actin monoclonal antibody Search Results


mouse monoclonal α actinin  (Cytoskeleton Inc)
95
Cytoskeleton Inc mouse monoclonal α actinin
(A,B) Cell surface topography revealed by platinum replica EM of non-extracted untreated (A) or 100 µM blebbistatin (BS)-treated cells (B). (C,D) Fluorescence microscopy of phalloidin-stained F-actin and immunostained <t>α-actinin</t> in detergent-extracted untreated (C) or 100 µM blebbistatin-treated cells (D). (E) Fractions of the cell perimeter occupied by lamellipodia and ruffles in untreated cells, cells treated with 75 µM or 100 µM blebbistatin, and cells recovering from treatment with 100 µM blebbistatin for indicated periods of time in minutes. Error bars, SD. (F,G) Fluorescence microscopy of phalloidin-stained F-actin and immunostained vinculin in detergent-extracted untreated (F) or 100 µM blebbistatin-treated (G) cells. Boxed regions in C, D, E, and G are zoomed in bottom panels. Scale bars, 2 µm (A,B) and 20 µm (C,D,F,G).
Mouse Monoclonal α Actinin, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 95 stars, based on 1 article reviews
mouse monoclonal α actinin - by Bioz Stars, 2026-03
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β actin  (Bioss)
95
Bioss β actin
(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and <t>β-actin.</t> Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.
β Actin, supplied by Bioss, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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β actin  (Proteintech)
97
Proteintech β actin
(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and <t>β-actin.</t> Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.
β Actin, supplied by Proteintech, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ta811000s  (OriGene)
94
OriGene ta811000s
(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and <t>β-actin.</t> Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.
Ta811000s, supplied by OriGene, 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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mouse anti actin c4  (Valiant Co Ltd)
93
Valiant Co Ltd mouse anti actin c4
(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and <t>β-actin.</t> Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.
Mouse Anti Actin C4, supplied by Valiant Co Ltd, 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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mouse monoclonal antibodies  (Valiant Co Ltd)
95
Valiant Co Ltd mouse monoclonal antibodies
(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and <t>β-actin.</t> Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.
Mouse Monoclonal Antibodies, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse monoclonal antibodies - by Bioz Stars, 2026-03
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mouse monoclonal β actin antibody  (Boster Bio)
91
Boster Bio mouse monoclonal β actin antibody
(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and <t>β-actin.</t> Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.
Mouse Monoclonal β Actin Antibody, supplied by Boster Bio, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse monoclonal β actin antibody - by Bioz Stars, 2026-03
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anti β actin  (Boster Bio)
93
Boster Bio anti β actin
(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and <t>β-actin.</t> Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.
Anti β Actin, supplied by Boster Bio, 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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anti β actin - by Bioz Stars, 2026-03
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mouse antibody against β actin  (OriGene)
95
OriGene mouse antibody against β actin
(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and <t>β-actin.</t> Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.
Mouse Antibody Against β Actin, supplied by OriGene, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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mouse anti β actin  (Boster Bio)
95
Boster Bio mouse anti β actin
(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and <t>β-actin.</t> Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.
Mouse Anti β Actin, supplied by Boster Bio, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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actin mp biomedicals 08637931  (Valiant Co Ltd)
86
Valiant Co Ltd actin mp biomedicals 08637931
(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and <t>β-actin.</t> Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.
Actin Mp Biomedicals 08637931, supplied by Valiant Co Ltd, 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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actin mp biomedicals 08637931 - by Bioz Stars, 2026-03
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Image Search Results


(A,B) Cell surface topography revealed by platinum replica EM of non-extracted untreated (A) or 100 µM blebbistatin (BS)-treated cells (B). (C,D) Fluorescence microscopy of phalloidin-stained F-actin and immunostained α-actinin in detergent-extracted untreated (C) or 100 µM blebbistatin-treated cells (D). (E) Fractions of the cell perimeter occupied by lamellipodia and ruffles in untreated cells, cells treated with 75 µM or 100 µM blebbistatin, and cells recovering from treatment with 100 µM blebbistatin for indicated periods of time in minutes. Error bars, SD. (F,G) Fluorescence microscopy of phalloidin-stained F-actin and immunostained vinculin in detergent-extracted untreated (F) or 100 µM blebbistatin-treated (G) cells. Boxed regions in C, D, E, and G are zoomed in bottom panels. Scale bars, 2 µm (A,B) and 20 µm (C,D,F,G).

