phospho-akt Search Results


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  • 99
    Cell Signaling Technology Inc phosphorylated phospho akt
    Effect of GLP-1 treatment on the insulin signaling cascade in myocytes cultured in high or normal glucose media. Satellite cells were isolated from lean, healthy males (n = 6), and differentiated in either high glucose (22 mM) or normal glucose (5 mM) media for seven days. Myocytes were treated with either 100 nM insulin or GLP-1 at indicated concentrations for 30 minutes before A) immunoblotting to assess the phosphorylation status of <t>PKB/Akt,</t> GSK3 and ERK1/2 and the total protein abundance of PKB/Akt and GLP-1R. Equal loading was ascertained by immunoblotting with an antibody against β-tubulin. Effect of high (open bars) and normal (black bars) glucose on phosphorylation of PKB Ser473 (B), PKB Thr308 (C), GSK3 (D) and ERK (E), and the total protein amount of GLP-1R (F) induced by insulin and GLP-1 was quantified (n = 6), normalized to total protein and expressed as arbitrary units. Significant changes from basal levels are indicated by * (P
    Phosphorylated Phospho Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 3150 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc phosphoakt thr308
    Effect of GLP-1 treatment on the insulin signaling cascade in myocytes cultured in high or normal glucose media. Satellite cells were isolated from lean, healthy males (n = 6), and differentiated in either high glucose (22 mM) or normal glucose (5 mM) media for seven days. Myocytes were treated with either 100 nM insulin or GLP-1 at indicated concentrations for 30 minutes before A) immunoblotting to assess the phosphorylation status of <t>PKB/Akt,</t> GSK3 and ERK1/2 and the total protein abundance of PKB/Akt and GLP-1R. Equal loading was ascertained by immunoblotting with an antibody against β-tubulin. Effect of high (open bars) and normal (black bars) glucose on phosphorylation of PKB Ser473 (B), PKB Thr308 (C), GSK3 (D) and ERK (E), and the total protein amount of GLP-1R (F) induced by insulin and GLP-1 was quantified (n = 6), normalized to total protein and expressed as arbitrary units. Significant changes from basal levels are indicated by * (P
    Phosphoakt Thr308, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 37 article reviews
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    88
    Thermo Fisher phospho akt pkb
    Both PfHz and sHz can activate <t>Akt/PKB.</t> 4a3B cells were treated with PfHz (A) or sHz (B) at concentrations of 1.25 to 50 μg/ml or with equivalent volumes of PBS as a control for 10 min. After stimulation, cells were lysed and analyzed by Western
    Phospho Akt Pkb, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc p akt pkb ser473
    Both PfHz and sHz can activate <t>Akt/PKB.</t> 4a3B cells were treated with PfHz (A) or sHz (B) at concentrations of 1.25 to 50 μg/ml or with equivalent volumes of PBS as a control for 10 min. After stimulation, cells were lysed and analyzed by Western
    P Akt Pkb Ser473, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Cell Signaling Technology Inc anti phospho akt pkb
    Both PfHz and sHz can activate <t>Akt/PKB.</t> 4a3B cells were treated with PfHz (A) or sHz (B) at concentrations of 1.25 to 50 μg/ml or with equivalent volumes of PBS as a control for 10 min. After stimulation, cells were lysed and analyzed by Western
    Anti Phospho Akt Pkb, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 88 stars, based on 24 article reviews
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    93
    ABclonal phospho akt s473
    Both PfHz and sHz can activate <t>Akt/PKB.</t> 4a3B cells were treated with PfHz (A) or sHz (B) at concentrations of 1.25 to 50 μg/ml or with equivalent volumes of PBS as a control for 10 min. After stimulation, cells were lysed and analyzed by Western
    Phospho Akt S473, supplied by ABclonal, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc phospho akt pkb ser473
    Western blot analysis of the ratio between phosphorylated <t>PKB/AKT</t> versus total PKB/AKT in the gastrocnemius muscle removed from F1-HF0 and F1-HFp mice stimulated or not by insulin (the fold stimulation by insulin, relative to the mean of the corresponding control without insulin was assigned above each band shown). For quantification, each blot has been hybridized to α-tubulin and the graphs below represent means ± SE; *p
    Phospho Akt Pkb Ser473, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho akt pkb ser473/product/Cell Signaling Technology Inc
    Average 99 stars, based on 48 article reviews
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    93
    Santa Cruz Biotechnology phospho akt
    Western blot was used to detect the PI3K, <t>AKT,</t> <t>mTOR,</t> P70S6K and 4EBP1 expression
    Phospho Akt, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 946 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Effect of GLP-1 treatment on the insulin signaling cascade in myocytes cultured in high or normal glucose media. Satellite cells were isolated from lean, healthy males (n = 6), and differentiated in either high glucose (22 mM) or normal glucose (5 mM) media for seven days. Myocytes were treated with either 100 nM insulin or GLP-1 at indicated concentrations for 30 minutes before A) immunoblotting to assess the phosphorylation status of PKB/Akt, GSK3 and ERK1/2 and the total protein abundance of PKB/Akt and GLP-1R. Equal loading was ascertained by immunoblotting with an antibody against β-tubulin. Effect of high (open bars) and normal (black bars) glucose on phosphorylation of PKB Ser473 (B), PKB Thr308 (C), GSK3 (D) and ERK (E), and the total protein amount of GLP-1R (F) induced by insulin and GLP-1 was quantified (n = 6), normalized to total protein and expressed as arbitrary units. Significant changes from basal levels are indicated by * (P

