anti β actin (Millipore)

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Millipore anti β actin
$siPRIM1-mediated effects on cell cycle progression in ATR s/s cells. (A) Cell cycle profile of DLD-1 ATR +/+ and ATR s/s cells 144 hours after siPRIM1 transfection as assessed by FACS analysis. (B) S-phase fraction of the cell cycle profile in detail. (C and D) Protein quantification in DLD-1 ATR +/+ and ATR s/s cells by immunoblotting 144 hours after siPRIM1 transfection. <t>β-Actin</t> was used as loading control. Percentage protein change of PRIM1 -depleted cells was normalized to NTC of DLD-1 ATR +/+ and ATR s/s cells. Error bars represent ±SEM of three independent experiments. Asterisks mark statistical significance using a two-tailed, unpaired Student's t test (* P$
Anti β Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti β actin/product/Millipore
Average 99 stars, based on 1 article reviews
Price from $9.99 to $1999.99

anti β actin - by Bioz Stars, 2021-03

99/100 stars

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1) Product Images from "Inactivation of PRIM1 Function Sensitizes Cancer Cells to ATR and CHK1 Inhibitors"

Article Title: Inactivation of PRIM1 Function Sensitizes Cancer Cells to ATR and CHK1 Inhibitors

Journal: Neoplasia (New York, N.Y.)

doi: 10.1016/j.neo.2018.08.009

$siPRIM1-mediated effects on cell cycle progression in ATR s/s cells. (A) Cell cycle profile of DLD-1 ATR +/+ and ATR s/s cells 144 hours after siPRIM1 transfection as assessed by FACS analysis. (B) S-phase fraction of the cell cycle profile in detail. (C and D) Protein quantification in DLD-1 ATR +/+ and ATR s/s cells by immunoblotting 144 hours after siPRIM1 transfection. β-Actin was used as loading control. Percentage protein change of PRIM1 -depleted cells was normalized to NTC of DLD-1 ATR +/+ and ATR s/s cells. Error bars represent ±SEM of three independent experiments. Asterisks mark statistical significance using a two-tailed, unpaired Student's t test (* P$
Figure Legend Snippet: siPRIM1-mediated effects on cell cycle progression in ATR s/s cells. (A) Cell cycle profile of DLD-1 ATR +/+ and ATR s/s cells 144 hours after siPRIM1 transfection as assessed by FACS analysis. (B) S-phase fraction of the cell cycle profile in detail. (C and D) Protein quantification in DLD-1 ATR +/+ and ATR s/s cells by immunoblotting 144 hours after siPRIM1 transfection. β-Actin was used as loading control. Percentage protein change of PRIM1 -depleted cells was normalized to NTC of DLD-1 ATR +/+ and ATR s/s cells. Error bars represent ±SEM of three independent experiments. Asterisks mark statistical significance using a two-tailed, unpaired Student's t test (* P

Techniques Used: Transfection, FACS, Two Tailed Test

siPRIM1-mediated sensitization of DLD-1 cells to ATR and CHK1 inhibitors. (A) Knockdown efficiency of PRIM1 via siRNA was confirmed by immunoblotting 96 hours after transfection. β-Actin was used as loading control. (B) Effects of ATR inhibitors, (C) CHK1 inhibitors, and (D) common chemotherapeutics on the proliferation of PRIM1 -depleted DLD-1 cells as compared to control and mock-transfected cells measured 120 hours after drug treatment. Error bars represent ±SEM of three independent experiments with each data point reflecting triplicate wells. Asterisks mark statistical significance using a two-tailed, unpaired Student's t test (* P

Figure Legend Snippet: siPRIM1-mediated sensitization of DLD-1 cells to ATR and CHK1 inhibitors. (A) Knockdown efficiency of PRIM1 via siRNA was confirmed by immunoblotting 96 hours after transfection. β-Actin was used as loading control. (B) Effects of ATR inhibitors, (C) CHK1 inhibitors, and (D) common chemotherapeutics on the proliferation of PRIM1 -depleted DLD-1 cells as compared to control and mock-transfected cells measured 120 hours after drug treatment. Error bars represent ±SEM of three independent experiments with each data point reflecting triplicate wells. Asterisks mark statistical significance using a two-tailed, unpaired Student's t test (* P

