anti β actin  (Abcam)

 
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    Name:
    Anti beta Actin antibody
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    ab16039
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    Structured Review

    Abcam anti β actin
    Chronic hypoxia (CH) increases phosphorylated (p-)cofilin and cofilin protein levels but not the p-cofilin-to-cofilin ratio. Western blots were performed on unfractionated lysates of intrapulmonary arteries from control (Con) and CH rats, and p-cofilin and cofilin protein levels were quantified by band intensity and normalized to <t>β-actin</t> protein expression. A : representative blots showing p-cofilin, cofilin, and β-actin levels in control and CH lysates under vehicle (Veh) and endothelin-1 (ET-1)-treated conditions. B : p-cofilin-to-cofilin ratio. SMIFH2, small-molecule inhibitor of formin homology domain 2; CytB, cytochalasin B. C : p-cofilin/β-actin. D : cofilin/β-actin levels. n = 6–9/group. * P

    https://www.bioz.com/result/anti β actin/product/Abcam
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti β actin - by Bioz Stars, 2021-03
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    Images

    1) Product Images from "Actin polymerization contributes to enhanced pulmonary vasoconstrictor reactivity after chronic hypoxia"

    Article Title: Actin polymerization contributes to enhanced pulmonary vasoconstrictor reactivity after chronic hypoxia

    Journal: American Journal of Physiology - Heart and Circulatory Physiology

    doi: 10.1152/ajpheart.00664.2017

    Chronic hypoxia (CH) increases phosphorylated (p-)cofilin and cofilin protein levels but not the p-cofilin-to-cofilin ratio. Western blots were performed on unfractionated lysates of intrapulmonary arteries from control (Con) and CH rats, and p-cofilin and cofilin protein levels were quantified by band intensity and normalized to β-actin protein expression. A : representative blots showing p-cofilin, cofilin, and β-actin levels in control and CH lysates under vehicle (Veh) and endothelin-1 (ET-1)-treated conditions. B : p-cofilin-to-cofilin ratio. SMIFH2, small-molecule inhibitor of formin homology domain 2; CytB, cytochalasin B. C : p-cofilin/β-actin. D : cofilin/β-actin levels. n = 6–9/group. * P
    Figure Legend Snippet: Chronic hypoxia (CH) increases phosphorylated (p-)cofilin and cofilin protein levels but not the p-cofilin-to-cofilin ratio. Western blots were performed on unfractionated lysates of intrapulmonary arteries from control (Con) and CH rats, and p-cofilin and cofilin protein levels were quantified by band intensity and normalized to β-actin protein expression. A : representative blots showing p-cofilin, cofilin, and β-actin levels in control and CH lysates under vehicle (Veh) and endothelin-1 (ET-1)-treated conditions. B : p-cofilin-to-cofilin ratio. SMIFH2, small-molecule inhibitor of formin homology domain 2; CytB, cytochalasin B. C : p-cofilin/β-actin. D : cofilin/β-actin levels. n = 6–9/group. * P

    Techniques Used: Western Blot, Expressing

    2) Product Images from "Optimization of Ultrasound-mediated Anti-angiogenic Cancer Gene Therapy"

    Article Title: Optimization of Ultrasound-mediated Anti-angiogenic Cancer Gene Therapy

    Journal: Molecular Therapy. Nucleic Acids

    doi: 10.1038/mtna.2013.20

    Endogenous VEGFR2 protein expression in tumor tissue for all treatment groups . ( a ) Relative intensity of VEGFR2 protein in all the groups normalized to internal control β-actin levels. VEGFR2 protein levels were reduced in all the treatment groups, with maximal reduction observed at PI-10 seconds. ( b ) Gradual decrease in VEGFR2 protein levels as developed on X-ray film in all treatment groups with no significant reduction in control, scrambled, and plasmid IV groups ( # P
    Figure Legend Snippet: Endogenous VEGFR2 protein expression in tumor tissue for all treatment groups . ( a ) Relative intensity of VEGFR2 protein in all the groups normalized to internal control β-actin levels. VEGFR2 protein levels were reduced in all the treatment groups, with maximal reduction observed at PI-10 seconds. ( b ) Gradual decrease in VEGFR2 protein levels as developed on X-ray film in all treatment groups with no significant reduction in control, scrambled, and plasmid IV groups ( # P

    Techniques Used: Expressing, Plasmid Preparation

    3) Product Images from "Identification of a Redox-Modulatory Interaction Between Uncoupling Protein 3 and Thioredoxin 2 in the Mitochondrial Intermembrane Space"

    Article Title: Identification of a Redox-Modulatory Interaction Between Uncoupling Protein 3 and Thioredoxin 2 in the Mitochondrial Intermembrane Space

