anti-actin Search Results


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  • 99
    Millipore monoclonal anti beta actin antibody
    Monoclonal Anti Beta Actin Antibody, 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/monoclonal anti beta actin antibody/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    monoclonal anti beta actin antibody - by Bioz Stars, 2021-06
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    99
    Abcam β actin
    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/β actin/product/Abcam
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    β actin - by Bioz Stars, 2021-06
    99/100 stars
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    86
    Santa Cruz Biotechnology β actin
    Protein expression levels of macrophage migration inhibitory factor (MIF), glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) in footpad skin lesions in a diabetic neuropathy (DN) rat model. Protein (20 μg) was obtained from each footpad tissue sample. Protein levels were examined by Western blot. As a control for Western blot analysis, the level of <t>β-actin</t> was determined using an antibody against β-actin. All columnar values are expressed as mean ± standard deviation (SD) ( n = 6 per group). * P
    β Actin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/β actin/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    β actin - by Bioz Stars, 2021-06
    86/100 stars
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    86
    Santa Cruz Biotechnology anti β actin
    miR-let-7c-5p overexpression inhibits EtOH-induced hepatic apoptosis. (A–C) Effects of miR-let7c-5p on cell apoptosis by western blot and flow cytometry. <t>β-actin</t> served as a loading control. Data shown are the mean ± SD from three independent experiments. ∗ P
    Anti β Actin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti β actin/product/Santa Cruz Biotechnology
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti β actin - by Bioz Stars, 2021-06
    86/100 stars
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    N/A
    Specific for the 42 kDa actin protein in lysates from skeletal cardiac gizzard and aorta tissues Reacts with all actin isoforms Unpurified ascites fluid Actin is the most abundant protein
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    N/A
    The Actin protein a component of the eukaryotic cytoskeleton is highly conserved between multiple species It is involved in various types of cell motility and maintenance of the cytoskeleton In
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    N/A
    Rabbit polyclonal to Actin alpha1 Conjugation note Unconjugated Application note WB IHC p ELISA Reactivity note Human Mouse Rat
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    N/A
    Rabbit polyclonal to Actin kappa Conjugation note Unconjugated Application note WB ELISA Reactivity note Human Mouse
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    Image Search Results


    Protein expression levels of macrophage migration inhibitory factor (MIF), glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) in footpad skin lesions in a diabetic neuropathy (DN) rat model. Protein (20 μg) was obtained from each footpad tissue sample. Protein levels were examined by Western blot. As a control for Western blot analysis, the level of β-actin was determined using an antibody against β-actin. All columnar values are expressed as mean ± standard deviation (SD) ( n = 6 per group). * P

    Journal: Molecular Pain

    Article Title: Expression of macrophage migration inhibitory factor in footpad skin lesions with diabetic neuropathy

    doi: 10.1177/1744806918775482

    Figure Lengend Snippet: Protein expression levels of macrophage migration inhibitory factor (MIF), glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) in footpad skin lesions in a diabetic neuropathy (DN) rat model. Protein (20 μg) was obtained from each footpad tissue sample. Protein levels were examined by Western blot. As a control for Western blot analysis, the level of β-actin was determined using an antibody against β-actin. All columnar values are expressed as mean ± standard deviation (SD) ( n = 6 per group). * P

    Article Snippet: Rabbit polyclonal antibody against MIF (1:200, Santa Cruz) and mouse monoclonal antibodies against IENF (1:200), GLO-I (1:1000) (Abcam, Cambridge, MA, USA) or β-actin (1:200, Santa Cruz) were used in this study.

    Techniques: Expressing, Migration, Western Blot, Standard Deviation

    Macrophage migration inhibitory factor (MIF), glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) expression level changes in human HaCaT keratinocytes after being exposed to various concentrations of methylglyoxal (MG). Expression levels of MIF, GLO-I, and IENF mRNAs and proteins were measured by real-time reverse transcription polymerase chain reaction (a) to (c) and Western blot (d) to (g), respectively. Real-time PCR analysis was performed with a SYBR Green assay system. Relative gene expression level normalized to β-actin was calculated with 2 −△△CT method. As a control for Western blot analysis, the level of β-actin was determined using an antibody against β-actin. All results are presented as mean ± SD of three independent experiments. * P

