19-096 Search Results


94
ATCC ccug 19096
Ccug 19096, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
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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Average 93 stars, based on 1 article reviews
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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
https://www.bioz.com/result/rabbit polyclonal anti actn4/product/Proteintech
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Proteintech antibodies against actn4
<t>ACTN4</t> expression in placental CTBs. a IHC staining of ACTN4 in the human first trimester placenta villi. CTBs were stained for CK7; Scale bars: 100 μm. b EdU labeling in explant cultures. Villous explants isolated from the first trimester placentas were treated with the control siRNA (si-NC) or ACTN4 siRNA (si-ACTN4). Representative pictures showed EdU (pink) labeling in the villous cytotrophoblasts of floating villi following 72-h treatment. Nuclei were counterstained with DAPI (blue). Scale bars: 100 μm. All data are presented as the means ± SEM of three independent experiments. * p < 0.05
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
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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

ACTN4 expression in placental CTBs. a IHC staining of ACTN4 in the human first trimester placenta villi. CTBs were stained for CK7; Scale bars: 100 μm. b EdU labeling in explant cultures. Villous explants isolated from the first trimester placentas were treated with the control siRNA (si-NC) or ACTN4 siRNA (si-ACTN4). Representative pictures showed EdU (pink) labeling in the villous cytotrophoblasts of floating villi following 72-h treatment. Nuclei were counterstained with DAPI (blue). Scale bars: 100 μm. All data are presented as the means ± SEM of three independent experiments. * p < 0.05

Journal: Reproductive Biology and Endocrinology : RB&E

Article Title: Alpha‐actinin‐4 is essential for maintaining normal trophoblast proliferation and differentiation during early pregnancy

doi: 10.1186/s12958-021-00733-0

Figure Lengend Snippet: ACTN4 expression in placental CTBs. a IHC staining of ACTN4 in the human first trimester placenta villi. CTBs were stained for CK7; Scale bars: 100 μm. b EdU labeling in explant cultures. Villous explants isolated from the first trimester placentas were treated with the control siRNA (si-NC) or ACTN4 siRNA (si-ACTN4). Representative pictures showed EdU (pink) labeling in the villous cytotrophoblasts of floating villi following 72-h treatment. Nuclei were counterstained with DAPI (blue). Scale bars: 100 μm. All data are presented as the means ± SEM of three independent experiments. * p < 0.05

Article Snippet: Following blocking with 5 % nonfat dry milk (Bio-Rad) at room temperature for 1 h, the membranes were immunoblotted overnight at 4 °C with primary antibodies against ACTN4 (1:3000, Proteintech), GCM-1(1:500, Proteintech), AKT (1:1000, Abcam), AKT phosphorylated at serine 473 (1:1000, Cell Signaling Technology, Danvers, MA, USA), p-GSK3β (1:1000, Cell Signaling Technology), Snail (1:1000, Cell Signaling Technology), N-cadherin (1:1000, Cell Signaling Technology), Vimentin (1:1000, Abcam), or β-actin (1:1000, Proteintech).

Techniques: Expressing, Immunohistochemistry, Staining, Labeling, Isolation

ACTN4 expression in the process of CTB differentiation into STBs. a Immunofluorescence staining for ACTN4 (red) and CK7 (green) in the freshly isolated primary human CTB cells. Staining was performed after 3 or 48 h of culture. Nuclei were counterstained with DAPI (blue). White dashed circles and white arrows indicate syncytialized cells and unsyncytialized cells, respectively. Scale bars: 100 μm. b Western blotting for ACTN4 and GCM-1 (a syncytiotrophoblast marker) in the primary human CTB cells after 3 or 48 h of culture. All data are presented as the means ± SEM of three independent experiments. ** P < 0.01; *** P < 0.001

Journal: Reproductive Biology and Endocrinology : RB&E

Article Title: Alpha‐actinin‐4 is essential for maintaining normal trophoblast proliferation and differentiation during early pregnancy

doi: 10.1186/s12958-021-00733-0

Figure Lengend Snippet: ACTN4 expression in the process of CTB differentiation into STBs. a Immunofluorescence staining for ACTN4 (red) and CK7 (green) in the freshly isolated primary human CTB cells. Staining was performed after 3 or 48 h of culture. Nuclei were counterstained with DAPI (blue). White dashed circles and white arrows indicate syncytialized cells and unsyncytialized cells, respectively. Scale bars: 100 μm. b Western blotting for ACTN4 and GCM-1 (a syncytiotrophoblast marker) in the primary human CTB cells after 3 or 48 h of culture. All data are presented as the means ± SEM of three independent experiments. ** P < 0.01; *** P < 0.001

Article Snippet: Following blocking with 5 % nonfat dry milk (Bio-Rad) at room temperature for 1 h, the membranes were immunoblotted overnight at 4 °C with primary antibodies against ACTN4 (1:3000, Proteintech), GCM-1(1:500, Proteintech), AKT (1:1000, Abcam), AKT phosphorylated at serine 473 (1:1000, Cell Signaling Technology, Danvers, MA, USA), p-GSK3β (1:1000, Cell Signaling Technology), Snail (1:1000, Cell Signaling Technology), N-cadherin (1:1000, Cell Signaling Technology), Vimentin (1:1000, Abcam), or β-actin (1:1000, Proteintech).