    Journal: Antioxidants & Redox Signaling

    doi: 10.1089/ars.2011.3888

    Effects of UCP3 on mitochondrial superoxide and H 2 O 2 production. (A) C2C12 myoblasts were stably infected with FG9-mock and -UCP3 lentivirus. Cell extracts (20 μg/lane) were subjected to SDS-PAGE followed by immunoblotting (IB) with anti-UCP3 and anti-β-actin antibodies. The ratio of UCP3 to β-actin was calculated by densitometric analysis. (B) Mock and UCP3-infected C2C12 myoblasts were assayed for membrane potential by flow cytometry using the fluorescent dye TMRM. (C) The rate of superoxide from mock- and UCP3-infected C2C12 myoblastic cells was assessed by dihydroethidium (DHE) fluorescence. Succinate and antimycin A were used as respiratory complex II substrate and complex III inhibitors, respectively. (D) The rate of H 2 O 2 production from isolated mitochondria in mock- and UCP3-infected C2C12 myoblastic cells was assessed by Amplex Red fluorescence. Succinate and pyruvate/malate were used as respiratory substrates. Rotenone was used as a complex I inhibitor. For ROS production experiments, means±SD from three independent experiments performed in duplicate are shown. * p
    Figure Legend Snippet: Effects of UCP3 on mitochondrial superoxide and H 2 O 2 production. (A) C2C12 myoblasts were stably infected with FG9-mock and -UCP3 lentivirus. Cell extracts (20 μg/lane) were subjected to SDS-PAGE followed by immunoblotting (IB) with anti-UCP3 and anti-β-actin antibodies. The ratio of UCP3 to β-actin was calculated by densitometric analysis. (B) Mock and UCP3-infected C2C12 myoblasts were assayed for membrane potential by flow cytometry using the fluorescent dye TMRM. (C) The rate of superoxide from mock- and UCP3-infected C2C12 myoblastic cells was assessed by dihydroethidium (DHE) fluorescence. Succinate and antimycin A were used as respiratory complex II substrate and complex III inhibitors, respectively. (D) The rate of H 2 O 2 production from isolated mitochondria in mock- and UCP3-infected C2C12 myoblastic cells was assessed by Amplex Red fluorescence. Succinate and pyruvate/malate were used as respiratory substrates. Rotenone was used as a complex I inhibitor. For ROS production experiments, means±SD from three independent experiments performed in duplicate are shown. * p

    Techniques Used: Stable Transfection, Infection, SDS Page, Flow Cytometry, Cytometry, Fluorescence, Isolation

    Effects of Trx2 active site mutations and oxidative stress on the interaction of UCP3 and Trx2. (A and B) HeLa cells were transfected with mock, UCP3-V5, Trx2-myc, C90STrx2-myc, C93STrx2-myc, or the double active site mutant (C90, 93S Trx2-myc) as indicated. Cells extracts (100 μg) were immunoprecipitated (IP) with anti-myc and anti-V5 antibodies and analyzed by immunoblotting (IB) with anti-V5 and anti-myc antibodies, respectively. (C and D) Cells transfected with UCP3-V5 and Trx2-myc were treated with hydrogen peroxide (H 2 O 2 ) (0.5 m M ) for 0–120 min (C) or 0.1 m M H 2 O 2 for 120 min (D) and cells were immnoprecipitated (IP) with anti-V5 antibodies and analyzed by IB with anti-myc antibodies. Equal protein loading was determined by immunoblotting for β-actin. N, nonprocessed Trx2; P, processed Trx2. IB, IP experiments are representative of at least three independent studies.
    Figure Legend Snippet: Effects of Trx2 active site mutations and oxidative stress on the interaction of UCP3 and Trx2. (A and B) HeLa cells were transfected with mock, UCP3-V5, Trx2-myc, C90STrx2-myc, C93STrx2-myc, or the double active site mutant (C90, 93S Trx2-myc) as indicated. Cells extracts (100 μg) were immunoprecipitated (IP) with anti-myc and anti-V5 antibodies and analyzed by immunoblotting (IB) with anti-V5 and anti-myc antibodies, respectively. (C and D) Cells transfected with UCP3-V5 and Trx2-myc were treated with hydrogen peroxide (H 2 O 2 ) (0.5 m M ) for 0–120 min (C) or 0.1 m M H 2 O 2 for 120 min (D) and cells were immnoprecipitated (IP) with anti-V5 antibodies and analyzed by IB with anti-myc antibodies. Equal protein loading was determined by immunoblotting for β-actin. N, nonprocessed Trx2; P, processed Trx2. IB, IP experiments are representative of at least three independent studies.

    Techniques Used: Transfection, Mutagenesis, Immunoprecipitation

    Interaction of UCP3 and thioredoxin 2 (Trx2). (A) Trx2 was identified as a UCP3 interacting partner by yeast two-hybrid analysis. The coding sequences for the hydrophilic amino acid residues 1–16 of the UCP3 gene were cloned into the pGBKT7 vector and used as bait. With a heart cDNA library used as prey, three potential UCP3 binding candidates were identified by yeast growth, with the arrow representing the Trx2-positive colony. (B) HeLa cells were transfected with empty vector (mock), myc-tagged Trx2 (Trx2-myc), and myc-tagged Trx2 with a truncated MTS (ΔMTS Trx2-myc). Cell extracts (20 μg/lane) were subjected to SDS-PAGE, followed by immunoblotting (IB) with anti-myc, anti-Trx2, and anti-β-actin antibodies. N, nonprocessed Trx2; P, processed Trx2. (C and D) HeLa (C) and C2C12 (D) cell extracts (100 μg) transfected with Mock, Trx2-myc, and V5-tagged UCP3 (UCP3-V5) were immunoprecipitated (IP) with anti-IgG, anti-myc, or anti-V5 antibodies and analyzed by immunoblotting to detect V5 (UCP3) and myc (Trx2). β-Actin was used as an internal standard. WCE, whole cell extracts. *indicates the nonspecific IgG band on the immunoblot. (E) HeLa cells transfected with UCP3-V5 ( top ) or Trx2-myc ( middle ) were immunostained with V5 ( green ) or myc ( green ) antibodies and co-stained with the mitochondrial indicator MitoTracker Red ( red ), as indicated. HeLa cells cotransfected with UCP3-V5 and Trx2-myc ( bottom ) were co-immunostained with V5 ( red ) and myc ( green ).
    Figure Legend Snippet: Interaction of UCP3 and thioredoxin 2 (Trx2). (A) Trx2 was identified as a UCP3 interacting partner by yeast two-hybrid analysis. The coding sequences for the hydrophilic amino acid residues 1–16 of the UCP3 gene were cloned into the pGBKT7 vector and used as bait. With a heart cDNA library used as prey, three potential UCP3 binding candidates were identified by yeast growth, with the arrow representing the Trx2-positive colony. (B) HeLa cells were transfected with empty vector (mock), myc-tagged Trx2 (Trx2-myc), and myc-tagged Trx2 with a truncated MTS (ΔMTS Trx2-myc). Cell extracts (20 μg/lane) were subjected to SDS-PAGE, followed by immunoblotting (IB) with anti-myc, anti-Trx2, and anti-β-actin antibodies. N, nonprocessed Trx2; P, processed Trx2. (C and D) HeLa (C) and C2C12 (D) cell extracts (100 μg) transfected with Mock, Trx2-myc, and V5-tagged UCP3 (UCP3-V5) were immunoprecipitated (IP) with anti-IgG, anti-myc, or anti-V5 antibodies and analyzed by immunoblotting to detect V5 (UCP3) and myc (Trx2). β-Actin was used as an internal standard. WCE, whole cell extracts. *indicates the nonspecific IgG band on the immunoblot. (E) HeLa cells transfected with UCP3-V5 ( top ) or Trx2-myc ( middle ) were immunostained with V5 ( green ) or myc ( green ) antibodies and co-stained with the mitochondrial indicator MitoTracker Red ( red ), as indicated. HeLa cells cotransfected with UCP3-V5 and Trx2-myc ( bottom ) were co-immunostained with V5 ( red ) and myc ( green ).