    Journal: PLoS ONE

    Article Title: Glucagon Like Peptide-1-Induced Glucose Metabolism in Differentiated Human Muscle Satellite Cells Is Attenuated by Hyperglycemia

    doi: 10.1371/journal.pone.0044284

    Figure Lengend Snippet: Effect of GLP-1 treatment on the insulin signaling cascade in myocytes cultured in high or normal glucose media. Satellite cells were isolated from lean, healthy males (n = 6), and differentiated in either high glucose (22 mM) or normal glucose (5 mM) media for seven days. Myocytes were treated with either 100 nM insulin or GLP-1 at indicated concentrations for 30 minutes before A) immunoblotting to assess the phosphorylation status of PKB/Akt, GSK3 and ERK1/2 and the total protein abundance of PKB/Akt and GLP-1R. Equal loading was ascertained by immunoblotting with an antibody against β-tubulin. Effect of high (open bars) and normal (black bars) glucose on phosphorylation of PKB Ser473 (B), PKB Thr308 (C), GSK3 (D) and ERK (E), and the total protein amount of GLP-1R (F) induced by insulin and GLP-1 was quantified (n = 6), normalized to total protein and expressed as arbitrary units. Significant changes from basal levels are indicated by * (P

    Article Snippet: Phospho-Akt/PKB (Ser473 ), phospho-Akt/PKB (Thr308 ), phospho-GSK3α/β (Ser21/9 ), phospho-ERK1/2 (Thr202 /Tyr204 ), phospho-PKCζ/λ (Thr410/403 ), anti-PKB and anti-β-tubulin, antibodies were from Cell Signalling Technology (Boston, MA).

    Techniques: Cell Culture, Isolation

    The effect of GLP-1 on glucose uptake in myocytes cultured in normal glucose media is PI3K-dependent. Satellite cells were isolated from lean, healthy males (n = 6), and differentiated in either high glucose (22 mM, open bars) or normal glucose (5 mM, black bars) media for seven days. Myocytes were treated with 100 nM wortmannin (40 minutes) in the absence or presence of either 100 nM insulin or 100 nM GLP-1 for the penultimate 30 minutes before assessing 2-deoxyglucose uptake in to myocytes (A) cultured in high glucose (22 mM) or (B) normal glucose (5 mM) media. (C) Lysates were immunoblotted for phosphorylation status of PKB/Akt and PKCζ/λ and total protein amount of PKB/Akt under the same conditions. Immunoblots were quantified (n = 6), normalized to total protein and expressed as arbitrary units (D and E). (F) Total protein amount of GLUT4 was assessed by immunoblot and quantified (n = 5). Significant changes from basal levels are indicated by * (P

    Journal: PLoS ONE

    Article Title: Glucagon Like Peptide-1-Induced Glucose Metabolism in Differentiated Human Muscle Satellite Cells Is Attenuated by Hyperglycemia

    doi: 10.1371/journal.pone.0044284

    Figure Lengend Snippet: The effect of GLP-1 on glucose uptake in myocytes cultured in normal glucose media is PI3K-dependent. Satellite cells were isolated from lean, healthy males (n = 6), and differentiated in either high glucose (22 mM, open bars) or normal glucose (5 mM, black bars) media for seven days. Myocytes were treated with 100 nM wortmannin (40 minutes) in the absence or presence of either 100 nM insulin or 100 nM GLP-1 for the penultimate 30 minutes before assessing 2-deoxyglucose uptake in to myocytes (A) cultured in high glucose (22 mM) or (B) normal glucose (5 mM) media. (C) Lysates were immunoblotted for phosphorylation status of PKB/Akt and PKCζ/λ and total protein amount of PKB/Akt under the same conditions. Immunoblots were quantified (n = 6), normalized to total protein and expressed as arbitrary units (D and E). (F) Total protein amount of GLUT4 was assessed by immunoblot and quantified (n = 5). Significant changes from basal levels are indicated by * (P

    Article Snippet: Phospho-Akt/PKB (Ser473 ), phospho-Akt/PKB (Thr308 ), phospho-GSK3α/β (Ser21/9 ), phospho-ERK1/2 (Thr202 /Tyr204 ), phospho-PKCζ/λ (Thr410/403 ), anti-PKB and anti-β-tubulin, antibodies were from Cell Signalling Technology (Boston, MA).

