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phosphorylated foxo1 p foxo1  (Cell Signaling Technology Inc)
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Cell Signaling Technology Inc phosphorylated foxo1 p foxo1
Fig. 3. Leucine activates the protein kinase B (Akt)/Forkhead box O1 <t>(FoxO1)</t> pathway during porcine myoblast differentiation. When the cells reached approximately 80 % confluence, porcine myoblasts were induced to differentiate with medium containing different concentrations of leucine for 3 d. Akt, phosphorylated Akt (P-Akt), phosphorylated FoxO1 <t>(P-FoxO1)</t> and <t>FoxO1</t> <t>protein</t> levels were determined by Western blot analysis. Equal loading was monitored with anti-glyceraldehyde-3- phosphate dehydrogenase (GAPDH) antibody. Mean values with their standard errors of the densitometry results from three independent experiments are shown in the lower panel. ** P < 0·01, *** P < 0·001 as compared with negative control.
Phosphorylated Foxo1 P Foxo1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Fig. 3. Leucine activates the protein kinase B (Akt)/Forkhead box O1 (FoxO1) pathway during porcine myoblast differentiation. When the cells reached approximately 80 % confluence, porcine myoblasts were induced to differentiate with medium containing different concentrations of leucine for 3 d. Akt, phosphorylated Akt (P-Akt), phosphorylated FoxO1 (P-FoxO1) and FoxO1 protein levels were determined by Western blot analysis. Equal loading was monitored with anti-glyceraldehyde-3- phosphate dehydrogenase (GAPDH) antibody. Mean values with their standard errors of the densitometry results from three independent experiments are shown in the lower panel. ** P < 0·01, *** P < 0·001 as compared with negative control.

Journal: British Journal of Nutrition

Article Title: Leucine promotes differentiation of porcine myoblasts through the protein kinase B (Akt)/Forkhead box O1 signalling pathway

doi: 10.1017/s0007114518000181

Figure Lengend Snippet: Fig. 3. Leucine activates the protein kinase B (Akt)/Forkhead box O1 (FoxO1) pathway during porcine myoblast differentiation. When the cells reached approximately 80 % confluence, porcine myoblasts were induced to differentiate with medium containing different concentrations of leucine for 3 d. Akt, phosphorylated Akt (P-Akt), phosphorylated FoxO1 (P-FoxO1) and FoxO1 protein levels were determined by Western blot analysis. Equal loading was monitored with anti-glyceraldehyde-3- phosphate dehydrogenase (GAPDH) antibody. Mean values with their standard errors of the densitometry results from three independent experiments are shown in the lower panel. ** P < 0·01, *** P < 0·001 as compared with negative control.

Article Snippet: After blocking with 5% bovine serum albumin in Trisbuffered saline/Tween-20 (TBS/T) for 2 h at room temperature, the membranes were incubated at 4°C overnight with primary antibodies against myogenin (1:50, catalogue no. sc-12732; Santa Cruz), MyoD (1:50, catalogue no. sc-304, Santa Cruz), Akt (1:1000, catalogue no. 9272; Cell Signaling), phosphorylated Akt (P-Akt) (1:1000, catalogue no. 9271; Cell Signaling), FoxO1 (1:1000, catalogue no. 2880; Cell Signaling), phosphorylated FoxO1 (P-FoxO1) (1:1000, catalogue no. 9461; Cell Signaling), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (1:3000, catalogue no. sc-20357; Cell Signaling) or β-actin (1:3000, catalogue no. sc-1616; Cell Signaling).

Techniques: Western Blot, Negative Control

Fig. 4. Leucine promotes porcine myoblast differentiation through the protein kinase B (Akt)/Forkhead box O1 (FoxO1) signalling pathway. When the cells reached approximately 80% confluence, porcine myoblasts were induced to differentiate with medium containing 4 mM leucine and 1 µM wortmannin for 3 d. Myogenin and myogenic determining factor (MyoD) protein levels (a, b) were determined by Western blot analysis. Equal loading was monitored with anti-β-actin antibody. Mean values with their standard errors of the densitometry results from three independent experiments are shown in the lower panel. Myosin heavy chain (MHC) expression (c) was analysed by immunofluorescence microscopy (4,6-diamidino-2-phenylindole (DAPI) staining also shown). *** P< 0·001 as compared with negative control. DMSO, dimethylsulfoxide.

Journal: British Journal of Nutrition

Article Title: Leucine promotes differentiation of porcine myoblasts through the protein kinase B (Akt)/Forkhead box O1 signalling pathway

doi: 10.1017/s0007114518000181

Figure Lengend Snippet: Fig. 4. Leucine promotes porcine myoblast differentiation through the protein kinase B (Akt)/Forkhead box O1 (FoxO1) signalling pathway. When the cells reached approximately 80% confluence, porcine myoblasts were induced to differentiate with medium containing 4 mM leucine and 1 µM wortmannin for 3 d. Myogenin and myogenic determining factor (MyoD) protein levels (a, b) were determined by Western blot analysis. Equal loading was monitored with anti-β-actin antibody. Mean values with their standard errors of the densitometry results from three independent experiments are shown in the lower panel. Myosin heavy chain (MHC) expression (c) was analysed by immunofluorescence microscopy (4,6-diamidino-2-phenylindole (DAPI) staining also shown). *** P< 0·001 as compared with negative control. DMSO, dimethylsulfoxide.

Article Snippet: After blocking with 5% bovine serum albumin in Trisbuffered saline/Tween-20 (TBS/T) for 2 h at room temperature, the membranes were incubated at 4°C overnight with primary antibodies against myogenin (1:50, catalogue no. sc-12732; Santa Cruz), MyoD (1:50, catalogue no. sc-304, Santa Cruz), Akt (1:1000, catalogue no. 9272; Cell Signaling), phosphorylated Akt (P-Akt) (1:1000, catalogue no. 9271; Cell Signaling), FoxO1 (1:1000, catalogue no. 2880; Cell Signaling), phosphorylated FoxO1 (P-FoxO1) (1:1000, catalogue no. 9461; Cell Signaling), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (1:3000, catalogue no. sc-20357; Cell Signaling) or β-actin (1:3000, catalogue no. sc-1616; Cell Signaling).

Techniques: Western Blot, Expressing, Immunofluorescence, Microscopy, Staining, Negative Control