    Techniques Used: Clone Assay, Plasmid Preparation, cDNA Library Assay, Binding Assay, Transfection, SDS Page, Immunoprecipitation, Staining

    Submitochondrial localization of the UCP3/Trx2 interaction. (A) Mitochondria isolated from HeLa cells transfected with UCP3 and Trx2 were suspended in RIPA buffer+SDS or lysis buffer+Triton X-100, respectively. Mitochondrial pellets and supernatants were subjected to SDS-PAGE followed by immunoblotting (IB) with anti-myc, anti-V5, anti-COX4, and anti-DNA polymerase γ (DPγ) antibodies. PPT, mitochondrial pellet after centrifugation; SDS, RIPA buffer; SUP, supernatant after centrifugation; Triton X-100; lysis buffer. (B) . Mitochondrial pellets and supernatants were resuspended in SDS-PAGE buffer, and then loaded onto an SDS-PAGE gel. Immunoblots show the presence of the intermembrane space (IMS) resident Smac and the matrix resident HSP60 in mitochondria that were untreated or treated with proteinase K (Pro K) (lanes 2–7) and increasing concentrations of digitonin (DIG) (lanes 3–7, 0.1 to 0.7 mg/ml DIG). (C) N (VN)- and C (VC)- terminal fragments of Venus fluorescent proteins were fused to the C-terminus of UCP3 (resides 1–308) (UCP3-VN) or ΔCUCP3 (residues1–234) (ΔCUCP3-VN), and the C-terminus of Trx2, respectively. The fragments of fluorescent proteins of belonging to UCP3-VN and ΔCUCP3-VN were localized to the mitochondrial IMS and matrix, respectively. (D) HeLa cells were transfected with UCP3-VN, Trx2-VC, ΔCUCP3-VN and Trx2-VC, and UCP3-VN and Trx2-VC. Cell extracts (100 μg) were immunoprecipitated (IP) with anti-myc antibodies and analyzed by IB to detect V5 (UCP3) and myc (Trx2). β-Actin was used as an internal standard. (E) Fluorescent images of HeLa cells transfected with UCP3-VN, Trx2-VC, ΔCUCP3-VN and Trx2-VC, and UCP3-VN and Trx2-VC as indicated in each panel. (F) ).
    Figure Legend Snippet: Submitochondrial localization of the UCP3/Trx2 interaction. (A) Mitochondria isolated from HeLa cells transfected with UCP3 and Trx2 were suspended in RIPA buffer+SDS or lysis buffer+Triton X-100, respectively. Mitochondrial pellets and supernatants were subjected to SDS-PAGE followed by immunoblotting (IB) with anti-myc, anti-V5, anti-COX4, and anti-DNA polymerase γ (DPγ) antibodies. PPT, mitochondrial pellet after centrifugation; SDS, RIPA buffer; SUP, supernatant after centrifugation; Triton X-100; lysis buffer. (B) . Mitochondrial pellets and supernatants were resuspended in SDS-PAGE buffer, and then loaded onto an SDS-PAGE gel. Immunoblots show the presence of the intermembrane space (IMS) resident Smac and the matrix resident HSP60 in mitochondria that were untreated or treated with proteinase K (Pro K) (lanes 2–7) and increasing concentrations of digitonin (DIG) (lanes 3–7, 0.1 to 0.7 mg/ml DIG). (C) N (VN)- and C (VC)- terminal fragments of Venus fluorescent proteins were fused to the C-terminus of UCP3 (resides 1–308) (UCP3-VN) or ΔCUCP3 (residues1–234) (ΔCUCP3-VN), and the C-terminus of Trx2, respectively. The fragments of fluorescent proteins of belonging to UCP3-VN and ΔCUCP3-VN were localized to the mitochondrial IMS and matrix, respectively. (D) HeLa cells were transfected with UCP3-VN, Trx2-VC, ΔCUCP3-VN and Trx2-VC, and UCP3-VN and Trx2-VC. Cell extracts (100 μg) were immunoprecipitated (IP) with anti-myc antibodies and analyzed by IB to detect V5 (UCP3) and myc (Trx2). β-Actin was used as an internal standard. (E) Fluorescent images of HeLa cells transfected with UCP3-VN, Trx2-VC, ΔCUCP3-VN and Trx2-VC, and UCP3-VN and Trx2-VC as indicated in each panel. (F) ).

