phospho-akt ser473 Search Results


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    Cell Signaling Technology Inc phosphoakt ser 473
    Phosphoakt Ser 473, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phosphoakt ser 473/product/Cell Signaling Technology Inc
    Average 99 stars, based on 26 article reviews
    Price from $9.99 to $1999.99
    phosphoakt ser 473 - by Bioz Stars, 2020-08
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    99
    Cell Signaling Technology Inc phospho akt ser 473
    Effects of CO-EtOAc on the regulation of insulin receptor-mediated signaling. Relative protein levels of hepatic: ( A ) IRS-1 (phosphorylated IRS-1 at Ser-307 and total IRS-1); and ( B ) <t>Akt</t> (phosphorylated Akt at <t>Ser-473</t> and total Akt) were detected by Western blot analysis. Data are represented as mean ± SEM ( n = 8–10). Values with different letters are statistically different ( p
    Phospho Akt Ser 473, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 514 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho akt ser 473/product/Cell Signaling Technology Inc
    Average 99 stars, based on 514 article reviews
    Price from $9.99 to $1999.99
    phospho akt ser 473 - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    99
    Cell Signaling Technology Inc phospho ser 473 akt
    Phosphorylation of <t>Akt</t> and GSK3β and dissociation of GSK3β/β-catenin complexes in AZ-521 cells infected with H. pylori , but not an isogenic VacA-knock-out mutant strain. AZ-521 cells were infected for 6 h with H. pylori ATCC43504 ( WT strain ) or its isogenic VacA-knock-out mutant strain (Δ VacA strain ). Cells incubated without infection (uninfected cells) were used as a negative control. A , after incubation, phosphorylation of Akt and GSK3β in cells was determined by Western blot analysis with <t>anti-phospho-Ser-473</t> Akt, Akt phospho-Ser-9 GSK3β, and GSK3β antibodies. Quantification of phospho-Ser-473 Akt and phospho-Ser-9 GSK3β obtained with control ( open bars ), WT strain ( black bars ), and Δ VacA strain ( gray bars ) was determined by densitometry. Data are means ± S.E. of values from triplicate experiments, with an n = 3 per experiment. Statistical significance: * , p
    Phospho Ser 473 Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 161 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho ser 473 akt/product/Cell Signaling Technology Inc
    Average 99 stars, based on 161 article reviews
    Price from $9.99 to $1999.99
    phospho ser 473 akt - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    99
    Cell Signaling Technology Inc anti phospho akt ser 473 antibodies
    FoxO3a expression decreases on collagen. A , serum-starved human lung fibroblasts were attached to collagen (100 μg/ml, upper panel )-coated plates as a function of time. <t>Akt</t> and <t>Ser-473-phosphorylated</t> Akt levels were then measured. B , human lung fibroblasts were serum-starved for 2 days followed by attachment to collagen-coated plates as a function of time. FoxO3a, FoxO1, and FoxO4 expression levels were measured ( upper and lower panels , respectively). Glyceraldehyde-3-phosphate dehydrogenase ( GAPDH ) and actin were used as a loading control. C , serum-starved human lung fibroblasts were attached to fibronectin- (10 μg/ml), vitronectin- (10 μg/ml), and laminin (10 μg/ml)-coated plates as a function of time. FoxO3a expression levels were measured. Actin was used as a loading control.
    Anti Phospho Akt Ser 473 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho akt ser 473 antibodies/product/Cell Signaling Technology Inc
    Average 99 stars, based on 75 article reviews
    Price from $9.99 to $1999.99
    anti phospho akt ser 473 antibodies - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    Image Search Results


    Effects of CO-EtOAc on the regulation of insulin receptor-mediated signaling. Relative protein levels of hepatic: ( A ) IRS-1 (phosphorylated IRS-1 at Ser-307 and total IRS-1); and ( B ) Akt (phosphorylated Akt at Ser-473 and total Akt) were detected by Western blot analysis. Data are represented as mean ± SEM ( n = 8–10). Values with different letters are statistically different ( p