    Techniques: Cell Culture, Isolation, Western Blot

    Effect of GLP-1 and/or insulin on glucose uptake and GLUT4 protein. Satellite cells were isolated from lean, healthy males (n = 6), and differentiated in either high glucose (22 mM, open bars) or normal glucose (5 mM, black bars) media for seven days. Myocytes were treated with either 100 nM insulin and/or 100 nM GLP-1 for 30 minutes before either (A) assessing 2-deoxyglucose uptake or (B) immunoblotting to assess phosphorylation status of PKB/Akt and total protein amount of PKB/Akt or (C) immunoblotting to assess the protein level of GLUT4. The effect of high (open bars) and normal (black bars) glucose on GLUT4 protein level was quantified ((D); n = 6), normalized to total protein and expressed as arbitrary units. Significant changes from basal levels are indicated by * (P

    Journal: PLoS ONE

    Article Title: Glucagon Like Peptide-1-Induced Glucose Metabolism in Differentiated Human Muscle Satellite Cells Is Attenuated by Hyperglycemia

    doi: 10.1371/journal.pone.0044284

    Figure Lengend Snippet: Effect of GLP-1 and/or insulin on glucose uptake and GLUT4 protein. Satellite cells were isolated from lean, healthy males (n = 6), and differentiated in either high glucose (22 mM, open bars) or normal glucose (5 mM, black bars) media for seven days. Myocytes were treated with either 100 nM insulin and/or 100 nM GLP-1 for 30 minutes before either (A) assessing 2-deoxyglucose uptake or (B) immunoblotting to assess phosphorylation status of PKB/Akt and total protein amount of PKB/Akt or (C) immunoblotting to assess the protein level of GLUT4. The effect of high (open bars) and normal (black bars) glucose on GLUT4 protein level was quantified ((D); n = 6), normalized to total protein and expressed as arbitrary units. Significant changes from basal levels are indicated by * (P

    Article Snippet: Phospho-Akt/PKB (Ser473 ), phospho-Akt/PKB (Thr308 ), phospho-GSK3α/β (Ser21/9 ), phospho-ERK1/2 (Thr202 /Tyr204 ), phospho-PKCζ/λ (Thr410/403 ), anti-PKB and anti-β-tubulin, antibodies were from Cell Signalling Technology (Boston, MA).

    Techniques: Isolation

    Decrease in Akt phosphorylation facilitated by human insulin in cells of fat body in the hyperlipidemic silkworm. ( A , B ) Silkworms were fed a normal diet (N.D.) or a diet containing 10% (w/w) glucose (G.D.) for 18 h, and then the silkworm fat bodies were isolated. ( A ) Fat bodies were cultured in Grace’s insect medium with or without human insulin (final conc. 160 μg/ml) at 27 °C for 0-20 min. ( B ) Fat bodies were cultured in Grace’s insect medium with or without human insulin (final conc. 0-160 μg/ml) at 27 °C for 15 min. ( C ) Silkworms were fed a normal diet (N.D.) for 18 h, and then the fat bodies were isolated. Fat bodies were cultured in Grace’s insect medium with 0.2% BSA or palmitate (final conc. 500 μM) with 0.2% BSA at 27 °C for 1 h. Human insulin (final conc. 160 μg/ml) or Grace’s insect medium were added to the culture medium, and the fat bodies were further incubated at 27 °C for 20 min. Phosphorylated Akt and β-actin were determined by Western blot analysis. Samples were loaded in the same gel. Cropped blots were used. Full-length blots are presented in Supplementary Fig. 6 .

    Journal: Scientific Reports

    Article Title: Diabetic silkworms for evaluation of therapeutically effective drugs against type II diabetes

    doi: 10.1038/srep10722

    Figure Lengend Snippet: Decrease in Akt phosphorylation facilitated by human insulin in cells of fat body in the hyperlipidemic silkworm. ( A , B ) Silkworms were fed a normal diet (N.D.) or a diet containing 10% (w/w) glucose (G.D.) for 18 h, and then the silkworm fat bodies were isolated. ( A ) Fat bodies were cultured in Grace’s insect medium with or without human insulin (final conc. 160 μg/ml) at 27 °C for 0-20 min. ( B ) Fat bodies were cultured in Grace’s insect medium with or without human insulin (final conc. 0-160 μg/ml) at 27 °C for 15 min. ( C ) Silkworms were fed a normal diet (N.D.) for 18 h, and then the fat bodies were isolated. Fat bodies were cultured in Grace’s insect medium with 0.2% BSA or palmitate (final conc. 500 μM) with 0.2% BSA at 27 °C for 1 h. Human insulin (final conc. 160 μg/ml) or Grace’s insect medium were added to the culture medium, and the fat bodies were further incubated at 27 °C for 20 min. Phosphorylated Akt and β-actin were determined by Western blot analysis. Samples were loaded in the same gel. Cropped blots were used. Full-length blots are presented in Supplementary Fig. 6 .