    Techniques Used: Isolation, Transfection, Lysis, SDS Page, Centrifugation, Western Blot, Immunoprecipitation

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    Incubation:

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    Article Snippet: .. The membrane was then incubated overnight at 4°C with rabbit anti-P2X4 (1:100, Alomone Labs, Israel) and mouse anti-β-actin monoclonal (1:2000; Abcam, Cambridge, MA, United States) antibodies. .. After washes in TBST, the membrane was then incubated with Alexa Fluor 700-conjugated goat anti-rabbit antibody (1:5000; Abcam, Cambridge, MA, United States) for 60 min. Target bands were revealed with a fluorescence scanner (Odyssey Infrared Imaging System, LI-COR Biotechnology, NE, United States).

    Article Title: Nuclear factor-κB modulates osteogenesis of periodontal ligament stem cells through competition with β-catenin signaling in inflammatory microenvironments
    Article Snippet: The protein concentration in the extracted lysates was determined with a protein assay kit (Beyotime) according to the manufacturer's recommended protocol. .. Aliquots of 20–60 μ g per sample were separated by 10% SDS-polyacrylamide gel electrophoresis, transferred to the polyvinylidene fluoride membranes (Millipore) and blocked with 5% nonfat milk powder in PBST (PBS with 0.1% Tween); next, they were incubated with the following primary antibodies overnight: anti-Osterix, anti-GSK-3β , anti-β -catenin, anti-β -actin (Abcam, Cambridge, UK), anti-p-GSK-3β , anti-p65, anti-p-p65, anti-Iκ Bα , anti-p- Iκ Bα , anti-HDAC1 (Cell Signaling Technology, Beverly, MA, USA) and anti-active-β -catenin (Millipore). .. The membranes were then incubated with horseradish peroxidase-conjugated anti-mouse or anti-rabbit IgG secondary antibody (Boster, Wuhan, China).

    Bradford Protein Assay:

    Article Title: Divergent effects of RIP1 or RIP3 blockade in murine models of acute liver injury
    Article Snippet: Western blotting For western blotting, total protein was isolated from 10 mg liver tissue by homogenization in RIPA buffer (50 mM pH7.4 Tris-Hcl, 150 mM NaCl, 0.5% Na-deoxycolate, 0.5% NP-40, 0.25% SDS, 5 mM EDTA) with Complete Protease Inhibitor Cocktail (Roche, Pleasanton, CA, USA). .. After determining total protein by Bradford protein assay, 10% polyacrylamide gels (NuPage, Invitrogen, Grand Island, NY, USA) were equiloaded, electrophoresed at 200 V, electrotransferred to PVDF membranes, and probed with monoclonal antibodies to β -actin (no. ab8227), c-FLIP (no. ab8421), FADD (no. ab24533), RIP3 (no. ab152130, all Abcam), RIP1 (no. 3493), Caspase 1 (no. 2225), Caspase 3 (no. 9664S), and Caspase 8 (no. 4790). .. Blots were developed by ECL (Thermo Scientific, Ashvile, NC, USA).

    Blocking Assay:

    Article Title: Inhibitory Activity of the Flower Buds of Lonicera japonica Thunb. against Histamine Production and l-Histidine Decarboxylase in Human Keratinocytes
    Article Snippet: Concentration of protein measured using a 2-D Quant kit (GE Healthcare Bio-Sciences Corp.). .. After blocking with 1% skim milk in PBS containing 0.1% Tween 20, the membrane was cut, at approximately 50-kDa point, and the upper and lower parts were reacted overnight with rabbit polyclonal anti-HDC (Progen Biotechnik GmbH, Heidelberg, Germany) and anti-β-actin antibodies (1/1,000 each, Abcam, Tokyo, Japan) at 4 °C, respectively. .. After washing with PBS containing 0.1% Tween 20, the membranes were incubated with fluorophore-labeled donkey anti-rabbit IgG antibody (1/1,000) for 2 h at room temperature.

    Nucleic Acid Electrophoresis:

    Article Title: Nuclear factor-κB modulates osteogenesis of periodontal ligament stem cells through competition with β-catenin signaling in inflammatory microenvironments
    Article Snippet: The protein concentration in the extracted lysates was determined with a protein assay kit (Beyotime) according to the manufacturer's recommended protocol. .. Aliquots of 20–60 μ g per sample were separated by 10% SDS-polyacrylamide gel electrophoresis, transferred to the polyvinylidene fluoride membranes (Millipore) and blocked with 5% nonfat milk powder in PBST (PBS with 0.1% Tween); next, they were incubated with the following primary antibodies overnight: anti-Osterix, anti-GSK-3β , anti-β -catenin, anti-β -actin (Abcam, Cambridge, UK), anti-p-GSK-3β , anti-p65, anti-p-p65, anti-Iκ Bα , anti-p- Iκ Bα , anti-HDAC1 (Cell Signaling Technology, Beverly, MA, USA) and anti-active-β -catenin (Millipore). .. The membranes were then incubated with horseradish peroxidase-conjugated anti-mouse or anti-rabbit IgG secondary antibody (Boster, Wuhan, China).