Journal: PLoS ONE

Article Title: Functions of Nonmuscle Myosin II in Assembly of the Cellular Contractile System

doi: 10.1371/journal.pone.0040814

Figure Lengend Snippet: (A,B) Cell surface topography revealed by platinum replica EM of non-extracted untreated (A) or 100 µM blebbistatin (BS)-treated cells (B). (C,D) Fluorescence microscopy of phalloidin-stained F-actin and immunostained α-actinin in detergent-extracted untreated (C) or 100 µM blebbistatin-treated cells (D). (E) Fractions of the cell perimeter occupied by lamellipodia and ruffles in untreated cells, cells treated with 75 µM or 100 µM blebbistatin, and cells recovering from treatment with 100 µM blebbistatin for indicated periods of time in minutes. Error bars, SD. (F,G) Fluorescence microscopy of phalloidin-stained F-actin and immunostained vinculin in detergent-extracted untreated (F) or 100 µM blebbistatin-treated (G) cells. Boxed regions in C, D, E, and G are zoomed in bottom panels. Scale bars, 2 µm (A,B) and 20 µm (C,D,F,G).

Article Snippet: The following primary antibodies were used: mouse monoclonal α-actinin (Cytoskeleton), mouse monoclonal vinculin (Sigma), rabbit polyclonal NMII from bovine spleen , rabbit polyclonal mono- (Ser19) or double- (Thr18/Ser19) phosphorylated MRLC (Cell Signaling Technology, a gift from Dr. C. Chen, University of Pennsylvania).

Techniques: Fluorescence, Microscopy, Staining

(1) NMII activation : Inactive NMII molecules diffuse to lamellipodia, where they are activated by double phosphorylation of MRLC. (2) Focal complex formation: Active unpolymerized NMII molecules bind actin filaments in lamellipodia and undergo the retrograde flow with them. If two NMII heads bind different actin filaments, one of which is anchored to a nascent adhesion, the resulting strain stabilizes the nascent adhesion and promotes its transformation to a focal complex. Long filaments in filopodia can encounter more NMII molecules increasing a probability of focal complex formation under filopodial bundles. (3) Assembly of NMII filaments: NMII molecules pulling on actin filaments attached to focal complexes experience a greater load, which triggers tension-dependent NMII polymerization at these sites. (4) Stress fiber formation: Multivalent NMII filaments exert large forces sufficient to promote maturation of focal complexes to focal adhesions. They also cross-link and align disordered actin filaments into bundles producing stress fibers. However, additional events, such as recruitment of α-actinin, are needed for the formation of semi-sarcomeric pattern in stress fibers.

Journal: PLoS ONE

Article Title: Functions of Nonmuscle Myosin II in Assembly of the Cellular Contractile System

doi: 10.1371/journal.pone.0040814

Figure Lengend Snippet: (1) NMII activation : Inactive NMII molecules diffuse to lamellipodia, where they are activated by double phosphorylation of MRLC. (2) Focal complex formation: Active unpolymerized NMII molecules bind actin filaments in lamellipodia and undergo the retrograde flow with them. If two NMII heads bind different actin filaments, one of which is anchored to a nascent adhesion, the resulting strain stabilizes the nascent adhesion and promotes its transformation to a focal complex. Long filaments in filopodia can encounter more NMII molecules increasing a probability of focal complex formation under filopodial bundles. (3) Assembly of NMII filaments: NMII molecules pulling on actin filaments attached to focal complexes experience a greater load, which triggers tension-dependent NMII polymerization at these sites. (4) Stress fiber formation: Multivalent NMII filaments exert large forces sufficient to promote maturation of focal complexes to focal adhesions. They also cross-link and align disordered actin filaments into bundles producing stress fibers. However, additional events, such as recruitment of α-actinin, are needed for the formation of semi-sarcomeric pattern in stress fibers.

Article Snippet: The following primary antibodies were used: mouse monoclonal α-actinin (Cytoskeleton), mouse monoclonal vinculin (Sigma), rabbit polyclonal NMII from bovine spleen , rabbit polyclonal mono- (Ser19) or double- (Thr18/Ser19) phosphorylated MRLC (Cell Signaling Technology, a gift from Dr. C. Chen, University of Pennsylvania).

Techniques: Activation Assay, Transformation Assay

(A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and β-actin. Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.

Journal: Cancer research

Article Title: Loss of a negative feedback loop between IRF8 and AR promotes prostate cancer growth and enzalutamide resistance