    Article Snippet: The relative amount of phosphorylated JNK or phosphorylated Akt or phosphorylated AMPK to β-actin was determined.

    Techniques: Isolation, Cell Culture, Incubation, Western Blot

    BAFF signal transduction in human mesangial cells. Human mesangial cells were subjected to serum starvation for 4 h, and then BAFF treatment (Veh, 5, 20, 100 ng/mL, indicated with the symbol ( ) for 10 min. The harvested cells were lysed for western blot, with antibodies used as indicated ( a ). b This experiment was repeated independently at least three times and expression ratios of target proteins were normalized to GAPDH or the unphosphorylated form of the protein. Specifically, NF-κBp100: NF-κBp100/GAPDH; p-NF-κBp65: p-NF-κBp65/NF-κBp65; p-Akt: p-Akt/Akt; p-Erk: p-Erk/Erk; p-p38: p-p38/p38. Statistical significance is indicated as * p

    Journal: BMC Nephrology

    Article Title: BAFF promotes proliferation of human mesangial cells through interaction with BAFF-R

    doi: 10.1186/s12882-015-0064-y

    Figure Lengend Snippet: BAFF signal transduction in human mesangial cells. Human mesangial cells were subjected to serum starvation for 4 h, and then BAFF treatment (Veh, 5, 20, 100 ng/mL, indicated with the symbol ( ) for 10 min. The harvested cells were lysed for western blot, with antibodies used as indicated ( a ). b This experiment was repeated independently at least three times and expression ratios of target proteins were normalized to GAPDH or the unphosphorylated form of the protein. Specifically, NF-κBp100: NF-κBp100/GAPDH; p-NF-κBp65: p-NF-κBp65/NF-κBp65; p-Akt: p-Akt/Akt; p-Erk: p-Erk/Erk; p-p38: p-p38/p38. Statistical significance is indicated as * p

    Article Snippet: Reagents Major reagents included recombinant human BAFF (310–13, Peprotech, Rocky Hill, NJ, USA);BAFF-R antibody for flow cytometry and western blot (14–9117, eBioscience, San Diego, CA, USA); BAFF-R Fc chimera (1162-BR-050, R & D Systems, Minneapolis, MN, USA); phospho-Akt (2965) and Akt antibodies (9272, Cell Signaling Technology, Danvers, MA, USA); phospho-Erk (Thr202/Tyr204) (9106) and Erk antibodies (9102, Cell Signaling Technology); phospho-MAPKp38 (Thr180/Tyr182) (9211) and MAPKp38 antibodies (9212, Cell Signaling Technology); phospho-NF-κB p65 (Ser536) (3033) and NF-κB p65 antibodies (4764, Cell Signaling Technology); NF-κB p100 antibody(BS1247, Bioworld, China); Na+ /K+ -ATPase antibody (BS4259, Bioworld); carboxyfluoresceinsuccinimidyl ester (CFSE) (C34554, Life Technologies, Carlsbad, CA, USA); reverse transcription (RR014A) and real-time PCR kits (DRR036A, TAKARA, Shiga, Japan); TRIzol (15596–18) and DNaseI (AM2235, Life Technologies); protein extraction buffer (P0013, Beyotime, China); MTS Proliferation Assay kit (G3582, Promega, Madison, WI, USA); and a membrane protein extraction kit (89842, Pierce, Thermo Scientific, Waltham, MA, USA).

    Techniques: Transduction, Western Blot, Expressing

    Ritonavir inhibits Ser473 pAkt and expression of constitutively active Akt reduces ritonavir sensitivity of breast cancer lines

    Journal:

    Article Title: Effects of HIV Protease Inhibitor Ritonavir on Akt-Regulated Cell Proliferation in Breast Cancer

    doi: 10.1158/1078-0432.CCR-05-1167

    Figure Lengend Snippet: Ritonavir inhibits Ser473 pAkt and expression of constitutively active Akt reduces ritonavir sensitivity of breast cancer lines

    Article Snippet: The primary rabbit polyclonal antisera included anti-bodies to human ER-α (sc-7207; Santa Cruz Biotechnology), Akt (9272; Cell Signaling Technology, Beverly, MA), phosphorylated Akt (pAkt) recognizing phosphorylated Ser473 (9271; Cell Signaling Technology), Akt phosphosubstrate antibody recognizing the motif (R/K)X(R/K)-XX(pT/pS) (9611; Cell Signaling Technology), extracellular signal-regulated kinase (9102; Cell Signaling Technology), phosphorylated extracellular signal-regulated kinase antibody recognizing phosphorylated Thr202 and Thr204 (9101; Cell Signaling Technology), Hsp90α (SPS771; Stressgen), Rb (554136; Becton Dickinson, San Jose, CA), phosphorylated Rb (pRb; 9308; Cell Signaling Technology), CDK2 (sc-163; Santa Cruz Biotechnology), CDK4 (sc-260; Santa Cruz Biotechnology), CDK6 (sc-177; Santa Cruz Biotechnology), cyclin D1 (sc-718; Santa Cruz Biotechnology), and cyclin E (sc-481; Santa Cruz Biotechnology).