Techniques Used: Transfection, Two Tailed Test

Verification of synthetic lethality between ATR and PRIM1 . (A) Quantification of ATR protein in DLD-1 ATR +/+ , ATR s/s , and ATR resc cells by immunoblotting. β-Actin was used as loading control. (B) MMC sensitivity was assessed 120 hours after treatment by proliferation assay in DLD-1 ATR +/+ , ATR s/s , and ATR resc cells. (C) Quantification of siRNA-mediated PRIM1 depletion (10 nM) 120 hours after transfection by immunoblotting. β-Actin was used as loading control. (D) Proliferation inhibition was assessed 144 hours after transfection by proliferation assay in DLD-1 ATR +/+ , ATR s/s , and ATR resc cells. Error bars represent ±SEM of three independent experiments with each data point reflecting triplicate wells. Asterisks mark statistical significance using a two-tailed, unpaired Student's t test (* P

Figure Legend Snippet: Verification of synthetic lethality between ATR and PRIM1 . (A) Quantification of ATR protein in DLD-1 ATR +/+ , ATR s/s , and ATR resc cells by immunoblotting. β-Actin was used as loading control. (B) MMC sensitivity was assessed 120 hours after treatment by proliferation assay in DLD-1 ATR +/+ , ATR s/s , and ATR resc cells. (C) Quantification of siRNA-mediated PRIM1 depletion (10 nM) 120 hours after transfection by immunoblotting. β-Actin was used as loading control. (D) Proliferation inhibition was assessed 144 hours after transfection by proliferation assay in DLD-1 ATR +/+ , ATR s/s , and ATR resc cells. Error bars represent ±SEM of three independent experiments with each data point reflecting triplicate wells. Asterisks mark statistical significance using a two-tailed, unpaired Student's t test (* P

Techniques Used: Proliferation Assay, Transfection, Inhibition, Two Tailed Test

siPRIM1-mediated sensitization to ATR and CHK1 inhibitors in a panel of different cancer cell lines. (A) Knockdown efficiency of PRIM1 via siRNA was confirmed by immunoblotting 96 hours after transfection. β-Actin was used as loading control. (B) Effects of ATR and (C) CHK1 inhibitors on the proliferation of PRIM1 -depleted SW480, RKO, and PaTu 8988t cells as compared to control and mock-transfected cells measured 120 hours after drug treatment. Error bars represent ±SEM of at least three independent experiments with each data point reflecting triplicate wells. Asterisks mark statistical significance using a two-tailed, unpaired Student's t test (* P

Figure Legend Snippet: siPRIM1-mediated sensitization to ATR and CHK1 inhibitors in a panel of different cancer cell lines. (A) Knockdown efficiency of PRIM1 via siRNA was confirmed by immunoblotting 96 hours after transfection. β-Actin was used as loading control. (B) Effects of ATR and (C) CHK1 inhibitors on the proliferation of PRIM1 -depleted SW480, RKO, and PaTu 8988t cells as compared to control and mock-transfected cells measured 120 hours after drug treatment. Error bars represent ±SEM of at least three independent experiments with each data point reflecting triplicate wells. Asterisks mark statistical significance using a two-tailed, unpaired Student's t test (* P

Techniques Used: Transfection, Two Tailed Test

Incubation:

Article Title: Apolipoprotein E is an HIV-1-inducible inhibitor of viral production and infectivity in macrophages
Article Snippet: Supernatants from these lysates were subjected to SDS-polyacrylamide gel electrophoresis and transferred to Immobilon-P PVDF transfer membranes. .. The membranes were then incubated with the following primary antibodies: anti-ApoE (EP1347Y; Abcam), anti-apolipoprotein B (AB742; EMD Millipore), anti-HIV-1 p24 rabbit polyclonal antibody (65–004; Bioacademia, Japan), anti-HIV-1 p24 mouse monoclonal antibody (A2-851-100; Icosagen, Estonia), anti-HIV-1 Env (KD-247) [ ], anti-VSV Glycoprotein (P5D4; Sigma), anti-HA (HA-7; Sigma), and anti- β -actin (AC-15; Sigma). .. After the incubation with HRP-labeled secondary antibodies, proteins were visualized using Western Lightning Plus-ECL (PerkinElmer) and an Amersham Imager 600 imaging system (GE Healthcare).