Techniques: Expressing, Immunofluorescence, Staining, Isolation, Western Blot, Marker

Role of ACNT4 in villous explants outgrowth. a IHC staining of ACTN4 in the human first trimester placenta villi. iEVTs were stained for HLA-G. Scale bars: 200 μm. b EdU labeling in explant cultures. Representative pictures showed EdU (pink) labeling in the CCTs of the anchoring villi after 72-h treatment of ACNT4 with siRNA. Nuclei were counterstained with DAPI (blue). Scale bars: 100 μm. c Outgrowth of induced EVTs in a villous explant culture model. Left panel, bright and fluorescent field views showing that small interfering RNA labeled with FAM successfully penetrated the villous explants. Right panel, the outgrowth of induced EVTs from villous explants treated with control siRNA (si-NC) or ACTN4 siRNA (si-ACTN4) for 24 and 48 h. Scale bar: 1000 μm. All data are presented as the means ± SEM of three independent experiments, * P < 0.05; ** P < 0.01

Journal: Reproductive Biology and Endocrinology : RB&E

Article Title: Alpha‐actinin‐4 is essential for maintaining normal trophoblast proliferation and differentiation during early pregnancy

doi: 10.1186/s12958-021-00733-0

Figure Lengend Snippet: Role of ACNT4 in villous explants outgrowth. a IHC staining of ACTN4 in the human first trimester placenta villi. iEVTs were stained for HLA-G. Scale bars: 200 μm. b EdU labeling in explant cultures. Representative pictures showed EdU (pink) labeling in the CCTs of the anchoring villi after 72-h treatment of ACNT4 with siRNA. Nuclei were counterstained with DAPI (blue). Scale bars: 100 μm. c Outgrowth of induced EVTs in a villous explant culture model. Left panel, bright and fluorescent field views showing that small interfering RNA labeled with FAM successfully penetrated the villous explants. Right panel, the outgrowth of induced EVTs from villous explants treated with control siRNA (si-NC) or ACTN4 siRNA (si-ACTN4) for 24 and 48 h. Scale bar: 1000 μm. All data are presented as the means ± SEM of three independent experiments, * P < 0.05; ** P < 0.01

Article Snippet: Following blocking with 5 % nonfat dry milk (Bio-Rad) at room temperature for 1 h, the membranes were immunoblotted overnight at 4 °C with primary antibodies against ACTN4 (1:3000, Proteintech), GCM-1(1:500, Proteintech), AKT (1:1000, Abcam), AKT phosphorylated at serine 473 (1:1000, Cell Signaling Technology, Danvers, MA, USA), p-GSK3β (1:1000, Cell Signaling Technology), Snail (1:1000, Cell Signaling Technology), N-cadherin (1:1000, Cell Signaling Technology), Vimentin (1:1000, Abcam), or β-actin (1:1000, Proteintech).

Techniques: Immunohistochemistry, Staining, Labeling, Small Interfering RNA

Effects of ACTN4 on HTR8/SVneo cell invasion and migration. a TRITC-Phalloidin staining on si-NC and si-ACTN4 of HTR8/SVneo cells. Scale bar, 200 μm. b Representative images and quantification of cells from the HTR8/SVneo cells with invasion in the presence or absence of a Matrigel-coated membrane for 24 h. Scale bar: 200 μm. c HTR8/SVneo cells attached to the culture plates after wounding and treatment with ACTN4 siRNA. The percentage of wound closure was calculated at 24 h. Scale bar: 400 μm. All data are presented as the means ± SEM of three independent experiments. ** P < 0.01

Journal: Reproductive Biology and Endocrinology : RB&E

Article Title: Alpha‐actinin‐4 is essential for maintaining normal trophoblast proliferation and differentiation during early pregnancy

doi: 10.1186/s12958-021-00733-0

Figure Lengend Snippet: Effects of ACTN4 on HTR8/SVneo cell invasion and migration. a TRITC-Phalloidin staining on si-NC and si-ACTN4 of HTR8/SVneo cells. Scale bar, 200 μm. b Representative images and quantification of cells from the HTR8/SVneo cells with invasion in the presence or absence of a Matrigel-coated membrane for 24 h. Scale bar: 200 μm. c HTR8/SVneo cells attached to the culture plates after wounding and treatment with ACTN4 siRNA. The percentage of wound closure was calculated at 24 h. Scale bar: 400 μm. All data are presented as the means ± SEM of three independent experiments. ** P < 0.01