    Techniques: Expressing

    The increase in AKT phosphorylation in primary cultured Schwann cells (pSC) by DHA is abolished by PI3K inhibitors. pSC were treated with DHA (50 µM) for (1–24 hr) (a). pSC were treated with DHA in the presence or absence of LY294002(40 µM), BKM120 (2 µM) and for 6 hrs (b). pSC cell lysates were prepared and subjected to Western blot analysis using specific antibodies against AKTp‐Ser473, AKTp‐Thr308, and total AKT. The blots were then analyzed using the Li‐Cor Odyssey system. The data represent mean ± SEM of at least three independent experiments. A representative Western blot is shown above each bar graph. * p

    Journal: Brain and Behavior

    Article Title: Protective effect of docosahexaenoic acid on lipotoxicity‐mediated cell death in Schwann cells: Implication of PI3K/AKT and mTORC2 pathways. Protective effect of docosahexaenoic acid on lipotoxicity‐mediated cell death in Schwann cells: Implication of PI3K/AKT and mTORC2 pathways

    doi: 10.1002/brb3.1123

    Figure Lengend Snippet: The increase in AKT phosphorylation in primary cultured Schwann cells (pSC) by DHA is abolished by PI3K inhibitors. pSC were treated with DHA (50 µM) for (1–24 hr) (a). pSC were treated with DHA in the presence or absence of LY294002(40 µM), BKM120 (2 µM) and for 6 hrs (b). pSC cell lysates were prepared and subjected to Western blot analysis using specific antibodies against AKTp‐Ser473, AKTp‐Thr308, and total AKT. The blots were then analyzed using the Li‐Cor Odyssey system. The data represent mean ± SEM of at least three independent experiments. A representative Western blot is shown above each bar graph. * p

    Article Snippet: Finally, we obtained the antibodies to total AKT (mouse, Cat# 2920, http://scicrunch.org/resolver/AB_1147620 ) and phosphorylated AKT Ser473 (rabbit, Cat# 4060, http://scicrunch.org/resolver/AB_2315049 ) or Thr308 (rabbit, Cat# 2965, http://scicrunch.org/resolver/AB_2255933 ), and rapamycin from Cell signaling Technology (Danver, MA), the actin (mouse, Cat# A5441, http://scicrunch.org/resolver/AB_476744 ) from Sigma‐Aldrich (St Louis, MO) and Torin 1 from Tocris Bioscience (Bristol, UK).

    Techniques: Cell Culture, Western Blot

    DHA eliminates apoptotic cell death and restores AKT phosphorylation in primary cultured Schwann cells (pSC) under PA‐LTx. pSC were treated with BSA alone (CTL), with PA:BSA (2:1) alone, with DHA (50 µM) alone or co‐treated with PA:BSA (2:1) and DHA (50 µM) for 48 hr. Nuclear morphology was determined by Hoechst staining. Nuclear condensations are indicated with white arrows (a). The pSC culture lysates were prepared and subjected to Western blot analysis using specific antibodies against AKTp‐Ser473, AKTp‐Thr308, and total AKT protein. The blots were then analyzed using the Li‐Cor Odyssey system. A representative Western blot is shown by each bar graph (b). The data represent mean ± SEM of at least four independent experiments. * p

    Journal: Brain and Behavior

    Article Title: Protective effect of docosahexaenoic acid on lipotoxicity‐mediated cell death in Schwann cells: Implication of PI3K/AKT and mTORC2 pathways. Protective effect of docosahexaenoic acid on lipotoxicity‐mediated cell death in Schwann cells: Implication of PI3K/AKT and mTORC2 pathways

    doi: 10.1002/brb3.1123

    Figure Lengend Snippet: DHA eliminates apoptotic cell death and restores AKT phosphorylation in primary cultured Schwann cells (pSC) under PA‐LTx. pSC were treated with BSA alone (CTL), with PA:BSA (2:1) alone, with DHA (50 µM) alone or co‐treated with PA:BSA (2:1) and DHA (50 µM) for 48 hr. Nuclear morphology was determined by Hoechst staining. Nuclear condensations are indicated with white arrows (a). The pSC culture lysates were prepared and subjected to Western blot analysis using specific antibodies against AKTp‐Ser473, AKTp‐Thr308, and total AKT protein. The blots were then analyzed using the Li‐Cor Odyssey system. A representative Western blot is shown by each bar graph (b). The data represent mean ± SEM of at least four independent experiments. * p