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mouse anti β actin (Millipore)

Millipore mouse anti β actin

K562 cells with ectopic HD5 expression. (A) Screening of cell lines for endogenous HD5 expression. HD5 mRNA levels were measured in total cellular RNA by qRT-PCR and expressed as percentages of <t>β-actin</t> (Act B) mRNA levels. (B) HD5 mRNA expression

Mouse Anti β Actin, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mouse anti β actin/product/Millipore
Average 97 stars, based on 1 article reviews
Price from $9.99 to $1999.99

mouse anti β actin - by Bioz Stars, 2021-03

97/100 stars

Buy from Supplier

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Journal: Journal of Virology

Article Title: Studies on the Interaction of Tumor-Derived HD5 Alpha Defensins with Adenoviruses and Implications for Oncolytic Adenovirus Therapy

doi: 10.1128/JVI.02030-16

Figure Lengend Snippet: K562 cells with ectopic HD5 expression. (A) Screening of cell lines for endogenous HD5 expression. HD5 mRNA levels were measured in total cellular RNA by qRT-PCR and expressed as percentages of β-actin (Act B) mRNA levels. (B) HD5 mRNA expression

Article Snippet: After blots were stripped with Restore Western blot striping buffer (Thermo Scientific, Waltham, MA), they were incubated with mouse anti-β-actin (Sigma, St. Louis, MO) (1:5,000).

Techniques: Expressing, Quantitative RT-PCR, Activated Clotting Time Assay

ShRNA plasmid design and in vitro LGI1-shRNA downregulation. A) shRNA construct: LGI1-shRNA is under the promoter mU6 (murine U6 small-non-coding-RNA), meanwhile the EGFP (enhanced green fluorescent protein) is under the independent promoter PGK (phosphoglycerate kinase). NeoR/KanR (Neomycin/Kanamycin Resistance). B) LGI1 expression in neuronal cultures. The first lane is the endogenous level of LGI1 in untreated primary cultures, the second lane shows the levels of LGI1 in cultures transduced with scramble virus and the fourth and last lane shows the levels of LGI1 in cultures transduced with shRNA-LGI1. The β-actin and EGFP signals are also shown. EGFP intensity was detected to evaluate that the reporter gene was also expressed at the same time as the shRNA and hence could be a reliable source of transduction rate. C) Quantification of LGI1 concentrations detected by the western blot method. p=0.005 two-tailed Student’s t-test (blots n=5 from 5 distinct preparations).

Journal: bioRxiv

Article Title: LGI1 downregulation increases neuronal circuit excitability

doi: 10.1101/2019.12.17.879833

Figure Lengend Snippet: ShRNA plasmid design and in vitro LGI1-shRNA downregulation. A) shRNA construct: LGI1-shRNA is under the promoter mU6 (murine U6 small-non-coding-RNA), meanwhile the EGFP (enhanced green fluorescent protein) is under the independent promoter PGK (phosphoglycerate kinase). NeoR/KanR (Neomycin/Kanamycin Resistance). B) LGI1 expression in neuronal cultures. The first lane is the endogenous level of LGI1 in untreated primary cultures, the second lane shows the levels of LGI1 in cultures transduced with scramble virus and the fourth and last lane shows the levels of LGI1 in cultures transduced with shRNA-LGI1. The β-actin and EGFP signals are also shown. EGFP intensity was detected to evaluate that the reporter gene was also expressed at the same time as the shRNA and hence could be a reliable source of transduction rate. C) Quantification of LGI1 concentrations detected by the western blot method. p=0.005 two-tailed Student’s t-test (blots n=5 from 5 distinct preparations).

Article Snippet: The following antibodies and dilutions were used: 1:250 polyclonal goat-anti-LGI1 (Santa Cruz, c-19), 1:4000 monoclonal mouse-anti β-actin (Sigma), 1:1000 rabbit-anti-GFP (Abcam ab6556).