    Western Blot:

    Article Title: The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington’s disease patients
    Article Snippet: Approximately 30 μg of total protein was separated by SDS–PAGE, transferred to polyvinylidene difluoride membranes (Millipore) and subjected to immunoblotting. .. Western blot analysis was performed with anti-UBR5 (Stem Cell Technologies, #60094, 1:1000), anti-UBE3A (Cell Signaling, ab#7526, 1:1000), anti-RNF181 (ThermoFisher Scientific, PA5-31008, 1:2000), anti-UBR7 (ThermoFisher Scientific, PA5-31559, 1:1000), anti-ATXN3 (Merck, MAB5360, 1:500), anti-FUS (Abcam, #154141, 1:1000), anti-GFP (Immunokontakt, 210-PS-1GF, 1:5000), anti-polyubiquitinylated conjugates (Enzo, PW8805-0500, 1:1000), anti-p62 (Progen, GP62-C, 1:1000), anti-LC3 (Sigma, L7543, 1:1000), anti-DARPP32 (Abcam, #40801, 1:1000) and anti-β-actin (Abcam, #8226, 1:5000). .. To detect HTT protein, we used anti-HTT (Cell Signaling, ab#5656, 1:1000), a monoclonal antibody produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro1220 of human HTT protein.

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  • 99
    Abcam anti β actin antibody
    Protein expression levels of PERK, IRE1α and ATF6 in ovaries of aged mice. Representative western blot images (a) and quantification of PERK, IRE1α and ATF6 protein expression levels (b). <t>β-ACTIN</t> served as an internal control. Data are expressed as the mean ± SEM, expressed by error bars.
    Anti β Actin Antibody, supplied by Abcam, 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 antibody/product/Abcam
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti β actin antibody - by Bioz Stars, 2021-03
    99/100 stars
      Buy from Supplier

    99
    Abcam mouse anti β actin
    Gastrodin (GSTD) increased osteogenic transcription Runx2, decreased adipogenic factor peroxisome proliferator-activated receptor (PPAR)γ isoform 2 and activated nuclear factor-like 2 (NRF2) pathway protein expression levels. Representative western blot analyses for total protein was analyzed by western blotting in dexamethasone (DEX)-treated MC3T3-E1 cells with or without GSTD pretreatment at different doses. The relative protein expression levels were measured using the fold-change in each protein relative to <t>β-actin</t> from the same sample. The data are expressed as the mean ± standard deviation. ## P
    Mouse Anti β Actin, supplied by Abcam, 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/mouse anti β actin/product/Abcam
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse anti β actin - by Bioz Stars, 2021-03
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    99
    Abcam anti β actin
    Hirudin regulated fibrosis-related factors in Ang II-induced myocardial fibroblasts. ( A ) The relative mRNA levels of MMP-2, MMP-9, TIMP-2 was evaluated by qRT-PCR. ( B ) The relative protein levels of MMP-2, MMP-9, TIMP-2 was examined by western blot. ( C ) qRT-PCR was performed to determine the mRNA levels of FN, TGF-β1, COL-I and COL-III. ( D ) Western blot was carried out to detect the protein levels of FN, TGF-β1, COL-I and COL-III, and normalized to <t>β-actin</t> expression. Gray value was detected and counted by quality one. * P
    Anti β Actin, supplied by Abcam, 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/Abcam
    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
      Buy from Supplier

    Image Search Results


    Protein expression levels of PERK, IRE1α and ATF6 in ovaries of aged mice. Representative western blot images (a) and quantification of PERK, IRE1α and ATF6 protein expression levels (b). β-ACTIN served as an internal control. Data are expressed as the mean ± SEM, expressed by error bars.

    Journal: The Journal of Veterinary Medical Science

    Article Title: Intravenous human endothelial progenitor cell administration into aged mice enhances embryo development and oocyte quality by reducing inflammation, endoplasmic reticulum stress and apoptosis

    doi: 10.1292/jvms.18-0242

    Figure Lengend Snippet: Protein expression levels of PERK, IRE1α and ATF6 in ovaries of aged mice. Representative western blot images (a) and quantification of PERK, IRE1α and ATF6 protein expression levels (b). β-ACTIN served as an internal control. Data are expressed as the mean ± SEM, expressed by error bars.

    Article Snippet: The loading and blotting of the amount of protein was verified by reprobing the membrane with anti-β actin antibody (1:5,000; Abcam) followed by Coomassie Blue staining.

    Techniques: Expressing, Mouse Assay, Western Blot

    Gastrodin (GSTD) increased osteogenic transcription Runx2, decreased adipogenic factor peroxisome proliferator-activated receptor (PPAR)γ isoform 2 and activated nuclear factor-like 2 (NRF2) pathway protein expression levels. Representative western blot analyses for total protein was analyzed by western blotting in dexamethasone (DEX)-treated MC3T3-E1 cells with or without GSTD pretreatment at different doses. The relative protein expression levels were measured using the fold-change in each protein relative to β-actin from the same sample. The data are expressed as the mean ± standard deviation. ## P

    Journal: International Journal of Molecular Medicine

    Article Title: Gastrodin protects MC3T3-E1 osteoblasts from dexamethasone-induced cellular dysfunction and promotes bone formation via induction of the NRF2 signaling pathway

    doi: 10.3892/ijmm.2018.3414

    Figure Lengend Snippet: Gastrodin (GSTD) increased osteogenic transcription Runx2, decreased adipogenic factor peroxisome proliferator-activated receptor (PPAR)γ isoform 2 and activated nuclear factor-like 2 (NRF2) pathway protein expression levels. Representative western blot analyses for total protein was analyzed by western blotting in dexamethasone (DEX)-treated MC3T3-E1 cells with or without GSTD pretreatment at different doses. The relative protein expression levels were measured using the fold-change in each protein relative to β-actin from the same sample. The data are expressed as the mean ± standard deviation. ## P

    Article Snippet: Rabbit anti-HO-1 (cat. no. ab68477; 1:1,000), rabbit anti-NQO-1 (cat. no. ab76956; 1:1,000), and mouse anti-β-actin (cat. no. ab8245; 1:1,000), Anti-OCN (cat. no. ab93876; 1:1,000) monoclonal antibodies were purchased from Abcam (Cambridge, MA, USA).