    Article Snippet: Finally, we obtained the antibodies to total AKT (mouse, Cat# 2920, http://scicrunch.org/resolver/AB_1147620 ) and phosphorylated AKT Ser473 (rabbit, Cat# 4060, http://scicrunch.org/resolver/AB_2315049 ) or Thr308 (rabbit, Cat# 2965, http://scicrunch.org/resolver/AB_2255933 ), and rapamycin from Cell signaling Technology (Danver, MA), the actin (mouse, Cat# A5441, http://scicrunch.org/resolver/AB_476744 ) from Sigma‐Aldrich (St Louis, MO) and Torin 1 from Tocris Bioscience (Bristol, UK).

    Techniques: Cell Culture, CTL Assay, Staining, Western Blot

    PA‐LTx induced apoptosis and a decrease in AKT phosphorylation in primary Schwann cells (pSC). pSC were treated with BSA alone (control), PA:BSA (2:1) for 24–48 hr. (a) Cell viability was assessed by crystal violet assay. (b) The effect of PA:BSA (2:1) on AKT phosphorylation was examined by Western blot. The pSC cell lysates from control cultures (CTL) exposed to BSA alone and cultures exposed to PA:BSA (2:1) at 1, 3, 6, 12, and 24 hr (hrs.) were prepared and subjected to specific antibodies against AKTp‐Ser473, AKTp‐Thr308 and to total AKT. The blots were then analyzed using the Li‐Cor Odyssey system. A representative Western blot is shown above each bar graph. The data represent mean ± SE of at least four independent experiments. * p

    Journal: Brain and Behavior

    Article Title: Protective effect of docosahexaenoic acid on lipotoxicity‐mediated cell death in Schwann cells: Implication of PI3K/AKT and mTORC2 pathways. Protective effect of docosahexaenoic acid on lipotoxicity‐mediated cell death in Schwann cells: Implication of PI3K/AKT and mTORC2 pathways

    doi: 10.1002/brb3.1123

    Figure Lengend Snippet: PA‐LTx induced apoptosis and a decrease in AKT phosphorylation in primary Schwann cells (pSC). pSC were treated with BSA alone (control), PA:BSA (2:1) for 24–48 hr. (a) Cell viability was assessed by crystal violet assay. (b) The effect of PA:BSA (2:1) on AKT phosphorylation was examined by Western blot. The pSC cell lysates from control cultures (CTL) exposed to BSA alone and cultures exposed to PA:BSA (2:1) at 1, 3, 6, 12, and 24 hr (hrs.) were prepared and subjected to specific antibodies against AKTp‐Ser473, AKTp‐Thr308 and to total AKT. The blots were then analyzed using the Li‐Cor Odyssey system. A representative Western blot is shown above each bar graph. The data represent mean ± SE of at least four independent experiments. * p

    Article Snippet: Finally, we obtained the antibodies to total AKT (mouse, Cat# 2920, http://scicrunch.org/resolver/AB_1147620 ) and phosphorylated AKT Ser473 (rabbit, Cat# 4060, http://scicrunch.org/resolver/AB_2315049 ) or Thr308 (rabbit, Cat# 2965, http://scicrunch.org/resolver/AB_2255933 ), and rapamycin from Cell signaling Technology (Danver, MA), the actin (mouse, Cat# A5441, http://scicrunch.org/resolver/AB_476744 ) from Sigma‐Aldrich (St Louis, MO) and Torin 1 from Tocris Bioscience (Bristol, UK).

    Techniques: Crystal Violet Assay, Western Blot, CTL Assay

    The Effect of PI3K/AKT inhibitors on primary Schwann cells (pSC) viability. pSC cultures were treated with PI3K inhibitors LY290042 (a), and BKM120 (b) for 48 hr followed by crystal violet assay to measure cell viability. The effect of LY290042 (c) and BKM120 (d) on AKT phosphorylation was examined by Western blot. The pSC cells lysates were prepared and subjected to specific antibodies against AKTp‐Ser473, AKTp‐Thr308, and total AKT protein. The blots were then analyzed using the Li‐Cor Odyssey system. A representative Western blot is shown above each bar graph. The data represent mean ± SE of at least four independent experiments. * p