    Journal: Molecular Pain

    Article Title: Expression of macrophage migration inhibitory factor in footpad skin lesions with diabetic neuropathy

    doi: 10.1177/1744806918775482

    Figure Lengend Snippet: Macrophage migration inhibitory factor (MIF), glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) expression level changes in human HaCaT keratinocytes after being exposed to various concentrations of methylglyoxal (MG). Expression levels of MIF, GLO-I, and IENF mRNAs and proteins were measured by real-time reverse transcription polymerase chain reaction (a) to (c) and Western blot (d) to (g), respectively. Real-time PCR analysis was performed with a SYBR Green assay system. Relative gene expression level normalized to β-actin was calculated with 2 −△△CT method. As a control for Western blot analysis, the level of β-actin was determined using an antibody against β-actin. All results are presented as mean ± SD of three independent experiments. * P

    Article Snippet: Rabbit polyclonal antibody against MIF (1:200, Santa Cruz) and mouse monoclonal antibodies against IENF (1:200), GLO-I (1:1000) (Abcam, Cambridge, MA, USA) or β-actin (1:200, Santa Cruz) were used in this study.

    Techniques: Migration, Expressing, Reverse Transcription Polymerase Chain Reaction, Western Blot, Real-time Polymerase Chain Reaction, SYBR Green Assay

    Effects of macrophage migration inhibitory factor (MIF) small interfering RNA (siRNA) in the presence of 400 μm methylglyoxal (MG) in human HaCaT keratinocytes. Cells were transfected with MIF siRNA or a control siRNA as well as recombinant human (rh)-MIF before stimulation with MG. Expression levels of MIF, glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) mRNAs and proteins were measured by real-time reverse transcription polymerase chain reaction (a) to (c) and Western blot (d) to (g), respectively. Real-time PCR analysis was performed with a SYBR Green assay system. Relative gene expression levels normalized to β-actin was calculated with 2 −△△CT method. As a control for Western blot analysis, the level of β-actin was determined using an antibody against β-actin. All results are presented as mean ± SD of three independent experiments. ++ P

    Journal: Molecular Pain

    Article Title: Expression of macrophage migration inhibitory factor in footpad skin lesions with diabetic neuropathy

    doi: 10.1177/1744806918775482

    Figure Lengend Snippet: Effects of macrophage migration inhibitory factor (MIF) small interfering RNA (siRNA) in the presence of 400 μm methylglyoxal (MG) in human HaCaT keratinocytes. Cells were transfected with MIF siRNA or a control siRNA as well as recombinant human (rh)-MIF before stimulation with MG. Expression levels of MIF, glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) mRNAs and proteins were measured by real-time reverse transcription polymerase chain reaction (a) to (c) and Western blot (d) to (g), respectively. Real-time PCR analysis was performed with a SYBR Green assay system. Relative gene expression levels normalized to β-actin was calculated with 2 −△△CT method. As a control for Western blot analysis, the level of β-actin was determined using an antibody against β-actin. All results are presented as mean ± SD of three independent experiments. ++ P

    Article Snippet: Rabbit polyclonal antibody against MIF (1:200, Santa Cruz) and mouse monoclonal antibodies against IENF (1:200), GLO-I (1:1000) (Abcam, Cambridge, MA, USA) or β-actin (1:200, Santa Cruz) were used in this study.

    Techniques: Migration, Small Interfering RNA, Transfection, Recombinant, Expressing, Reverse Transcription Polymerase Chain Reaction, Western Blot, Real-time Polymerase Chain Reaction, SYBR Green Assay

    Macrophage migration inhibitory factor (MIF), glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) expression level changes in human HaCaT keratinocytes after being exposed to recombinant human (rh)-MIF in the presence of 400 μm MG. Expression levels of MIF, GLO-I, and IENF mRNAs and proteins were measured by real-time reverse transcription polymerase chain reaction (a) to (c) and Western blot (d) to (g), respectively. Real-time PCR analysis was performed with a SYBR Green assay system. Relative gene expression level normalized to β-actin was calculated with 2 −△△CT method. As a control for Western blot analysis, the level of β-actin was determined using an antibody against β-actin. All results are presented as mean ± SD of three independent experiments. * P

