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  • 93
    ATCC c pusillum atcc 19096
    C Pusillum Atcc 19096, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/c pusillum atcc 19096/product/ATCC
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    93
    Proteintech immunoblottedwith primary antibodies against actn4
    Immunoblottedwith Primary Antibodies Against Actn4, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/immunoblottedwith primary antibodies against actn4/product/Proteintech
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    Proteintech alpha actinin polyclonal antibody
    Key reagents and resources used in this study.
    Alpha Actinin Polyclonal Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Proteintech anti α actinin4
    Key reagents and resources used in this study.
    Anti α Actinin4, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Proteintech rabbit polyclonal anti actn4
    MTBP interacts with <t>ACTN4</t> and inhibits ACTN4-mediated cell migration. (a) Whole cell extracts from SaOs2-LM7 cells were immunoprecipitated (IP) with MTBP (BP) or ACTN4 (A4) antibodies (endogenous). Immunoprecipitants were subjected to western blotting for MTBP or ACTN4. Matched isotype antibodies (Iso) were used as negative controls. In vitro translated ACTN4 and FLAG-tagged MTBP were incubated in PBS and immunoprecipitated with ACTN4 (A4, left) or FLAG antibodies (FL, right), followed by immunoblotting for MTBP or ACTN4, respectively ( in vitro ). (b) Immunofluorescence was performed to examine endogenous colocalization of MTBP and ACTN4 in SaOs2-LM7 cells using indicated antibodies. DNA was stained using DAPI. Results were analyzed on a Leica epifluorescence microscope. A merge picture indicates that MTBP and ACTN4 partially colocalize mainly in the cytoplasm (yellow). (c, d) SaOs2-LM7 and U2OS cells stably infected with either empty (ACTN4−) or ACTN4 -encoding (ACTN4+) lentiviral vectors were infected with empty (MTBP−) or MTBP -encoding (MTBP+) adenoviruses (c). Cells stably infected with empty ( ACTN4 −) or ACTN4 shRNA-encoding ( ACTN4 +) lentiviral vectors were transiently transfected with non-targeted ( MTBP −) or MTBP- specific ( MTBP +) siRNAs (d). Thirty six hours after manipulation of MTBP expression, migration assays were performed. Migrating cells were stained and entire fields were counted. Graphs showing relative cell migration (%) compared to the number of migrating cells in control. Western blotting results below the graphs demonstrating successful manipulation of MTBP and ACTN4 expression. Error bars are means ± S.D. from three independent experiments. *, P < 0.05 and **, P < 0.01; t test. N.S., not significant. Control: white, MTBP alone manipulated: grey, ACTN4 alone manipulated: oblique, MTBP and ACTN4 manipulated: black.
    Rabbit Polyclonal Anti Actn4, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Key reagents and resources used in this study.

    Journal: Cell Death and Differentiation

    Article Title: Inhibition of cGAS-STING by JQ1 alleviates oxidative stress-induced retina inflammation and degeneration

    doi: 10.1038/s41418-022-00967-4

    Figure Lengend Snippet: Key reagents and resources used in this study.

    Article Snippet: Alpha Actinin Polyclonal antibody , Proteintech , cat# 11313-2.