    Journal: Nutrients

    Article Title: Chinese Olive (Canarium album L.) Fruit Extract Attenuates Metabolic Dysfunction in Diabetic Rats

    doi: 10.3390/nu9101123

    Figure Lengend Snippet: Effects of CO-EtOAc on the regulation of insulin receptor-mediated signaling. Relative protein levels of hepatic: ( A ) IRS-1 (phosphorylated IRS-1 at Ser-307 and total IRS-1); and ( B ) Akt (phosphorylated Akt at Ser-473 and total Akt) were detected by Western blot analysis. Data are represented as mean ± SEM ( n = 8–10). Values with different letters are statistically different ( p

    Article Snippet: The blots were blocked with 5% (w /v ) skim milk and probed with antibodies against CPT-1 (Abcam, Cambridge, MA, USA), AMPKα, phospho-AMPKα (Thr-172), LDLR, ABCA1 (Gene Tex, Irvine, CA, USA), IRS-1, phospho-IRS-1 (Ser-307), Akt, and phospho-Akt (Ser-473) (Cell Signaling Technology, Beverly, MA, USA) separately, followed by goat anti-rabbit or mouse IgG horseradish peroxidase (HRP)-conjugated secondary antibodies.

    Techniques: Western Blot

    Phosphorylation of Akt and GSK3β and dissociation of GSK3β/β-catenin complexes in AZ-521 cells infected with H. pylori , but not an isogenic VacA-knock-out mutant strain. AZ-521 cells were infected for 6 h with H. pylori ATCC43504 ( WT strain ) or its isogenic VacA-knock-out mutant strain (Δ VacA strain ). Cells incubated without infection (uninfected cells) were used as a negative control. A , after incubation, phosphorylation of Akt and GSK3β in cells was determined by Western blot analysis with anti-phospho-Ser-473 Akt, Akt phospho-Ser-9 GSK3β, and GSK3β antibodies. Quantification of phospho-Ser-473 Akt and phospho-Ser-9 GSK3β obtained with control ( open bars ), WT strain ( black bars ), and Δ VacA strain ( gray bars ) was determined by densitometry. Data are means ± S.E. of values from triplicate experiments, with an n = 3 per experiment. Statistical significance: * , p

    Journal: The Journal of Biological Chemistry

    Article Title: Helicobacter pylori VacA-induced Inhibition of GSK3 through the PI3K/Akt Signaling Pathway * VacA-induced Inhibition of GSK3 through the PI3K/Akt Signaling Pathway * S⃞

    doi: 10.1074/jbc.M806981200

    Figure Lengend Snippet: Phosphorylation of Akt and GSK3β and dissociation of GSK3β/β-catenin complexes in AZ-521 cells infected with H. pylori , but not an isogenic VacA-knock-out mutant strain. AZ-521 cells were infected for 6 h with H. pylori ATCC43504 ( WT strain ) or its isogenic VacA-knock-out mutant strain (Δ VacA strain ). Cells incubated without infection (uninfected cells) were used as a negative control. A , after incubation, phosphorylation of Akt and GSK3β in cells was determined by Western blot analysis with anti-phospho-Ser-473 Akt, Akt phospho-Ser-9 GSK3β, and GSK3β antibodies. Quantification of phospho-Ser-473 Akt and phospho-Ser-9 GSK3β obtained with control ( open bars ), WT strain ( black bars ), and Δ VacA strain ( gray bars ) was determined by densitometry. Data are means ± S.E. of values from triplicate experiments, with an n = 3 per experiment. Statistical significance: * , p

    Article Snippet: After incubation, cell lysates were subjected to SDS-PAGE in 10% gels, and then transferred to PVDF membranes for Western blotting using anti-phospho-Thr-308 Akt, phospho-Ser-473 Akt, phospho-Ser-9 GSK3β, Akt, or GSK3β antibodies (products of Cell Signaling).

    Techniques: Infection, Knock-Out, Mutagenesis, Incubation, Negative Control, Western Blot

    FoxO3a expression decreases on collagen. A , serum-starved human lung fibroblasts were attached to collagen (100 μg/ml, upper panel )-coated plates as a function of time. Akt and Ser-473-phosphorylated Akt levels were then measured. B , human lung fibroblasts were serum-starved for 2 days followed by attachment to collagen-coated plates as a function of time. FoxO3a, FoxO1, and FoxO4 expression levels were measured ( upper and lower panels , respectively). Glyceraldehyde-3-phosphate dehydrogenase ( GAPDH ) and actin were used as a loading control. C , serum-starved human lung fibroblasts were attached to fibronectin- (10 μg/ml), vitronectin- (10 μg/ml), and laminin (10 μg/ml)-coated plates as a function of time. FoxO3a expression levels were measured. Actin was used as a loading control.