    Journal: Molecular Pain

    Article Title: Expression of macrophage migration inhibitory factor in footpad skin lesions with diabetic neuropathy

    doi: 10.1177/1744806918775482

    Figure Lengend Snippet: Macrophage migration inhibitory factor (MIF), glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) expression level changes in human HaCaT keratinocytes after being exposed to recombinant human (rh)-MIF in the presence of 400 μm MG. Expression levels of MIF, GLO-I, and IENF mRNAs and proteins were measured by real-time reverse transcription polymerase chain reaction (a) to (c) and Western blot (d) to (g), respectively. Real-time PCR analysis was performed with a SYBR Green assay system. Relative gene expression level normalized to β-actin was calculated with 2 −△△CT method. As a control for Western blot analysis, the level of β-actin was determined using an antibody against β-actin. All results are presented as mean ± SD of three independent experiments. * P

    Article Snippet: Rabbit polyclonal antibody against MIF (1:200, Santa Cruz) and mouse monoclonal antibodies against IENF (1:200), GLO-I (1:1000) (Abcam, Cambridge, MA, USA) or β-actin (1:200, Santa Cruz) were used in this study.

    Techniques: Migration, Expressing, Recombinant, Reverse Transcription Polymerase Chain Reaction, Western Blot, Real-time Polymerase Chain Reaction, SYBR Green Assay

    Expressions levels of macrophage migration inhibitory factor (MIF), glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) mRNAs in footpad skin lesions in a diabetic neuropathy (DN) rat model. Total RNA (10 μg) obtained from each footpad tissue sample was reverse transcribed into cDNA. Real-time polymerase chain reaction was performed with a SYBR Green assay system. Relative gene expression levels normalized to that of β-actin was determined with 2 −ΔΔCT method. All columnar values are expressed as mean ± standard deviation ( SD ) ( n = 6 per group). * P

    Journal: Molecular Pain

    Article Title: Expression of macrophage migration inhibitory factor in footpad skin lesions with diabetic neuropathy

    doi: 10.1177/1744806918775482

    Figure Lengend Snippet: Expressions levels of macrophage migration inhibitory factor (MIF), glyoxalase I (GLO-I), and intraepidermal nerve fibers (IENF) mRNAs in footpad skin lesions in a diabetic neuropathy (DN) rat model. Total RNA (10 μg) obtained from each footpad tissue sample was reverse transcribed into cDNA. Real-time polymerase chain reaction was performed with a SYBR Green assay system. Relative gene expression levels normalized to that of β-actin was determined with 2 −ΔΔCT method. All columnar values are expressed as mean ± standard deviation ( SD ) ( n = 6 per group). * P

    Article Snippet: Rabbit polyclonal antibody against MIF (1:200, Santa Cruz) and mouse monoclonal antibodies against IENF (1:200), GLO-I (1:1000) (Abcam, Cambridge, MA, USA) or β-actin (1:200, Santa Cruz) were used in this study.

    Techniques: Migration, Real-time Polymerase Chain Reaction, SYBR Green Assay, Expressing, Standard Deviation

    miR-let-7c-5p overexpression inhibits EtOH-induced hepatic apoptosis. (A–C) Effects of miR-let7c-5p on cell apoptosis by western blot and flow cytometry. β-actin served as a loading control. Data shown are the mean ± SD from three independent experiments. ∗ P

    Journal: Frontiers in Pharmacology

    Article Title: The Long Non-coding RNA MEG3/miR-let-7c-5p Axis Regulates Ethanol-Induced Hepatic Steatosis and Apoptosis by Targeting NLRC5

    doi: 10.3389/fphar.2018.00302

    Figure Lengend Snippet: miR-let-7c-5p overexpression inhibits EtOH-induced hepatic apoptosis. (A–C) Effects of miR-let7c-5p on cell apoptosis by western blot and flow cytometry. β-actin served as a loading control. Data shown are the mean ± SD from three independent experiments. ∗ P

    Article Snippet: The categories and concentrations of primary antibodies: anti-PPAR-α (Rabbit, 1:800, ab8934, Abcam, United Kingdom), SREBP-1c (Rabbit, 1:800, ab28481, Abcam, United Kingdom), anti-Bax (Rabbit, 1:800, ab32503, Abcam, United Kingdom), anti-Bcl2 (Rabbit, 1:800, ab196495, Abcam, United Kingdom), anti-caspase 9 (Rabbit, 1:800, ab184786, Abcam, United Kingdom), and anti-NLRC5 (Rabbit, 1:800, ab117624, Abcam, United Kingdom); anti-caspase 3 (Rabbit, 1:800, #8242, Cell Signaling Tech, Danvers, MA, United States), anti-β-actin (Mouse, 1:300, sc47778, Santa Cruz, CA, United States).