Techniques: shRNA, Plasmid Preparation, In Vitro, Construct, Expressing, Transduction, Western Blot, Two Tailed Test

Effects of various concentrations of the resveratrol on KGN cells. Cells were incubated with resveratrol at 0, 10, 25, 50, and 100 μmol/L for 24 h. A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

Journal: Reproductive Medicine and Biology

Article Title: Resveratrol protects mitochondrial quantity by activating SIRT1/PGC‐1α expression during ovarian hypoxia, et al. Resveratrol protects mitochondrial quantity by activating SIRT1/PGC‐1α expression during ovarian hypoxia

doi: 10.1002/rmb2.12323

Figure Lengend Snippet: Effects of various concentrations of the resveratrol on KGN cells. Cells were incubated with resveratrol at 0, 10, 25, 50, and 100 μmol/L for 24 h. A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

Article Snippet: Blots were then incubated for 1 hour at room temperature (25°C) with rabbit monoclonal SIRT1 antibody (1:400; Santa Cruz Biotechnology, Inc), rabbit monoclonal HIF‐1a antibody (1:1000; Epitomics), or mouse monoclonal β‐actin antibody (1:5000; Sigma‐Aldrich) as the primary antibody, and anti‐rabbit immunoglobulin IgG peroxidase‐labeled secondary antibody (1:10 000; GE Healthcare Life Science) or anti‐mouse IgG peroxidase‐labeled secondary antibody (1:10 000; GE Healthcare Life Science) as the secondary antibody.

Techniques: Incubation, Real-time Polymerase Chain Reaction, Western Blot, Enzyme-linked Immunosorbent Assay

Protective effects of resveratrol against CoCl 2 ‐induced hypoxic stress. KGN cells were cultured in medium containing 100 μmol/L CoCl 2 with or without the 50 μmol/L resveratrol. A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control protein. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

Journal: Reproductive Medicine and Biology

doi: 10.1002/rmb2.12323

Figure Lengend Snippet: Protective effects of resveratrol against CoCl 2 ‐induced hypoxic stress. KGN cells were cultured in medium containing 100 μmol/L CoCl 2 with or without the 50 μmol/L resveratrol. A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control protein. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

Techniques: Cell Culture, Real-time Polymerase Chain Reaction, Western Blot, Enzyme-linked Immunosorbent Assay

Effects of CoCl 2 ‐induced hypoxic stress on mRNA expression and protein secretion. KGN cells were incubated for 24 h in medium containing with 10 μmol/L or 100 μmol/L CoCl 2 . A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

Journal: Reproductive Medicine and Biology

doi: 10.1002/rmb2.12323

Figure Lengend Snippet: Effects of CoCl 2 ‐induced hypoxic stress on mRNA expression and protein secretion. KGN cells were incubated for 24 h in medium containing with 10 μmol/L or 100 μmol/L CoCl 2 . A, SIRT1 mRNA levels were assessed by real‐time PCR and calculated after normalization to EF1α mRNA levels. B, The protein levels of SIRT1 were quantified by Western blotting, and β‐actin was used as the control. C, The protein levels were quantified using ImageJ. D, VEGF protein levels were analyzed by ELISA. E, The mtDNA copy number was determined using real‐time PCR. Fold differences are shown compared with the control, for which the value was defined as 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

Techniques: Expressing, Incubation, Real-time Polymerase Chain Reaction, Western Blot, Enzyme-linked Immunosorbent Assay

Effect of resveratrol on HIF‐1α. KGN cells were incubated for 24 h in medium containing 100 μmol/L CoCl 2 with or without 50 μmol/L resveratrol (n = 3). A, The expression of HIF‐1α was quantified by Western blotting. The levels of HIF‐1α were normalized to levels of β‐actin (n = 3). B, The protein levels were quantified using ImageJ. C, VEGF protein levels were analyzed by ELISA. Fold differences are shown compared with the control, for which the value was defined 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

Journal: Reproductive Medicine and Biology

doi: 10.1002/rmb2.12323

Figure Lengend Snippet: Effect of resveratrol on HIF‐1α. KGN cells were incubated for 24 h in medium containing 100 μmol/L CoCl 2 with or without 50 μmol/L resveratrol (n = 3). A, The expression of HIF‐1α was quantified by Western blotting. The levels of HIF‐1α were normalized to levels of β‐actin (n = 3). B, The protein levels were quantified using ImageJ. C, VEGF protein levels were analyzed by ELISA. Fold differences are shown compared with the control, for which the value was defined 1.0. The data are presented as the mean ± SEM, n = 3. Statistically significant differences are indicated by brackets: * P