    Techniques: Expressing, Western Blot, Standard Deviation

    Hirudin regulated fibrosis-related factors in Ang II-induced myocardial fibroblasts. ( A ) The relative mRNA levels of MMP-2, MMP-9, TIMP-2 was evaluated by qRT-PCR. ( B ) The relative protein levels of MMP-2, MMP-9, TIMP-2 was examined by western blot. ( C ) qRT-PCR was performed to determine the mRNA levels of FN, TGF-β1, COL-I and COL-III. ( D ) Western blot was carried out to detect the protein levels of FN, TGF-β1, COL-I and COL-III, and normalized to β-actin expression. Gray value was detected and counted by quality one. * P

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Hirudin Protects Ang II-Induced Myocardial Fibroblasts Fibrosis by Inhibiting the Extracellular Signal-Regulated Kinase1/2 (ERK1/2) Pathway

    doi: 10.12659/MSM.909044

    Figure Lengend Snippet: Hirudin regulated fibrosis-related factors in Ang II-induced myocardial fibroblasts. ( A ) The relative mRNA levels of MMP-2, MMP-9, TIMP-2 was evaluated by qRT-PCR. ( B ) The relative protein levels of MMP-2, MMP-9, TIMP-2 was examined by western blot. ( C ) qRT-PCR was performed to determine the mRNA levels of FN, TGF-β1, COL-I and COL-III. ( D ) Western blot was carried out to detect the protein levels of FN, TGF-β1, COL-I and COL-III, and normalized to β-actin expression. Gray value was detected and counted by quality one. * P

    Article Snippet: The membranes were incubated with anti-matrix metalloproteinase-2 (MMP-2) (AmyJet Scientific, 12015-01, 1: 2000), anti-MMP-9 (R & D, AF909-SP, 1: 1000), anti-tissue inhibitor of metalloproteinases-2 (TIMP-2) (R & D, AF971, 1: 1200), anti-fibronectin (FN) (Abcam, ab2413, 1: 800), anti-transforming growth factor beta 1 (TGF-β1) (R & D, FAB766G, 1: 700), anti-collagen-I (COL-I) (Abcam, ab90395, 1: 1000), anti-collagen III (COL-III) (Abcam, ab7778, 1: 800), anti-p-ERK1/2 (CST, 8544, 1: 1000), anti-ERK1/2 (CST, 9102, 1: 700), and anti-β-actin (Abcam, ab8226, 1: 2000) at 4°C for 24 hours.

    Techniques: Quantitative RT-PCR, Western Blot, Expressing

    Hirudin downregulated ERK1/2 pathway in Ang II-induced myocardial fibroblasts. ( A ) The proteins expression levels of ERK1/2 and p-ERK1/2 were examined by western blot. ( B ) Quantification of protein expression was carried out with GraphPad prism 7.0. β-actin was used as internal control. The gray value was evaluated and calculated by quality one. * P

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    Article Title: Hirudin Protects Ang II-Induced Myocardial Fibroblasts Fibrosis by Inhibiting the Extracellular Signal-Regulated Kinase1/2 (ERK1/2) Pathway

    doi: 10.12659/MSM.909044

    Figure Lengend Snippet: Hirudin downregulated ERK1/2 pathway in Ang II-induced myocardial fibroblasts. ( A ) The proteins expression levels of ERK1/2 and p-ERK1/2 were examined by western blot. ( B ) Quantification of protein expression was carried out with GraphPad prism 7.0. β-actin was used as internal control. The gray value was evaluated and calculated by quality one. * P

    Article Snippet: The membranes were incubated with anti-matrix metalloproteinase-2 (MMP-2) (AmyJet Scientific, 12015-01, 1: 2000), anti-MMP-9 (R & D, AF909-SP, 1: 1000), anti-tissue inhibitor of metalloproteinases-2 (TIMP-2) (R & D, AF971, 1: 1200), anti-fibronectin (FN) (Abcam, ab2413, 1: 800), anti-transforming growth factor beta 1 (TGF-β1) (R & D, FAB766G, 1: 700), anti-collagen-I (COL-I) (Abcam, ab90395, 1: 1000), anti-collagen III (COL-III) (Abcam, ab7778, 1: 800), anti-p-ERK1/2 (CST, 8544, 1: 1000), anti-ERK1/2 (CST, 9102, 1: 700), and anti-β-actin (Abcam, ab8226, 1: 2000) at 4°C for 24 hours.

    Techniques: Expressing, Western Blot

    Ado inhibits cell viability and triggers ER stress in HepG2 cells. (A) Time- and dose-dependent cytotoxic effects of Ado on HepG2 cells. Cells were treated with different concentrations of Ado (1.0–4.0 mM) for 12, 24, or 48 h. Cell viability was determined by MTT assay. Results are expressed as percentages of cell growth relative to initial number of viable cells. (B) Cells were treated with 2.0 mM for 6, 12, or 24 h. The cell cycle distribution was evaluated using flow cytometric assay by PI staining. (C) HepG2 cells were treated with 2.0 mM Ado for 24 h. Cells were collected and subjected to total RNA extraction. The mRNA levels of ER stress-related genes GRP78, PERK, ATF4, CHOP, Cyt C and caspase-3 were assessed by RT-PCR. (D) HepG2 cells underwent the aforementioned treatment and were collected and subjected to western blot analyses with specific antibodies directed against GRP78, PERK, ATF4, CHOP, Cyt C and cleaved caspase-3, or β-actin. The density of the corresponding bands was assessed quantitatively using image analysis software and corrected by reference to the value of β-actin. Bar graphs represent the mean fluorescence intensity. *P