    Journal: The Journal of Biological Chemistry

    Article Title: ?1-Integrin-Collagen Interaction Suppresses FoxO3a by the Coordination of Akt and PP2A *

    doi: 10.1074/jbc.M109.052845

    Figure Lengend Snippet: FoxO3a expression decreases on collagen. A , serum-starved human lung fibroblasts were attached to collagen (100 μg/ml, upper panel )-coated plates as a function of time. Akt and Ser-473-phosphorylated Akt levels were then measured. B , human lung fibroblasts were serum-starved for 2 days followed by attachment to collagen-coated plates as a function of time. FoxO3a, FoxO1, and FoxO4 expression levels were measured ( upper and lower panels , respectively). Glyceraldehyde-3-phosphate dehydrogenase ( GAPDH ) and actin were used as a loading control. C , serum-starved human lung fibroblasts were attached to fibronectin- (10 μg/ml), vitronectin- (10 μg/ml), and laminin (10 μg/ml)-coated plates as a function of time. FoxO3a expression levels were measured. Actin was used as a loading control.

    Article Snippet: Anti-Akt and anti-phospho-Akt (Ser-473) antibodies were obtained form Cell Signaling Technologies.

    Techniques: Expressing

    PTEN inhibition increases fibroblast proliferation via high Akt activity. A , upper panel , RT-PCR. Serum-starved fibroblasts were plated on collagen-coated dishes for the indicated times. The cells were lysed and total RNA was isolated by TRIzol. RT-PCR was performed as described under “Materials and Methods.” Lower panel , pulse-chase analysis. Fibroblasts were incubated in methionine-free medium followed by DMEM containing [ 35 S]methionine as outlined under “Materials and Methods.” The cells were then plated on collagen-coated dishes in DMEM + 10% fetal calf serum for the indicated times. The cells were lysed, PTEN was immunoprecipitated from labeled cell extracts and resolved by SDS-PAGE. Radiolabeled PTEN was visualized by autoradiography. B , human lung fibroblasts were infected with adenovirus expressing wild type PTEN or mutant PTEN followed by serum starvation for 1 day. Cells were then attached to collagen-coated plates (100 μg/ml) for 48 h. Total Akt, phosphorylated Akt, and FoxO3a expression levels were then measured. Wt , wild type PTEN; Mu , phosphatase-dead mutant PTEN; Vec , empty vector. C , PTEN −/− and PTEN +/+ cells were serum-starved for 24 h followed by attachment to collagen-coated plates as a function of time. FoxO3a, Ser-253-phosphorylated FoxO3a, and Ser-473-phosphorylated Akt levels were measured. Glyceraldehyde-3-phosphate dehydrogenase ( GAPDH ) was used as a loading control. D , PTEN −/− fibroblasts infected with adenovirus expressing wild type PTEN ( Wt ), phosphatase-dead mutant PTEN ( Mu ), or empty vector ( Vec ) were attached to collagen-coated plates for 60 min. FoxO3a and Ser-253-phosphorylated FoxO3a expression levels were then measured. GAPDH was used as a loading control. E , 3,000 PTEN −/− and PTEN +/+ cells were incubated in DMEM and cell numbers were counted at 72 h as described under “Materials and Methods.” The results are representative of three different experiments. F , serum-starved lung fibroblasts infected with adenovirus expressing hyperactive Akt ( Akt H ) or dominant Akt ( Akt DN , T308A, S473A) were seeded on collagen-coated plates for 30 min. FoxO3a, Ser-253 phosphorylated FoxO3a ( p-FoxO3a ), and Ser-473 phosphorylated Akt ( p-Akt ) levels were measured. GAPDH was used as a loading control.