doi: 10.1158/0008-5472.CAN-19-2549

Figure Lengend Snippet: (A, B) PC3 cells were co-transfected with AR plus IRF8 or AR plus vector control plasmid for 6h and treated with CHX (100 μg/mL) for the indicated time. Cell lysates were immunoblotted for AR, IRF8 and β-actin. Relative quantification was carried out for three biological replicates using β-actin as loading control. P-values were calculated using Student’s t test. ∗, p < 0.05; ∗∗, p < 0.01. (C) HEK293T cells were co-transfected with pIRF8, pAR or vector control for 48 h and incubated with CHX in the presence of proteasome inhibitor MG132 (10 μM), calpain inhibitors MG101 (10 μM), MG132 (0.1 μM), calpastatin (5 μM) or lysosomal inhibitor leupeptin (Leu, 50 μM) for 5 h, or DMSO as control. Cell lysates were analyzed for IRF-8 and β-actin expression. (D) Cells were cotransfected with the AR and control (pcDNA3.1) or IRF8 plasmids for 24 h, and treated with DMSO or MG132 (10 μM) for 5 h. Cell lysates were immunoblotted with the indicated antibodies. (E) Confocal microscopy for endogenous IRF8 and AR in LNCaP cells treated with DHT (10 nM) for 48 h. (F) Co-IP of IRF8 and AR in HEK293T cells co-transfected with pIRF8, pAR or vector control for 48 h. (G) Western blots were performed using indicated antibodies after IP of the full-length and truncated forms of AR from HEK293T WCL using the Flag antibody. (H) HEK293T cells were transfected with various combinations of pAR, pIRF8, and pFlag-Ub plasmids for 48 h. Cells were treated with MG132(10 μM) for 5 h, followed by nuclear and cytoplasmic protein lysate preparation and cytosolic protein were used for IP with an anti-AR antibody and IB with the indicated antibodies. (I) HEK293 cells were transfected with AR, IRF8, and WT, K48, or K63 ubiquitin (Ub) plasmids. Cells lysates were subjected to IP 48 h later with an anti-AR antibody followed by IB with an anti-HA antibody. (J) PC3 cells were first transfected with pcDNA3.1 or IRF8 for 12 h and then transfected again with HA-MDM2 or HA-MDM2 and AR for 48 h. The amount of plasmids was slightly adjusted to make the proteins expressed in similar level in different samples. Cell lysates were subjected to IP and followed by IB with the indicated antibodies.

Article Snippet: 30 μg total protein was separated by SDS-polyacrylamide gels and transferred to PVDF transfer membrane and the membranes were incubated with specific antibodies for IRF8 (ab28696, Abcam), AR (ab74272, Abcam), p-STAT1(Tyr701), p-STAT1 (Ser727), STAT1 (Cell Signaling Technology), β-actin (bsm-33036M, Bioss, China).

Techniques: Transfection, Plasmid Preparation, Incubation, Expressing, Confocal Microscopy, Co-Immunoprecipitation Assay, Western Blot

(A) Knockdown efficiency in LNCaP-shIRF8 cells determined by western blot. (B) Absorbance at 450 nm of LNCaP-shIRF8 cultured with 5% FBS (left panel), 5% CSS (middle panel), or 5% CSS containing 1 nM R1881 (right panel) in 96-well plates for 24–120 h. (C) Representative images of clone formation of LNCaP-shNC and LNCaP-shIRF8 cells cultured for 10 days. (D) Representative sphere formation of LNCaP-shNC and LNCaP-shIRF8 cells cultured for 14 days. (E, F) Knockdown of IRF8 in tumorigenesis. Tumour growth of LNCaP-shIRF8 cells in BALB/c nude mice (E, n=9), and in castrated BALB/c nude mice (F, n=9). (G) Representative images of IHC staining of PCNA in LNCaP-shIRF8 BALB/c xenografts. Scale bar, 100 μm. (H, I) OE of IRF8 in tumorigenesis. Proliferation (H) of 22RV1-IRF8 overexpression cells in vitro and tumour growth of 22RV1-IRF8 overexpression cells in vivo (I, n=9). (J) Western blot analysis for p-P38 MAPK, P38 MAPK, p-ERK, ERK, p-AKT(Thr308), p-AKT(Ser473), AKT, CD133, Oct3/4, and β-actin in LNCaP-shNC and LNCaP-shIRF8 cells.

Journal: Cancer research

Article Title: Loss of a negative feedback loop between IRF8 and AR promotes prostate cancer growth and enzalutamide resistance

doi: 10.1158/0008-5472.CAN-19-2549

Figure Lengend Snippet: (A) Knockdown efficiency in LNCaP-shIRF8 cells determined by western blot. (B) Absorbance at 450 nm of LNCaP-shIRF8 cultured with 5% FBS (left panel), 5% CSS (middle panel), or 5% CSS containing 1 nM R1881 (right panel) in 96-well plates for 24–120 h. (C) Representative images of clone formation of LNCaP-shNC and LNCaP-shIRF8 cells cultured for 10 days. (D) Representative sphere formation of LNCaP-shNC and LNCaP-shIRF8 cells cultured for 14 days. (E, F) Knockdown of IRF8 in tumorigenesis. Tumour growth of LNCaP-shIRF8 cells in BALB/c nude mice (E, n=9), and in castrated BALB/c nude mice (F, n=9). (G) Representative images of IHC staining of PCNA in LNCaP-shIRF8 BALB/c xenografts. Scale bar, 100 μm. (H, I) OE of IRF8 in tumorigenesis. Proliferation (H) of 22RV1-IRF8 overexpression cells in vitro and tumour growth of 22RV1-IRF8 overexpression cells in vivo (I, n=9). (J) Western blot analysis for p-P38 MAPK, P38 MAPK, p-ERK, ERK, p-AKT(Thr308), p-AKT(Ser473), AKT, CD133, Oct3/4, and β-actin in LNCaP-shNC and LNCaP-shIRF8 cells.