    Journal: Oncology Reports

    Article Title: Inhibition of autophagy enhances adenosine-induced apoptosis in human hepatoblastoma HepG2 cells

    doi: 10.3892/or.2018.6899

    Figure Lengend Snippet: Ado inhibits cell viability and triggers ER stress in HepG2 cells. (A) Time- and dose-dependent cytotoxic effects of Ado on HepG2 cells. Cells were treated with different concentrations of Ado (1.0–4.0 mM) for 12, 24, or 48 h. Cell viability was determined by MTT assay. Results are expressed as percentages of cell growth relative to initial number of viable cells. (B) Cells were treated with 2.0 mM for 6, 12, or 24 h. The cell cycle distribution was evaluated using flow cytometric assay by PI staining. (C) HepG2 cells were treated with 2.0 mM Ado for 24 h. Cells were collected and subjected to total RNA extraction. The mRNA levels of ER stress-related genes GRP78, PERK, ATF4, CHOP, Cyt C and caspase-3 were assessed by RT-PCR. (D) HepG2 cells underwent the aforementioned treatment and were collected and subjected to western blot analyses with specific antibodies directed against GRP78, PERK, ATF4, CHOP, Cyt C and cleaved caspase-3, or β-actin. The density of the corresponding bands was assessed quantitatively using image analysis software and corrected by reference to the value of β-actin. Bar graphs represent the mean fluorescence intensity. *P

    Article Snippet: ATF4 (cat. no. ab23760), GRP78 (cat. no. ab21685), PERK (cat. no. ab65142), p-AMPK (cat. no. ab133448), AMPK (cat. no. ab80039), p-ULK1 (cat. no. ab229540), ULK1 (cat. no. ab167139), p-mTOR (cat. no. ab84400), mTOR (cat. no. ab32028), CHOP (cat. no. ab11419), cytochrome c (cat. no. ab110325) and β-actin (cat. no. ab8226) were purchased from Abcam (Cambridge, MA, USA).

    Techniques: MTT Assay, Flow Cytometry, Staining, RNA Extraction, Reverse Transcription Polymerase Chain Reaction, Western Blot, Software, Fluorescence

    Inhibition of autophagy enhances ER stress-mediated apoptotic cell death. (A) HepG2 cells were treated with 2.0 mM Ado or 10 µM LY alone. In the combination treatment group, the cells were pre-treated with 10 µM LY for 2 h, followed by 2.0 mM Ado treatment. Cell viability was determined by MTT assay at the indicated time-points. (B) Cell apoptosis was detected by Hoechst staining. Images were captured under a fluorescence microscope (original magnification, ×200). Arrows indicate apoptotic cells. (C) The mRNA levels of Cyt C, AMPK and p62 were assessed by RT-PCR. (D) HepG2 cells underwent the aforementioned treatment and were collected and subjected to western blot analyses with specific antibodies directed against Cyt C, p-AMPK, AMPK, p62, LC3-I and LC3-II, or β-actin. Bar graphs represent the mean protein band intensity. Relative quantity of the aforementioned proteins was computed. (E) Mitochondrial membrane potential (ΔΨm) indicated by Rhodamine-123 was detected by flow cytometry. Bar graphs represent the mean fluorescence intensity. *P

    Journal: Oncology Reports

    Article Title: Inhibition of autophagy enhances adenosine-induced apoptosis in human hepatoblastoma HepG2 cells

    doi: 10.3892/or.2018.6899

    Figure Lengend Snippet: Inhibition of autophagy enhances ER stress-mediated apoptotic cell death. (A) HepG2 cells were treated with 2.0 mM Ado or 10 µM LY alone. In the combination treatment group, the cells were pre-treated with 10 µM LY for 2 h, followed by 2.0 mM Ado treatment. Cell viability was determined by MTT assay at the indicated time-points. (B) Cell apoptosis was detected by Hoechst staining. Images were captured under a fluorescence microscope (original magnification, ×200). Arrows indicate apoptotic cells. (C) The mRNA levels of Cyt C, AMPK and p62 were assessed by RT-PCR. (D) HepG2 cells underwent the aforementioned treatment and were collected and subjected to western blot analyses with specific antibodies directed against Cyt C, p-AMPK, AMPK, p62, LC3-I and LC3-II, or β-actin. Bar graphs represent the mean protein band intensity. Relative quantity of the aforementioned proteins was computed. (E) Mitochondrial membrane potential (ΔΨm) indicated by Rhodamine-123 was detected by flow cytometry. Bar graphs represent the mean fluorescence intensity. *P

    Article Snippet: ATF4 (cat. no. ab23760), GRP78 (cat. no. ab21685), PERK (cat. no. ab65142), p-AMPK (cat. no. ab133448), AMPK (cat. no. ab80039), p-ULK1 (cat. no. ab229540), ULK1 (cat. no. ab167139), p-mTOR (cat. no. ab84400), mTOR (cat. no. ab32028), CHOP (cat. no. ab11419), cytochrome c (cat. no. ab110325) and β-actin (cat. no. ab8226) were purchased from Abcam (Cambridge, MA, USA).