    Journal: Brain and Behavior

    Article Title: Protective effect of docosahexaenoic acid on lipotoxicity‐mediated cell death in Schwann cells: Implication of PI3K/AKT and mTORC2 pathways. Protective effect of docosahexaenoic acid on lipotoxicity‐mediated cell death in Schwann cells: Implication of PI3K/AKT and mTORC2 pathways

    doi: 10.1002/brb3.1123

    Figure Lengend Snippet: The Effect of PI3K/AKT inhibitors on primary Schwann cells (pSC) viability. pSC cultures were treated with PI3K inhibitors LY290042 (a), and BKM120 (b) for 48 hr followed by crystal violet assay to measure cell viability. The effect of LY290042 (c) and BKM120 (d) on AKT phosphorylation was examined by Western blot. The pSC cells lysates were prepared and subjected to specific antibodies against AKTp‐Ser473, AKTp‐Thr308, and total AKT protein. The blots were then analyzed using the Li‐Cor Odyssey system. A representative Western blot is shown above each bar graph. The data represent mean ± SE of at least four independent experiments. * p

    Article Snippet: Finally, we obtained the antibodies to total AKT (mouse, Cat# 2920, http://scicrunch.org/resolver/AB_1147620 ) and phosphorylated AKT Ser473 (rabbit, Cat# 4060, http://scicrunch.org/resolver/AB_2315049 ) or Thr308 (rabbit, Cat# 2965, http://scicrunch.org/resolver/AB_2255933 ), and rapamycin from Cell signaling Technology (Danver, MA), the actin (mouse, Cat# A5441, http://scicrunch.org/resolver/AB_476744 ) from Sigma‐Aldrich (St Louis, MO) and Torin 1 from Tocris Bioscience (Bristol, UK).

    Techniques: Crystal Violet Assay, Western Blot

    BASCs express p110α and have Ser473-phosphorylated AKT. Immunofluorescent staining of tissue sections to detect triply stained (CCSP/SPC/p110α or pAKT) cells at terminal bronchi. BASCs encircled (x40 magnification). Calibration bar in lower right panel represents 50 μm.

    Journal: PLoS ONE

    Article Title: Phosphatidylinositol 3-Kinase Mediates Bronchioalveolar Stem Cell Expansion in Mouse Models of Oncogenic K-ras-Induced Lung Cancer

    doi: 10.1371/journal.pone.0002220

    Figure Lengend Snippet: BASCs express p110α and have Ser473-phosphorylated AKT. Immunofluorescent staining of tissue sections to detect triply stained (CCSP/SPC/p110α or pAKT) cells at terminal bronchi. BASCs encircled (x40 magnification). Calibration bar in lower right panel represents 50 μm.

    Article Snippet: Reagents Antibodies purchased for these studies include rabbit anti-p110α (sc-7174), p110β (sc-7175), SPC (sc-13979), goat anti-CC10 (sc-9772) and PTEN (sc-6818) (Santa Cruz Biotechnology, Santa Cruz, CA), rabbit anti-total AKT (9272), Ser473-phosphorylated AKT (9271), Ser21/9-phosphorylated GSK3α/β (9331), total GSK3 (9332), cleaved caspase-3 (9661), Poly (ADP-ribose) polymerase (9542), phosphorylated-histone H3 (9701), Ser28-phosphorylated histone H3 (9713P) (Cell Signaling Technologies, Danvers, MA), rabbit anti-SPC (WRAB-SPC, Seven Hills Bioreagents, Cincinnati, OH), rabbit anti-CCSP (07-623, Upstate Biotechnologies, Lake Placid, NY), FITC-conjugated anti-Sca-1 (557405), biotin-conjugated anti-CD45 (553771) biotin-conjugated-CD31 (558737), PE-conjugated anti-CD34 (12-0341-33, eBioscience), anti-rabbit IgG Alexa Flour 488 (A11008), and anti-goat IgG Alexa Flour 594 (A11058) (Invitrogen, Carlsbad, CA).

    Techniques: Staining

    Both PfHz and sHz can activate Akt/PKB. 4a3B cells were treated with PfHz (A) or sHz (B) at concentrations of 1.25 to 50 μg/ml or with equivalent volumes of PBS as a control for 10 min. After stimulation, cells were lysed and analyzed by Western

    Journal:

    Article Title: Induction of Nitric Oxide Synthase and Activation of Signaling Proteins in Anopheles Mosquitoes by the Malaria Pigment, Hemozoin ▿

    doi: 10.1128/IAI.00645-07

    Figure Lengend Snippet: Both PfHz and sHz can activate Akt/PKB. 4a3B cells were treated with PfHz (A) or sHz (B) at concentrations of 1.25 to 50 μg/ml or with equivalent volumes of PBS as a control for 10 min. After stimulation, cells were lysed and analyzed by Western

    Article Snippet: Membranes were blocked overnight at 4°C with Tris-buffered saline (pH 7.4) containing 0.1% Tween 20 and 5% dried skim milk and incubated with a 1:1,000 dilution of polyclonal rabbit anti-phospho-transforming growth factor β-associated kinase 1 (anti-phospho-TAK1) (pT184; Cell Signaling Technology), anti-phospho-Akt/PKB (pT308; Biosource International), anti-phospho-aPKC zeta/lambda (anti-phospho-aPKCζ/λ) (pT410/403; Cell Signaling Technology), or anti-phospho-p38 MAPK (pT180pY182; Cayman Chemical) antiserum or a 1:10,000 dilution of monoclonal mouse anti-phospho-ERK1/2 (pT185/pY187; Sigma) antiserum for 6 h at room temperature.

