout MEFs were treated with H 2 O 2 as in (D). (F) Polκ in Rad18-depleted U2OS cells was transiently knocked down and the sensitivity of the cells to H 2 O 2 treatment were examined as in (D). Surviving fraction was expressed as a percentage of mock-treated cells. Values are the mean of three independent experiments (+/− SE).

    Article Snippet: Individual clones were isolated by limiting dilution in media containing puromycin (1 μg/mL) and screened for Rad18 expression levels with antibodies against Rad18 (Abcam).

    Techniques: Incubation, SDS Page, Positive Control, Double Knockout