    Techniques: Marker, Recombinant, Transfection, Expressing, Microarray, Software

    MTBP interacts with ACTN4 and inhibits ACTN4-mediated cell migration. (a) Whole cell extracts from SaOs2-LM7 cells were immunoprecipitated (IP) with MTBP (BP) or ACTN4 (A4) antibodies (endogenous). Immunoprecipitants were subjected to western blotting for MTBP or ACTN4. Matched isotype antibodies (Iso) were used as negative controls. In vitro translated ACTN4 and FLAG-tagged MTBP were incubated in PBS and immunoprecipitated with ACTN4 (A4, left) or FLAG antibodies (FL, right), followed by immunoblotting for MTBP or ACTN4, respectively ( in vitro ). (b) Immunofluorescence was performed to examine endogenous colocalization of MTBP and ACTN4 in SaOs2-LM7 cells using indicated antibodies. DNA was stained using DAPI. Results were analyzed on a Leica epifluorescence microscope. A merge picture indicates that MTBP and ACTN4 partially colocalize mainly in the cytoplasm (yellow). (c, d) SaOs2-LM7 and U2OS cells stably infected with either empty (ACTN4−) or ACTN4 -encoding (ACTN4+) lentiviral vectors were infected with empty (MTBP−) or MTBP -encoding (MTBP+) adenoviruses (c). Cells stably infected with empty ( ACTN4 −) or ACTN4 shRNA-encoding ( ACTN4 +) lentiviral vectors were transiently transfected with non-targeted ( MTBP −) or MTBP- specific ( MTBP +) siRNAs (d). Thirty six hours after manipulation of MTBP expression, migration assays were performed. Migrating cells were stained and entire fields were counted. Graphs showing relative cell migration (%) compared to the number of migrating cells in control. Western blotting results below the graphs demonstrating successful manipulation of MTBP and ACTN4 expression. Error bars are means ± S.D. from three independent experiments. *, P < 0.05 and **, P < 0.01; t test. N.S., not significant. Control: white, MTBP alone manipulated: grey, ACTN4 alone manipulated: oblique, MTBP and ACTN4 manipulated: black.

    Journal: Oncogene

    Article Title: MTBP suppresses cell migration and filopodia formation by inhibiting ACTN4

    doi: 10.1038/onc.2012.69

    Figure Lengend Snippet: MTBP interacts with ACTN4 and inhibits ACTN4-mediated cell migration. (a) Whole cell extracts from SaOs2-LM7 cells were immunoprecipitated (IP) with MTBP (BP) or ACTN4 (A4) antibodies (endogenous). Immunoprecipitants were subjected to western blotting for MTBP or ACTN4. Matched isotype antibodies (Iso) were used as negative controls. In vitro translated ACTN4 and FLAG-tagged MTBP were incubated in PBS and immunoprecipitated with ACTN4 (A4, left) or FLAG antibodies (FL, right), followed by immunoblotting for MTBP or ACTN4, respectively ( in vitro ). (b) Immunofluorescence was performed to examine endogenous colocalization of MTBP and ACTN4 in SaOs2-LM7 cells using indicated antibodies. DNA was stained using DAPI. Results were analyzed on a Leica epifluorescence microscope. A merge picture indicates that MTBP and ACTN4 partially colocalize mainly in the cytoplasm (yellow). (c, d) SaOs2-LM7 and U2OS cells stably infected with either empty (ACTN4−) or ACTN4 -encoding (ACTN4+) lentiviral vectors were infected with empty (MTBP−) or MTBP -encoding (MTBP+) adenoviruses (c). Cells stably infected with empty ( ACTN4 −) or ACTN4 shRNA-encoding ( ACTN4 +) lentiviral vectors were transiently transfected with non-targeted ( MTBP −) or MTBP- specific ( MTBP +) siRNAs (d). Thirty six hours after manipulation of MTBP expression, migration assays were performed. Migrating cells were stained and entire fields were counted. Graphs showing relative cell migration (%) compared to the number of migrating cells in control. Western blotting results below the graphs demonstrating successful manipulation of MTBP and ACTN4 expression. Error bars are means ± S.D. from three independent experiments. *, P < 0.05 and **, P < 0.01; t test. N.S., not significant. Control: white, MTBP alone manipulated: grey, ACTN4 alone manipulated: oblique, MTBP and ACTN4 manipulated: black.

    Article Snippet: For western blotting, rabbit polyclonal anti-ACTN4 (210-356-C050, Enzo Lifesciences, Exeter, UK), rabbit polyclonal anti-ACTN4 (19096-1-AP, ProteinTech, Chicago, IL), goat polyclonal anti-MTBP (K20, Santa Cruz Biotech, Santa Cruz, CA), mouse monoclonal anti-RGS-His (34610, Qiagen, Valencia, CA), rabbit polyclonal anti-actin (AAN01, Cytoskeleton, Denver, CO), mouse monoclonal anti-vinculin (10R-C105a, Fitzgerald, Acton, MA), mouse monoclonal vimentin (ab8978, Abcam, Cambridge, MA), rabbit polyclonal tropomyosin 3 (10737-1-AP, ProteinTech), and mouse monoclonal anti-β-tubulin (T0198, Sigma, St. Louis, MO) were used.