    Techniques: Inhibition, MTT Assay, Staining, Fluorescence, Microscopy, Reverse Transcription Polymerase Chain Reaction, Western Blot, Flow Cytometry, Cytometry

    Ado induces autophagy in HepG2 cells. (A) HepG2 cells were treated with 2.0 mM for 12, or 24 h and cells were stained with MDC. The autophagosomes were detected under fluorescence microscopy (magnification, ×200). (B) The mRNA levels of autophagy-related genes Beclin-1 and p62 were assessed by RT-PCR. (C) HepG2 cells underwent the aforementioned treatment and were collected and subjected to western blot analyses with specific antibodies directed against LC3-I, LC3-II, Beclin-1, p62 or β-actin. Bar graphs represent the mean protein band intensity. Relative quantity of the aforementioned proteins was computed after normalization with β-actin. *P

    Journal: Oncology Reports

    Article Title: Inhibition of autophagy enhances adenosine-induced apoptosis in human hepatoblastoma HepG2 cells

    doi: 10.3892/or.2018.6899

    Figure Lengend Snippet: Ado induces autophagy in HepG2 cells. (A) HepG2 cells were treated with 2.0 mM for 12, or 24 h and cells were stained with MDC. The autophagosomes were detected under fluorescence microscopy (magnification, ×200). (B) The mRNA levels of autophagy-related genes Beclin-1 and p62 were assessed by RT-PCR. (C) HepG2 cells underwent the aforementioned treatment and were collected and subjected to western blot analyses with specific antibodies directed against LC3-I, LC3-II, Beclin-1, p62 or β-actin. Bar graphs represent the mean protein band intensity. Relative quantity of the aforementioned proteins was computed after normalization with β-actin. *P

    Article Snippet: ATF4 (cat. no. ab23760), GRP78 (cat. no. ab21685), PERK (cat. no. ab65142), p-AMPK (cat. no. ab133448), AMPK (cat. no. ab80039), p-ULK1 (cat. no. ab229540), ULK1 (cat. no. ab167139), p-mTOR (cat. no. ab84400), mTOR (cat. no. ab32028), CHOP (cat. no. ab11419), cytochrome c (cat. no. ab110325) and β-actin (cat. no. ab8226) were purchased from Abcam (Cambridge, MA, USA).

    Techniques: Staining, Fluorescence, Microscopy, Reverse Transcription Polymerase Chain Reaction, Western Blot

    Inhibition of autophagy by AMPK siRNA enhances Ado-induced apoptosis and inhibits the AMPK/mTOR/ULK1 pathway. (A) HepG2 cells were transfected with AMPK siRNA (20 µM) or control siRNA (transfected with empty vector, 20 µM), then exposed to 2.0 mM Ado or not for 24 h and then the cell apoptotic ratio was determined by flow cytometry (FACS) with Annexin V-FITC and PI double staining. (B) HepG2 cells underwent the aforementioned treatment and were collected and the protein levels of the AMPK/mTOR/ULK1 pathway were assessed by western blotting. The phosphorylation ratios of p-AMPK/AMPK, p-ULK1/ULK1 and p-mTOR/mTOR were computed (C) The mRNA and protein levels of ER stress-related genes were assessed by RT-PCR and western blotting. HepG2 cells underwent the aforementioned treatment and were collected and subjected to western blot analyses with specific antibodies directed against CHOP, cleaved caspase-3, p62 and Cyt C or β-actin. Bar graphs represent the mean protein band intensity. (D) Mitochondrial membrane potential (ΔΨm) indicated by Rhodamine-123 was detected by flow cytometry. Bar graphs represent the mean fluorescence intensity. *P

    Journal: Oncology Reports

    Article Title: Inhibition of autophagy enhances adenosine-induced apoptosis in human hepatoblastoma HepG2 cells

    doi: 10.3892/or.2018.6899

    Figure Lengend Snippet: Inhibition of autophagy by AMPK siRNA enhances Ado-induced apoptosis and inhibits the AMPK/mTOR/ULK1 pathway. (A) HepG2 cells were transfected with AMPK siRNA (20 µM) or control siRNA (transfected with empty vector, 20 µM), then exposed to 2.0 mM Ado or not for 24 h and then the cell apoptotic ratio was determined by flow cytometry (FACS) with Annexin V-FITC and PI double staining. (B) HepG2 cells underwent the aforementioned treatment and were collected and the protein levels of the AMPK/mTOR/ULK1 pathway were assessed by western blotting. The phosphorylation ratios of p-AMPK/AMPK, p-ULK1/ULK1 and p-mTOR/mTOR were computed (C) The mRNA and protein levels of ER stress-related genes were assessed by RT-PCR and western blotting. HepG2 cells underwent the aforementioned treatment and were collected and subjected to western blot analyses with specific antibodies directed against CHOP, cleaved caspase-3, p62 and Cyt C or β-actin. Bar graphs represent the mean protein band intensity. (D) Mitochondrial membrane potential (ΔΨm) indicated by Rhodamine-123 was detected by flow cytometry. Bar graphs represent the mean fluorescence intensity. *P

    Article Snippet: ATF4 (cat. no. ab23760), GRP78 (cat. no. ab21685), PERK (cat. no. ab65142), p-AMPK (cat. no. ab133448), AMPK (cat. no. ab80039), p-ULK1 (cat. no. ab229540), ULK1 (cat. no. ab167139), p-mTOR (cat. no. ab84400), mTOR (cat. no. ab32028), CHOP (cat. no. ab11419), cytochrome c (cat. no. ab110325) and β-actin (cat. no. ab8226) were purchased from Abcam (Cambridge, MA, USA).

    Techniques: Inhibition, Transfection, Plasmid Preparation, Flow Cytometry, Cytometry, FACS, Double Staining, Western Blot, Reverse Transcription Polymerase Chain Reaction, Fluorescence