    Techniques: Over Expression, Western Blot, Flow Cytometry, Cytometry

    miR-let-7c-5p directly targets the NLRC5 gene in EtOH-induced liver injury. (A) Bioinformatics predicted miR-let-7c-5p binding sites in NLRC5 3′UTR. (B) Relative level of NLRC5 mRNA in primary hepatocytes by real-time PCR. (C) Immunohistochemical staining for NLRC5 in liver tissues 400×. (D) Luciferase reporter assay in 293T cells were co-transfected with the NLRC5-WT or mutant reporter vector in the miR-let-7c-5p binding sites and miR-let-7c-5p mimics. (E) Western blot analyses was performed to test NLRC5 expression after AML-12 cells were transfected with miR-let-7c-5p inhibitor NC, inhibitor, mimics NC or mimics. (F) Western blot analyses was performed to test NLRC5 expression. AML-12 cells were transfected with miR-let-7c-5p inhibitor or co-transfected with miR-let7c-5p inhibitor and the MEG3 siRNA. β-actin served as a loading control. Data shown are the mean ± SD from three independent experiments. ∗ P

    Journal: Frontiers in Pharmacology

    Article Title: The Long Non-coding RNA MEG3/miR-let-7c-5p Axis Regulates Ethanol-Induced Hepatic Steatosis and Apoptosis by Targeting NLRC5

    doi: 10.3389/fphar.2018.00302

    Figure Lengend Snippet: miR-let-7c-5p directly targets the NLRC5 gene in EtOH-induced liver injury. (A) Bioinformatics predicted miR-let-7c-5p binding sites in NLRC5 3′UTR. (B) Relative level of NLRC5 mRNA in primary hepatocytes by real-time PCR. (C) Immunohistochemical staining for NLRC5 in liver tissues 400×. (D) Luciferase reporter assay in 293T cells were co-transfected with the NLRC5-WT or mutant reporter vector in the miR-let-7c-5p binding sites and miR-let-7c-5p mimics. (E) Western blot analyses was performed to test NLRC5 expression after AML-12 cells were transfected with miR-let-7c-5p inhibitor NC, inhibitor, mimics NC or mimics. (F) Western blot analyses was performed to test NLRC5 expression. AML-12 cells were transfected with miR-let-7c-5p inhibitor or co-transfected with miR-let7c-5p inhibitor and the MEG3 siRNA. β-actin served as a loading control. Data shown are the mean ± SD from three independent experiments. ∗ P

    Article Snippet: The categories and concentrations of primary antibodies: anti-PPAR-α (Rabbit, 1:800, ab8934, Abcam, United Kingdom), SREBP-1c (Rabbit, 1:800, ab28481, Abcam, United Kingdom), anti-Bax (Rabbit, 1:800, ab32503, Abcam, United Kingdom), anti-Bcl2 (Rabbit, 1:800, ab196495, Abcam, United Kingdom), anti-caspase 9 (Rabbit, 1:800, ab184786, Abcam, United Kingdom), and anti-NLRC5 (Rabbit, 1:800, ab117624, Abcam, United Kingdom); anti-caspase 3 (Rabbit, 1:800, #8242, Cell Signaling Tech, Danvers, MA, United States), anti-β-actin (Mouse, 1:300, sc47778, Santa Cruz, CA, United States).