    Techniques: Western Blot

    Western blot analysis of the ratio between phosphorylated PKB/AKT versus total PKB/AKT in the gastrocnemius muscle removed from F1-HF0 and F1-HFp mice stimulated or not by insulin (the fold stimulation by insulin, relative to the mean of the corresponding control without insulin was assigned above each band shown). For quantification, each blot has been hybridized to α-tubulin and the graphs below represent means ± SE; *p

    Journal: PLoS ONE

    Article Title: Metabolic Outcome of Female Mice Exposed to a Mixture of Low-Dose Pollutants in a Diet-Induced Obesity Model

    doi: 10.1371/journal.pone.0124015

    Figure Lengend Snippet: Western blot analysis of the ratio between phosphorylated PKB/AKT versus total PKB/AKT in the gastrocnemius muscle removed from F1-HF0 and F1-HFp mice stimulated or not by insulin (the fold stimulation by insulin, relative to the mean of the corresponding control without insulin was assigned above each band shown). For quantification, each blot has been hybridized to α-tubulin and the graphs below represent means ± SE; *p

    Article Snippet: Immunoblotting was performed using rabbit polyclonal antibodies directed against ERα (sc-542, Santa Cruz Biotechnology, CliniSciences, Nanterre, France), EST (sc-292049, Santa Cruz Biotechnology), phospho-AKT/PKB (Ser473) (#4060, Cell Signaling Technology Europe, Leiden, The Nederlands) and total AKT/PKB (#9272, Cell Signaling Technology Europe), or mouse monoclonal antibodies directed against α-tubulin (sc-5286, Santa Cruz Biotechnology).

    Techniques: Western Blot, Mouse Assay

    (A) Effect of the mixture of pollutants on hepatic mRNA expression of xenobiotic nuclear receptors; (B) Analysis by Western blot of the ratio between phosphorylated PKB/AKT versus total PKB/AKT in liver removed from F1-HF0 and F1-HFp mice stimulated or not by insulin. For quantification, each blot has been hybridized to α-tubulin and the graphs below represent means ± SE; n = 7–8 mice. (C) and (D) Hepatic expression of Nr1c1 and of several PPARα-regulated genes (C) and of genes encoding proteins involved in lipogenesis (D). Results are means ± SE; *p

    Journal: PLoS ONE

    Article Title: Metabolic Outcome of Female Mice Exposed to a Mixture of Low-Dose Pollutants in a Diet-Induced Obesity Model

    doi: 10.1371/journal.pone.0124015

    Figure Lengend Snippet: (A) Effect of the mixture of pollutants on hepatic mRNA expression of xenobiotic nuclear receptors; (B) Analysis by Western blot of the ratio between phosphorylated PKB/AKT versus total PKB/AKT in liver removed from F1-HF0 and F1-HFp mice stimulated or not by insulin. For quantification, each blot has been hybridized to α-tubulin and the graphs below represent means ± SE; n = 7–8 mice. (C) and (D) Hepatic expression of Nr1c1 and of several PPARα-regulated genes (C) and of genes encoding proteins involved in lipogenesis (D). Results are means ± SE; *p

    Article Snippet: Immunoblotting was performed using rabbit polyclonal antibodies directed against ERα (sc-542, Santa Cruz Biotechnology, CliniSciences, Nanterre, France), EST (sc-292049, Santa Cruz Biotechnology), phospho-AKT/PKB (Ser473) (#4060, Cell Signaling Technology Europe, Leiden, The Nederlands) and total AKT/PKB (#9272, Cell Signaling Technology Europe), or mouse monoclonal antibodies directed against α-tubulin (sc-5286, Santa Cruz Biotechnology).

    Techniques: Expressing, Western Blot, Mouse Assay

    Western blot was used to detect the PI3K, AKT, mTOR, P70S6K and 4EBP1 expression

    Journal: International Journal of Ophthalmology

    Article Title: PI3K/AKT/mTOR signaling pathway inhibitors in proliferation of retinal pigment epithelial cells

    doi: 10.3980/j.issn.2222-3959.2012.06.05

    Figure Lengend Snippet: Western blot was used to detect the PI3K, AKT, mTOR, P70S6K and 4EBP1 expression

    Article Snippet: Similarly, as we shown in and , levels of phospho-AKT, phospho-mTOR, phospho-4EBP1 and phospho-p70S6K were significantly decreased in D407 cells treated with LY294002 compared with the control group ( P < 0.05).

    Techniques: Western Blot, Expressing