    Journal: The Journal of Biological Chemistry

    Article Title: ?1-Integrin-Collagen Interaction Suppresses FoxO3a by the Coordination of Akt and PP2A *

    doi: 10.1074/jbc.M109.052845

    Figure Lengend Snippet: PTEN inhibition increases fibroblast proliferation via high Akt activity. A , upper panel , RT-PCR. Serum-starved fibroblasts were plated on collagen-coated dishes for the indicated times. The cells were lysed and total RNA was isolated by TRIzol. RT-PCR was performed as described under “Materials and Methods.” Lower panel , pulse-chase analysis. Fibroblasts were incubated in methionine-free medium followed by DMEM containing [ 35 S]methionine as outlined under “Materials and Methods.” The cells were then plated on collagen-coated dishes in DMEM + 10% fetal calf serum for the indicated times. The cells were lysed, PTEN was immunoprecipitated from labeled cell extracts and resolved by SDS-PAGE. Radiolabeled PTEN was visualized by autoradiography. B , human lung fibroblasts were infected with adenovirus expressing wild type PTEN or mutant PTEN followed by serum starvation for 1 day. Cells were then attached to collagen-coated plates (100 μg/ml) for 48 h. Total Akt, phosphorylated Akt, and FoxO3a expression levels were then measured. Wt , wild type PTEN; Mu , phosphatase-dead mutant PTEN; Vec , empty vector. C , PTEN −/− and PTEN +/+ cells were serum-starved for 24 h followed by attachment to collagen-coated plates as a function of time. FoxO3a, Ser-253-phosphorylated FoxO3a, and Ser-473-phosphorylated Akt levels were measured. Glyceraldehyde-3-phosphate dehydrogenase ( GAPDH ) was used as a loading control. D , PTEN −/− fibroblasts infected with adenovirus expressing wild type PTEN ( Wt ), phosphatase-dead mutant PTEN ( Mu ), or empty vector ( Vec ) were attached to collagen-coated plates for 60 min. FoxO3a and Ser-253-phosphorylated FoxO3a expression levels were then measured. GAPDH was used as a loading control. E , 3,000 PTEN −/− and PTEN +/+ cells were incubated in DMEM and cell numbers were counted at 72 h as described under “Materials and Methods.” The results are representative of three different experiments. F , serum-starved lung fibroblasts infected with adenovirus expressing hyperactive Akt ( Akt H ) or dominant Akt ( Akt DN , T308A, S473A) were seeded on collagen-coated plates for 30 min. FoxO3a, Ser-253 phosphorylated FoxO3a ( p-FoxO3a ), and Ser-473 phosphorylated Akt ( p-Akt ) levels were measured. GAPDH was used as a loading control.

    Article Snippet: Anti-Akt and anti-phospho-Akt (Ser-473) antibodies were obtained form Cell Signaling Technologies.

    Techniques: Inhibition, Activity Assay, Reverse Transcription Polymerase Chain Reaction, Isolation, Pulse Chase, Incubation, Immunoprecipitation, Labeling, SDS Page, Autoradiography, Infection, Expressing, Mutagenesis, Plasmid Preparation

    Increased expression of downstream signaling targets of IGF-1 in Lama2 Dy-w +IGF-1tg muscle lysates. ( A ) Western blots of total Akt, phospho-Akt (Thr-308), phospho-Akt (Ser-473) and α-tubulin in muscles isolated from 6-week-old WT, Lama2 Dy-w and Lama2 Dy-w +IGF-1tg mice. ( B ) Relative optical density analysis of phospho-Thr-308-Akt levels in Lama2 Dy-w +IGF-1tg muscles (black bars) revealed a several-fold increase relative to Lama2 Dy-w (white bars) and WT (gray bars), whereas total Akt and phospho-Ser-473-Akt levels increased only marginally. ( C ) Western blots of phospho-ERK1/2, total ERK1/2 and α-tubulin in 6-week-old muscles isolated from Lama2 Dy-w and Lama2 Dy-w +IGF-1tg mice. ( D ) Relative optical density of total ERK1/2 was similar in Lama2 Dy-w and Lama2 Dy-w +IGF-1tg muscle lysates. However, an increase in relative phospho-ERK1/2 levels was seen in muscles of Lama2 Dy-w +IGF-1tg (black bars) compared with its non-transgenic littermates (white bars).