Article Snippet: Following blocking with 5 % nonfat dry milk (Bio-Rad) at room temperature for 1 h, the membranes were immunoblotted overnight at 4 °C with primary antibodies against ACTN4 (1:3000, Proteintech), GCM-1(1:500, Proteintech), AKT (1:1000, Abcam), AKT phosphorylated at serine 473 (1:1000, Cell Signaling Technology, Danvers, MA, USA), p-GSK3β (1:1000, Cell Signaling Technology), Snail (1:1000, Cell Signaling Technology), N-cadherin (1:1000, Cell Signaling Technology), Vimentin (1:1000, Abcam), or β-actin (1:1000, Proteintech).

Techniques: Migration, Staining

ACTN4 regulation of the AKT/GSK3β/Snail pathway in trophoblasts. Western blotting for ACTN4, p-AKT Ser473 , AKT, p-GSK3β, Snail, N-cadherin, and Vimentin in the first trimester villi (left panel) and HTR-8/SVneo cells (right panel) transfected with si-NC or si-ACTN4 for 72 h. All data are presented as the means ± SEM of three independent experiments. * P < 0.05; ** P < 0.01

Journal: Reproductive Biology and Endocrinology : RB&E

Article Title: Alpha‐actinin‐4 is essential for maintaining normal trophoblast proliferation and differentiation during early pregnancy

doi: 10.1186/s12958-021-00733-0

Figure Lengend Snippet: ACTN4 regulation of the AKT/GSK3β/Snail pathway in trophoblasts. Western blotting for ACTN4, p-AKT Ser473 , AKT, p-GSK3β, Snail, N-cadherin, and Vimentin in the first trimester villi (left panel) and HTR-8/SVneo cells (right panel) transfected with si-NC or si-ACTN4 for 72 h. All data are presented as the means ± SEM of three independent experiments. * P < 0.05; ** P < 0.01

Article Snippet: Following blocking with 5 % nonfat dry milk (Bio-Rad) at room temperature for 1 h, the membranes were immunoblotted overnight at 4 °C with primary antibodies against ACTN4 (1:3000, Proteintech), GCM-1(1:500, Proteintech), AKT (1:1000, Abcam), AKT phosphorylated at serine 473 (1:1000, Cell Signaling Technology, Danvers, MA, USA), p-GSK3β (1:1000, Cell Signaling Technology), Snail (1:1000, Cell Signaling Technology), N-cadherin (1:1000, Cell Signaling Technology), Vimentin (1:1000, Abcam), or β-actin (1:1000, Proteintech).

Techniques: Western Blot, Transfection

ACTN4 expression in the iEVTs from sPE placentas. a IHC staining of ACTN4 on the maternal side of normal and sPE placentas. Staining was performed on serial sections; iEVTs were stained for HLA-G. DS: decidual side. Scale bars: 200 μm. b Western blotting for ACTN4 on the maternal side of normal and sPE placentas. All data are presented as the means ± SEM of three independent experiments. *** P < 0.001

Journal: Reproductive Biology and Endocrinology : RB&E

Article Title: Alpha‐actinin‐4 is essential for maintaining normal trophoblast proliferation and differentiation during early pregnancy

doi: 10.1186/s12958-021-00733-0

Figure Lengend Snippet: ACTN4 expression in the iEVTs from sPE placentas. a IHC staining of ACTN4 on the maternal side of normal and sPE placentas. Staining was performed on serial sections; iEVTs were stained for HLA-G. DS: decidual side. Scale bars: 200 μm. b Western blotting for ACTN4 on the maternal side of normal and sPE placentas. All data are presented as the means ± SEM of three independent experiments. *** P < 0.001

Article Snippet: Following blocking with 5 % nonfat dry milk (Bio-Rad) at room temperature for 1 h, the membranes were immunoblotted overnight at 4 °C with primary antibodies against ACTN4 (1:3000, Proteintech), GCM-1(1:500, Proteintech), AKT (1:1000, Abcam), AKT phosphorylated at serine 473 (1:1000, Cell Signaling Technology, Danvers, MA, USA), p-GSK3β (1:1000, Cell Signaling Technology), Snail (1:1000, Cell Signaling Technology), N-cadherin (1:1000, Cell Signaling Technology), Vimentin (1:1000, Abcam), or β-actin (1:1000, Proteintech).

Techniques: Expressing, Immunohistochemistry, Staining, Western Blot