    Techniques: Binding Assay, Real-time Polymerase Chain Reaction, Immunohistochemistry, Staining, Luciferase, Reporter Assay, Transfection, Mutagenesis, Plasmid Preparation, Western Blot, Expressing

    Chronic ethanol consumption produces hepatic steatosis and apoptosis. (A) Triglyceride (TG) and total cholesterol (TCH) levels in serum and liver tissues. (B) Representative Oil Red O staining of liver tissues 400×. (C) The protein and mRNA levels of PPAR-α and SREBP-1c in liver tissues. (D,E) The protein levels of Bax/Bcl2, cleaved caspase 3 and cleaved caspase9 in liver tissues. β-actin served as a loading control. The values represent means ± SD ( n = 6 in CD-fed group, n = 6 in EtOH-fed group). ∗ P

    Journal: Frontiers in Pharmacology

    Article Title: The Long Non-coding RNA MEG3/miR-let-7c-5p Axis Regulates Ethanol-Induced Hepatic Steatosis and Apoptosis by Targeting NLRC5

    doi: 10.3389/fphar.2018.00302

    Figure Lengend Snippet: Chronic ethanol consumption produces hepatic steatosis and apoptosis. (A) Triglyceride (TG) and total cholesterol (TCH) levels in serum and liver tissues. (B) Representative Oil Red O staining of liver tissues 400×. (C) The protein and mRNA levels of PPAR-α and SREBP-1c in liver tissues. (D,E) The protein levels of Bax/Bcl2, cleaved caspase 3 and cleaved caspase9 in liver tissues. β-actin served as a loading control. The values represent means ± SD ( n = 6 in CD-fed group, n = 6 in EtOH-fed group). ∗ P

    Article Snippet: The categories and concentrations of primary antibodies: anti-PPAR-α (Rabbit, 1:800, ab8934, Abcam, United Kingdom), SREBP-1c (Rabbit, 1:800, ab28481, Abcam, United Kingdom), anti-Bax (Rabbit, 1:800, ab32503, Abcam, United Kingdom), anti-Bcl2 (Rabbit, 1:800, ab196495, Abcam, United Kingdom), anti-caspase 9 (Rabbit, 1:800, ab184786, Abcam, United Kingdom), and anti-NLRC5 (Rabbit, 1:800, ab117624, Abcam, United Kingdom); anti-caspase 3 (Rabbit, 1:800, #8242, Cell Signaling Tech, Danvers, MA, United States), anti-β-actin (Mouse, 1:300, sc47778, Santa Cruz, CA, United States).

    Techniques: Staining

    Reducing MEG3 expression inhibits EtOH-induced hepatic apoptosis. (A,B) Effect of MEG3 on expression of protein Bax/Bcl2, cleaved caspase 3 and cleaved caspase 9 in EtOH-induced AML-12 cells. The expression of proteins were determined by western blot. β-actin served as a loading control. (C) Flow cytometry analyses of apoptosis. The abscissa represents FITC-Annexin V staining and the ordinate represents PI staining. Data shown are the mean ± SD from three independent experiments. ∗ P

    Journal: Frontiers in Pharmacology

    Article Title: The Long Non-coding RNA MEG3/miR-let-7c-5p Axis Regulates Ethanol-Induced Hepatic Steatosis and Apoptosis by Targeting NLRC5

    doi: 10.3389/fphar.2018.00302

    Figure Lengend Snippet: Reducing MEG3 expression inhibits EtOH-induced hepatic apoptosis. (A,B) Effect of MEG3 on expression of protein Bax/Bcl2, cleaved caspase 3 and cleaved caspase 9 in EtOH-induced AML-12 cells. The expression of proteins were determined by western blot. β-actin served as a loading control. (C) Flow cytometry analyses of apoptosis. The abscissa represents FITC-Annexin V staining and the ordinate represents PI staining. Data shown are the mean ± SD from three independent experiments. ∗ P

    Article Snippet: The categories and concentrations of primary antibodies: anti-PPAR-α (Rabbit, 1:800, ab8934, Abcam, United Kingdom), SREBP-1c (Rabbit, 1:800, ab28481, Abcam, United Kingdom), anti-Bax (Rabbit, 1:800, ab32503, Abcam, United Kingdom), anti-Bcl2 (Rabbit, 1:800, ab196495, Abcam, United Kingdom), anti-caspase 9 (Rabbit, 1:800, ab184786, Abcam, United Kingdom), and anti-NLRC5 (Rabbit, 1:800, ab117624, Abcam, United Kingdom); anti-caspase 3 (Rabbit, 1:800, #8242, Cell Signaling Tech, Danvers, MA, United States), anti-β-actin (Mouse, 1:300, sc47778, Santa Cruz, CA, United States).