Article Snippet: 30 μg total protein was separated by SDS-polyacrylamide gels and transferred to PVDF transfer membrane and the membranes were incubated with specific antibodies for IRF8 (ab28696, Abcam), AR (ab74272, Abcam), p-STAT1(Tyr701), p-STAT1 (Ser727), STAT1 (Cell Signaling Technology), β-actin (bsm-33036M, Bioss, China).

Techniques: Western Blot, Cell Culture, Immunohistochemistry, Over Expression, In Vitro, In Vivo

(A) Western blot analysis for IRF8 and AR in the LNCaP-shIRF8 stable cell line for whole cell lysate (WCL), cytoplasm protein(Cyto), and nuclear protein(Nuc), β-actin, GAPDH, and lamin B were used as reference proteins, respectively. (B) Western blot analysis for IRF8 and AR in lysates of LNCaP cells or IRF8 and AR (AR full-length: ARfl and AR variants: ARvs) in 22RV1 cells 48 h after transfection with IRF8 plasmid (pIRF8) at various amounts (0.125–1 μg). (C) Western blot analysis of IRF8 and AR in HEK293T cells co-transfected with AR plasmid (0.3 μg) and different concentrations of IRF8 plasmid (0.125–1 μg) for 24 h and 48 h. (D) Western blot analysis of exogenous IRF8 and AR in PC3 cells transfected with AR plasmid (0.3 μg) and IRF8 plasmid (1 μg) alone or in combination for 48 h. (E) Western blot analysis of AR dimers under native polyacrylamide gel electrophoresis conditions in HEK293T cells transfected with pAR, pIRF8 and pFlag-Ub vector alone or in combination. (F) Western blot analysis of PSA, AR and IRF8 in LNCaP cells transfected with siRNA targeting IRF8 for 24 h. (G) Luciferase reporter assays for AR activity in IRF8-KD (LNCaP-shIRF8; left panels) and IRF8-OE (LNCaP-IRF8; right panels) LNCaP cells treated with DHT. ***p < 0.001 by one-way ANOVA.

Journal: Cancer research

Article Title: Loss of a negative feedback loop between IRF8 and AR promotes prostate cancer growth and enzalutamide resistance

doi: 10.1158/0008-5472.CAN-19-2549

Figure Lengend Snippet: (A) Western blot analysis for IRF8 and AR in the LNCaP-shIRF8 stable cell line for whole cell lysate (WCL), cytoplasm protein(Cyto), and nuclear protein(Nuc), β-actin, GAPDH, and lamin B were used as reference proteins, respectively. (B) Western blot analysis for IRF8 and AR in lysates of LNCaP cells or IRF8 and AR (AR full-length: ARfl and AR variants: ARvs) in 22RV1 cells 48 h after transfection with IRF8 plasmid (pIRF8) at various amounts (0.125–1 μg). (C) Western blot analysis of IRF8 and AR in HEK293T cells co-transfected with AR plasmid (0.3 μg) and different concentrations of IRF8 plasmid (0.125–1 μg) for 24 h and 48 h. (D) Western blot analysis of exogenous IRF8 and AR in PC3 cells transfected with AR plasmid (0.3 μg) and IRF8 plasmid (1 μg) alone or in combination for 48 h. (E) Western blot analysis of AR dimers under native polyacrylamide gel electrophoresis conditions in HEK293T cells transfected with pAR, pIRF8 and pFlag-Ub vector alone or in combination. (F) Western blot analysis of PSA, AR and IRF8 in LNCaP cells transfected with siRNA targeting IRF8 for 24 h. (G) Luciferase reporter assays for AR activity in IRF8-KD (LNCaP-shIRF8; left panels) and IRF8-OE (LNCaP-IRF8; right panels) LNCaP cells treated with DHT. ***p < 0.001 by one-way ANOVA.

Article Snippet: 30 μg total protein was separated by SDS-polyacrylamide gels and transferred to PVDF transfer membrane and the membranes were incubated with specific antibodies for IRF8 (ab28696, Abcam), AR (ab74272, Abcam), p-STAT1(Tyr701), p-STAT1 (Ser727), STAT1 (Cell Signaling Technology), β-actin (bsm-33036M, Bioss, China).

Techniques: Western Blot, Stable Transfection, Transfection, Plasmid Preparation, Polyacrylamide Gel Electrophoresis, Luciferase, Activity Assay