    Journal: Human Molecular Genetics

    Article Title: Muscle-specific expression of insulin-like growth factor 1 improves outcome in Lama2Dy-w mice, a model for congenital muscular dystrophy type 1A

    doi: 10.1093/hmg/ddr126

    Figure Lengend Snippet: Increased expression of downstream signaling targets of IGF-1 in Lama2 Dy-w +IGF-1tg muscle lysates. ( A ) Western blots of total Akt, phospho-Akt (Thr-308), phospho-Akt (Ser-473) and α-tubulin in muscles isolated from 6-week-old WT, Lama2 Dy-w and Lama2 Dy-w +IGF-1tg mice. ( B ) Relative optical density analysis of phospho-Thr-308-Akt levels in Lama2 Dy-w +IGF-1tg muscles (black bars) revealed a several-fold increase relative to Lama2 Dy-w (white bars) and WT (gray bars), whereas total Akt and phospho-Ser-473-Akt levels increased only marginally. ( C ) Western blots of phospho-ERK1/2, total ERK1/2 and α-tubulin in 6-week-old muscles isolated from Lama2 Dy-w and Lama2 Dy-w +IGF-1tg mice. ( D ) Relative optical density of total ERK1/2 was similar in Lama2 Dy-w and Lama2 Dy-w +IGF-1tg muscle lysates. However, an increase in relative phospho-ERK1/2 levels was seen in muscles of Lama2 Dy-w +IGF-1tg (black bars) compared with its non-transgenic littermates (white bars).

    Article Snippet: Blots were blocked with Odyssey blocking buffer diluted with TBS-Tween (TBST; 50 m m Tris–HCl, 150 m m NaCl, pH 7.6, and 0.1% Tween 20) and incubated overnight at 4°C with the following primary antibodies: anti-phospho-Akt-Thr-308 (1:800), anti-phospho-Akt-Ser-473 (1:800), total Akt (1:1000), phospho-ERK1/2 (1:800), total ERK1/(1:1000) (Cell Signaling Technology, Danvers, MA, USA) and anti-α-tubulin (1:5000) (Sigma-Aldrich).

    Techniques: Expressing, Western Blot, Isolation, Mouse Assay, Transgenic Assay

    Pim-2 maintains the survival and size of growth factor-deprived cells. ( A ) Western blots of Pim-2, Bcl-x L , phospho-Ser 473-Akt (mAkt) and ACTIN are shown using lysates from FL5.12 lines stably expressing Pim-2, mAkt, and Bcl-x L transgenes. Empty vector was used a negative control. ( B ) Percent viability was assessed daily for 18 d following IL-3 deprivation. (▪) Pim-2;(○) mAkt;(▵) Bcl-x L ; (⋄) vector control. The data are presented as the mean ± S.D. of triplicate samples and are representative of five independent experiments. ( C ) The mean forward scatter (as an indicator of cell size) of the cells in B are plotted versus days post-IL-3 withdrawal. (▪) Pim-2;(○) mAkt; (▵) Bcl-x L ; (⋄) vector control. Data are presented as the mean ± S.D. of triplicate samples and are representative of five independent experiments.

    Journal: Genes & Development

    Article Title: The serine/threonine kinase Pim-2 is a transcriptionally regulated apoptotic inhibitor

    doi: 10.1101/gad.1105003

    Figure Lengend Snippet: Pim-2 maintains the survival and size of growth factor-deprived cells. ( A ) Western blots of Pim-2, Bcl-x L , phospho-Ser 473-Akt (mAkt) and ACTIN are shown using lysates from FL5.12 lines stably expressing Pim-2, mAkt, and Bcl-x L transgenes. Empty vector was used a negative control. ( B ) Percent viability was assessed daily for 18 d following IL-3 deprivation. (▪) Pim-2;(○) mAkt;(▵) Bcl-x L ; (⋄) vector control. The data are presented as the mean ± S.D. of triplicate samples and are representative of five independent experiments. ( C ) The mean forward scatter (as an indicator of cell size) of the cells in B are plotted versus days post-IL-3 withdrawal. (▪) Pim-2;(○) mAkt; (▵) Bcl-x L ; (⋄) vector control. Data are presented as the mean ± S.D. of triplicate samples and are representative of five independent experiments.

    Article Snippet: Rabbit anti-total Akt, anti-phospho-Ser 473-AKT, anti-total 4E-BP1, anti-phospho-Ser 65-4E-BP1, anti-phospho-Thr 70-4E-BP1, anti-phospho-Thr 37/Thr 46-4E-BP1, and anti-phospho-GSK3β were purchased from Cell Signaling.

    Techniques: Western Blot, Stable Transfection, Expressing, Plasmid Preparation, Negative Control