    Techniques: Expressing, Western Blot, Flow Cytometry, Cytometry, Staining

    Reducing MEG3 expression inhibits EtOH-induced hepatic steatosis. (A) MEG3 successful knock down was verified by real-time PCR. (B) The levels of TG and TCH in AML-12 cells. (C) Oil Red O staining of AML-12 cells 400×. (D) Western blot analyses of PPAR-α and SREBP-1c in AML-12 cells. β-actin served as a loading control. Data shown are the mean ± SD from three independent experiments. ∗ P

    Journal: Frontiers in Pharmacology

    Article Title: The Long Non-coding RNA MEG3/miR-let-7c-5p Axis Regulates Ethanol-Induced Hepatic Steatosis and Apoptosis by Targeting NLRC5

    doi: 10.3389/fphar.2018.00302

    Figure Lengend Snippet: Reducing MEG3 expression inhibits EtOH-induced hepatic steatosis. (A) MEG3 successful knock down was verified by real-time PCR. (B) The levels of TG and TCH in AML-12 cells. (C) Oil Red O staining of AML-12 cells 400×. (D) Western blot analyses of PPAR-α and SREBP-1c in AML-12 cells. β-actin served as a loading control. Data shown are the mean ± SD from three independent experiments. ∗ P

    Article Snippet: The categories and concentrations of primary antibodies: anti-PPAR-α (Rabbit, 1:800, ab8934, Abcam, United Kingdom), SREBP-1c (Rabbit, 1:800, ab28481, Abcam, United Kingdom), anti-Bax (Rabbit, 1:800, ab32503, Abcam, United Kingdom), anti-Bcl2 (Rabbit, 1:800, ab196495, Abcam, United Kingdom), anti-caspase 9 (Rabbit, 1:800, ab184786, Abcam, United Kingdom), and anti-NLRC5 (Rabbit, 1:800, ab117624, Abcam, United Kingdom); anti-caspase 3 (Rabbit, 1:800, #8242, Cell Signaling Tech, Danvers, MA, United States), anti-β-actin (Mouse, 1:300, sc47778, Santa Cruz, CA, United States).

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Staining, Western Blot

    miR-let-7c-5p overexpression inhibits EtOH-induced hepatic steatosis. miR-let-7c-5p mimics or NC were transiently transfected into AML-12 cells, respectively. (A–C) Effects of miR-let-7c-5p on steatosis by oil red staining 400×, intracellular TCH and TG and western blot. β-actin served as a loading control. Data shown are the mean ± SD from three independent experiments. ∗ P

    Journal: Frontiers in Pharmacology

    Article Title: The Long Non-coding RNA MEG3/miR-let-7c-5p Axis Regulates Ethanol-Induced Hepatic Steatosis and Apoptosis by Targeting NLRC5

    doi: 10.3389/fphar.2018.00302

    Figure Lengend Snippet: miR-let-7c-5p overexpression inhibits EtOH-induced hepatic steatosis. miR-let-7c-5p mimics or NC were transiently transfected into AML-12 cells, respectively. (A–C) Effects of miR-let-7c-5p on steatosis by oil red staining 400×, intracellular TCH and TG and western blot. β-actin served as a loading control. Data shown are the mean ± SD from three independent experiments. ∗ P

    Article Snippet: The categories and concentrations of primary antibodies: anti-PPAR-α (Rabbit, 1:800, ab8934, Abcam, United Kingdom), SREBP-1c (Rabbit, 1:800, ab28481, Abcam, United Kingdom), anti-Bax (Rabbit, 1:800, ab32503, Abcam, United Kingdom), anti-Bcl2 (Rabbit, 1:800, ab196495, Abcam, United Kingdom), anti-caspase 9 (Rabbit, 1:800, ab184786, Abcam, United Kingdom), and anti-NLRC5 (Rabbit, 1:800, ab117624, Abcam, United Kingdom); anti-caspase 3 (Rabbit, 1:800, #8242, Cell Signaling Tech, Danvers, MA, United States), anti-β-actin (Mouse, 1:300, sc47778, Santa Cruz, CA, United States).

    Techniques: Over Expression, Transfection, Staining, Western Blot