    Techniques: Migration, Immunoprecipitation, Western Blot, In Vitro, Incubation, Immunofluorescence, Staining, Microscopy, Stable Transfection, Infection, shRNA, Transfection, Expressing

    MTBP inhibits ACTN4-mediated filopodia formation and cross-linking of F-actin. (a) SaOs2-LM7 (left) and U2OS (right) cells with or without ACTN4 overexpression were infected with empty (control) or MTBP -encoding (MTBP) adenoviruses. Forty eight (48) hours later, phalloidin staining was performed. Cells (n=100) were examined for filopodia formation. The percentages of cells positive for filopodia formation (top) and representative phalloidin staining pictures (bottom). (b) Actin bundling assay. In vitro translated MTBP and/or ACTN4 proteins were incubated with purified F-actin in the assay reaction, followed by protein sedimentation. Luciferase (Luc) was used as a negative control. Supernatant (S) and pellet (P) fractions were subjected to western blotting for actin, ACTN4, and MTBP (left). Graph showing the percentage of sedimented bundled F-actin (pellet) as analyzed by densitometry (right). Error bars are means ± S.D. from three independent experiments. **, P < 0.01; t test. N.S., not significant.

    Journal: Oncogene

    Article Title: MTBP suppresses cell migration and filopodia formation by inhibiting ACTN4

    doi: 10.1038/onc.2012.69

    Figure Lengend Snippet: MTBP inhibits ACTN4-mediated filopodia formation and cross-linking of F-actin. (a) SaOs2-LM7 (left) and U2OS (right) cells with or without ACTN4 overexpression were infected with empty (control) or MTBP -encoding (MTBP) adenoviruses. Forty eight (48) hours later, phalloidin staining was performed. Cells (n=100) were examined for filopodia formation. The percentages of cells positive for filopodia formation (top) and representative phalloidin staining pictures (bottom). (b) Actin bundling assay. In vitro translated MTBP and/or ACTN4 proteins were incubated with purified F-actin in the assay reaction, followed by protein sedimentation. Luciferase (Luc) was used as a negative control. Supernatant (S) and pellet (P) fractions were subjected to western blotting for actin, ACTN4, and MTBP (left). Graph showing the percentage of sedimented bundled F-actin (pellet) as analyzed by densitometry (right). Error bars are means ± S.D. from three independent experiments. **, P < 0.01; t test. N.S., not significant.

    Article Snippet: For western blotting, rabbit polyclonal anti-ACTN4 (210-356-C050, Enzo Lifesciences, Exeter, UK), rabbit polyclonal anti-ACTN4 (19096-1-AP, ProteinTech, Chicago, IL), goat polyclonal anti-MTBP (K20, Santa Cruz Biotech, Santa Cruz, CA), mouse monoclonal anti-RGS-His (34610, Qiagen, Valencia, CA), rabbit polyclonal anti-actin (AAN01, Cytoskeleton, Denver, CO), mouse monoclonal anti-vinculin (10R-C105a, Fitzgerald, Acton, MA), mouse monoclonal vimentin (ab8978, Abcam, Cambridge, MA), rabbit polyclonal tropomyosin 3 (10737-1-AP, ProteinTech), and mouse monoclonal anti-β-tubulin (T0198, Sigma, St. Louis, MO) were used.

    Techniques: Over Expression, Infection, Staining, In Vitro, Incubation, Purification, Sedimentation, Luciferase, Negative Control, Western Blot