Techniques: Incubation, Expressing, Western Blot, Enzyme-linked Immunosorbent Assay

Temporal changes in synaptic plasticity-related signals in the mouse hippocampus following methotrexate (MTX) administration. (A) N-methyl-D-aspartic acid receptor 1 (NMDAR1). (B) Calcium/calmodulin-dependent protein kinase II (CaMKII). (C) Extracellular signal-regulated kinase 1/2 (ERK1/2). (D) cAMP responsive element-binding protein (CREB). (E) Glutamate receptor 1 (GluR1). The relative expression levels of phosphorylated (P) and total (T) forms were determined by densitometry and normalized to β-actin signals. Furthermore, to examine the activation levels of each signal, the relative levels of the P forms were normalized to their T-forms. Data are reported as mean ± SEM of three mice per time point. Values for protein expression levels from the hippocampus of vehicle-treated controls were arbitrarily defined as 1 (bar graphs). a P

Journal: Neural Regeneration Research

Article Title: Temporal profiles of synaptic plasticity-related signals in adult mouse hippocampus with methotrexate treatment ☆

doi: 10.3969/j.issn.1673-5374.2012.21.008

Figure Lengend Snippet: Temporal changes in synaptic plasticity-related signals in the mouse hippocampus following methotrexate (MTX) administration. (A) N-methyl-D-aspartic acid receptor 1 (NMDAR1). (B) Calcium/calmodulin-dependent protein kinase II (CaMKII). (C) Extracellular signal-regulated kinase 1/2 (ERK1/2). (D) cAMP responsive element-binding protein (CREB). (E) Glutamate receptor 1 (GluR1). The relative expression levels of phosphorylated (P) and total (T) forms were determined by densitometry and normalized to β-actin signals. Furthermore, to examine the activation levels of each signal, the relative levels of the P forms were normalized to their T-forms. Data are reported as mean ± SEM of three mice per time point. Values for protein expression levels from the hippocampus of vehicle-treated controls were arbitrarily defined as 1 (bar graphs). a P

Article Snippet: Membranes were stripped and re-probed with a mouse monoclonal anti-β-actin (1:20 000; Sigma-Aldrich) for normalization.

Techniques: Binding Assay, Expressing, Activation Assay, Mouse Assay

Time-response changes of neurotrophic factors in the mouse hippocampus following administration of methotrexate (MTX). (A) Brain-derived neurotrophic factor (BDNF). (B) Glial cell line-derived neurotrophic factor (GDNF). The relative expression levels of proteins were determined by densitometry and normalized to β-actin signals. Data are reported as mean ± SEM. n = 3 mice per time point. Values for protein expression levels from the hippocampus of vehicle-treated controls (Cont) were arbitrarily defined as 1 (bar graphs). a P

Journal: Neural Regeneration Research

Article Title: Temporal profiles of synaptic plasticity-related signals in adult mouse hippocampus with methotrexate treatment ☆

doi: 10.3969/j.issn.1673-5374.2012.21.008

Figure Lengend Snippet: Time-response changes of neurotrophic factors in the mouse hippocampus following administration of methotrexate (MTX). (A) Brain-derived neurotrophic factor (BDNF). (B) Glial cell line-derived neurotrophic factor (GDNF). The relative expression levels of proteins were determined by densitometry and normalized to β-actin signals. Data are reported as mean ± SEM. n = 3 mice per time point. Values for protein expression levels from the hippocampus of vehicle-treated controls (Cont) were arbitrarily defined as 1 (bar graphs). a P

Article Snippet: Membranes were stripped and re-probed with a mouse monoclonal anti-β-actin (1:20 000; Sigma-Aldrich) for normalization.

Techniques: Derivative Assay, Expressing, Mouse Assay

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1) Product Images from "Inactivation of PRIM1 Function Sensitizes Cancer Cells to ATR and CHK1 Inhibitors"

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