anti β actin monoclonal antibody  (Millipore)

 
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    Name:
    Monoclonal Anti beta Actin antibody
    Description:
    Actin is a highly conserved protein that is a major component of both the cytoskeletal and contractile structures in all cell types It varies in amount being related to the type of differentiation and to the functional state of cells and tissues Actin can be found in two different forms of aggregation the globular or the fibrillar state and at least six distinct isoforms occur in vertebrates The actins exhibit over 90 sequence homology but each isoform has a unique NH2 terminal sequence The isoforms are comprised of three α actins skeletal cardiac smooth one β actin β non muscle and two γ actins γ smooth muscle and γ non muscle ACTB actin β gene codes for β actin It is a cytoskeletal housekeeping protein It is present in the cytoplasm The ACTB gene is located on human chromosome 7p22 1 Monoclonal Anti β Actin mouse IgG2a isotype is derived from the AC 74 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse
    Catalog Number:
    a5316
    Price:
    None
    Applications:
    Western blot analysis of MDCK cell lysates were performed using monoclonal anti-actin antibody as a primary antibody.
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    Structured Review

    Millipore anti β actin monoclonal antibody
    Monoclonal Anti beta Actin antibody
    Actin is a highly conserved protein that is a major component of both the cytoskeletal and contractile structures in all cell types It varies in amount being related to the type of differentiation and to the functional state of cells and tissues Actin can be found in two different forms of aggregation the globular or the fibrillar state and at least six distinct isoforms occur in vertebrates The actins exhibit over 90 sequence homology but each isoform has a unique NH2 terminal sequence The isoforms are comprised of three α actins skeletal cardiac smooth one β actin β non muscle and two γ actins γ smooth muscle and γ non muscle ACTB actin β gene codes for β actin It is a cytoskeletal housekeeping protein It is present in the cytoplasm The ACTB gene is located on human chromosome 7p22 1 Monoclonal Anti β Actin mouse IgG2a isotype is derived from the AC 74 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse
    https://www.bioz.com/result/anti β actin monoclonal antibody/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti β actin monoclonal antibody - by Bioz Stars, 2021-03
    99/100 stars

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    Stripping Membranes:

    Article Title: Sustained adrenergic signaling leads to increased metastasis in ovarian cancer via increased PGE2 synthesis
    Article Snippet: Blots were washed and incubated with HRP-conjugated secondary antibody (GE Health Sciences, Pittsburgh, PA)) for an hour and developed using a chemiluminescent detection system (GE Health Sciences). .. Loading control beta-actin (A5316; Sigma Aldrich (St. Louis, MO)) was probed similarly after the blot was stripped using Restore Stripping Buffer (Pierce, Rockford, IL) .. Immunostaining Paraffin-embedded slides were deparaffinized, dehydrated, and rehydrated using a series of acetone and alcohol washes.

    other:

    Article Title: Mitochondrial peptides modulate mitochondrial function during cellular senescence
    Article Snippet: Anti-Tom20 antibody (Cat. #SC-17764; Santa Cruz Biotechnology, Dallas, Texas, USA), anti-glutaminase antibody (GLS; Cat. #701965; ThermoFisher Scientific, Wilmington, DE, USA), and anti-β-actin antibody (Cat. A5316; Sigma) were also used.

    Article Title: MLN4924 neddylation inhibitor promotes cell death in paclitaxel-resistant human lung adenocarcinoma cells
    Article Snippet: The antibody against β-actin was purchased from Sigma-Aldrich (Merck KGaA, Darmstadt, Germany, A5316).

    Plasmid Preparation:

    Article Title: A polymorphism in the lysyl oxidase propeptide domain accelerates carcinogen-induced cancer
    Article Snippet: The number of microscopic lesions (nodules and abnormal structures) in each group was counted under a microscope to further assess tumor development in response to DMBA treatment. .. Antibodies used were Ki-67 (cloneSP6; Thermo Scientific), LOX-PP (rabbit polyclonal IgG) used as described previously , β-actin (#A-5316; Sigma–Aldrich) and biotinylated goat anti-rabbit IgG (Vector). ..

    Chloramphenicol Acetyltransferase Assay:

    Article Title: A RUNX2-Mediated Epigenetic Regulation of the Survival of p53 Defective Cancer Cells
    Article Snippet: .. Antibodies We used the following antibodies for immunoblotting: RUNX2 (Cell Signaling, Cat:8486), p53 (DO1, Santa Cruz, Cat:sc-126), β-actin (Sigma, Cat:A5316), Cleaved PARP (Promega, Cat: G7341), Tubulin (Sigma, Cat: T3526), CBFB (Cell Signaling, Cat: 12902s), and MYC (Epitomics, Cat: 1472–1). .. We used the following antibodies for ChIP: RUNX2 (house made using recombinant RUNX2 fragments), Menin (Bethyl, Cat: A300-105A), CBFB (Bethyl, Cat: A303-549A), RNA polymerase II, N20 (Santa Cruz, Cat: sc-899), H3K4me3 (Abcam, Cat: ab8580-100), H3K79me2 (Abcam, Cat: ab3594-100).

    Western Blot:

    Article Title: Methylcytosine dioxygenase TET3 interacts with thyroid hormone nuclear receptors and stabilizes their association to chromatin
    Article Snippet: Luciferase assay was carried out as described ( ). .. Monoclonal anti-FLAG M2-Peroxidase (HRP) (A8592, Sigma), monoclonal anti–β-Actin (A5316, Sigma), anti-GFP (ab290, Abcam), anti–β-tubulin (ab6046, Abcam), anti-TRα1/β1 (SC-739, SantaCruz), anti-Histone3 (ab1791, Abcam), anti-Myc (ab9106, Abcam) and anti-Ubiquitin (Z0458, Dako and VU101, Life Sensor) were used for Western blot or coimmunoprecipitation. .. Chemicals used in this study include: 3,3′,5-Triiodo- l -thyronine sodium salt (T3, sigma), CHX (Calbiochem), MG132 (Calbiochem), E64D (Enzo Life Sciences).

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    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
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    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

    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

    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: 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

    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: 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

    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 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

    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: 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

    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: 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

    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, 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