    Nuclear localization of MTBP is not required for inhibiting ACTN4 function. (a) Nuclear localization signal (NLS) domain in MTBP with mutated amino acids (underlined, left). Immunofluorescence images demonstrating the localization of FLAG-tagged full-length MTBP (MTBP) and mutant MTBP (MTBPnls, right). (b) SaOs2-LM7 cells with or without ACTN4 overexpression were infected with lentiviral vectors encoding empty (control) or MTBPnls mutant (MTBPnls), followed by cell migration assays. Migrating cells were stained, and entire fields were counted. Relative cell migration (%) compared to the number of migrating cells in control (top) and representative staining pictures (bottom). (c) Phalloidin staining was performed using the same cells as in Figure 5b. Cells (n= 100) were examined for filopodia formation. The percentages of cells positive for filopodia formation (top) and representative phalloidin staining pictures (bottom). Error bars are means ± S.D. from three independent experiments. *, P < 0.05 and **, P < 0.01; t test. (d) 293T cells which had undetectable levels of endogenous MTBP were transfected with Flag-tagged full-length MTBP (MTBP), NLS mutant (MTBPnls) and deletion mutants (F4 and ΔC). A diagram showing regions deleted for MTBP mutants. Forty-eight hours later, co-immunoprecipitation (IP) studies were performed using ACTN4 antibody (A4), followed by western blotting for MTBP. Matched isotype antibodies (Iso) were used as negative controls. In vitro synthesized ACTN4 and mutant MTBP (MTBPnls, F4, and ΔC) were co-incubated for co-IP studies using ACTN4 or FLAG (FL) antibodies, followed by immunoblotting for MTBP or ACTN4.

    Journal: Oncogene

    Article Title: MTBP suppresses cell migration and filopodia formation by inhibiting ACTN4

    doi: 10.1038/onc.2012.69

    Figure Lengend Snippet: Nuclear localization of MTBP is not required for inhibiting ACTN4 function. (a) Nuclear localization signal (NLS) domain in MTBP with mutated amino acids (underlined, left). Immunofluorescence images demonstrating the localization of FLAG-tagged full-length MTBP (MTBP) and mutant MTBP (MTBPnls, right). (b) SaOs2-LM7 cells with or without ACTN4 overexpression were infected with lentiviral vectors encoding empty (control) or MTBPnls mutant (MTBPnls), followed by cell migration assays. Migrating cells were stained, and entire fields were counted. Relative cell migration (%) compared to the number of migrating cells in control (top) and representative staining pictures (bottom). (c) Phalloidin staining was performed using the same cells as in Figure 5b. Cells (n= 100) were examined for filopodia formation. The percentages of cells positive for filopodia formation (top) and representative phalloidin staining pictures (bottom). Error bars are means ± S.D. from three independent experiments. *, P < 0.05 and **, P < 0.01; t test. (d) 293T cells which had undetectable levels of endogenous MTBP were transfected with Flag-tagged full-length MTBP (MTBP), NLS mutant (MTBPnls) and deletion mutants (F4 and ΔC). A diagram showing regions deleted for MTBP mutants. Forty-eight hours later, co-immunoprecipitation (IP) studies were performed using ACTN4 antibody (A4), followed by western blotting for MTBP. Matched isotype antibodies (Iso) were used as negative controls. In vitro synthesized ACTN4 and mutant MTBP (MTBPnls, F4, and ΔC) were co-incubated for co-IP studies using ACTN4 or FLAG (FL) antibodies, followed by immunoblotting for MTBP or ACTN4.

    Article Snippet: For western blotting, rabbit polyclonal anti-ACTN4 (210-356-C050, Enzo Lifesciences, Exeter, UK), rabbit polyclonal anti-ACTN4 (19096-1-AP, ProteinTech, Chicago, IL), goat polyclonal anti-MTBP (K20, Santa Cruz Biotech, Santa Cruz, CA), mouse monoclonal anti-RGS-His (34610, Qiagen, Valencia, CA), rabbit polyclonal anti-actin (AAN01, Cytoskeleton, Denver, CO), mouse monoclonal anti-vinculin (10R-C105a, Fitzgerald, Acton, MA), mouse monoclonal vimentin (ab8978, Abcam, Cambridge, MA), rabbit polyclonal tropomyosin 3 (10737-1-AP, ProteinTech), and mouse monoclonal anti-β-tubulin (T0198, Sigma, St. Louis, MO) were used.

    Techniques: Immunofluorescence, Mutagenesis, Over Expression, Infection, Migration, Staining, Transfection, Immunoprecipitation, Western Blot, In Vitro, Synthesized, Incubation, Co-Immunoprecipitation Assay