total akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total akt
    A , putative miR-221-binding sites (red) in the 3′-UTRs of PTEN ( top ). The middle panel shows sequence alignment of the miR-221 sequences (red color) with a region of the PTEN 3′-UTR (red) from indicated species. The bottom shows a mutant of PTEN 3′-UTR for pMIR-REPORT. B , SOSP-9607 cells were transfected with miR-221 mimic, miR-221 inhibitor, scramble oligonucleotide or nothing (blank). And then indicated protein and mRNA were detected. Rows 1 to 7, the expression of PTEN, <t>phospho-Akt</t> (p-Akt), total-Akt <t>(t-Akt),</t> Cyclin D1 (CCND1), p27 and p57 were analyzed by Western blot; row 8, β-actin was used as a loading control; row 9, PTEN mRNA level was measured by RT-PCR; row 10, GAPDH was used as an control. C , SOSP-9607 cells were co-transfected with miR-221 mimic or scramble oligonucleotide, and pMIR-REPORT vector consisting of a luciferase gene containing the wild type (PTEN-3′-UTR) or mutated (PTEN-mut-3′-UTR) miR-221 binding sites in its 3′-UTR region by using Lipofectamine 2000 reagent. The cells were also transfected with 50 ng pRL-TK vector as an internal standard. 24 h after transfection, luciferase activity was measured by using a dual luciferase reporter assay (Promega). D , similar experiments were performed in MG63 cells as described in panel C except that miR-221 mimic was instead by miR-221 inhibitor. The results were presented as relative luciferase activity (firefly Luc/Renilla Luc). All experiments were repeated three times in triplicate. Columns, mean of three independent experiments; bars, SD. **, p<0.01.
    Total Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/total akt/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    total akt - by Bioz Stars, 2023-01
    95/100 stars

    Images

    1) Product Images from "MicroRNA-221 Induces Cell Survival and Cisplatin Resistance through PI3K/Akt Pathway in Human Osteosarcoma"

    Article Title: MicroRNA-221 Induces Cell Survival and Cisplatin Resistance through PI3K/Akt Pathway in Human Osteosarcoma

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0053906

    A , putative miR-221-binding sites (red) in the 3′-UTRs of PTEN ( top ). The middle panel shows sequence alignment of the miR-221 sequences (red color) with a region of the PTEN 3′-UTR (red) from indicated species. The bottom shows a mutant of PTEN 3′-UTR for pMIR-REPORT. B , SOSP-9607 cells were transfected with miR-221 mimic, miR-221 inhibitor, scramble oligonucleotide or nothing (blank). And then indicated protein and mRNA were detected. Rows 1 to 7, the expression of PTEN, phospho-Akt (p-Akt), total-Akt (t-Akt), Cyclin D1 (CCND1), p27 and p57 were analyzed by Western blot; row 8, β-actin was used as a loading control; row 9, PTEN mRNA level was measured by RT-PCR; row 10, GAPDH was used as an control. C , SOSP-9607 cells were co-transfected with miR-221 mimic or scramble oligonucleotide, and pMIR-REPORT vector consisting of a luciferase gene containing the wild type (PTEN-3′-UTR) or mutated (PTEN-mut-3′-UTR) miR-221 binding sites in its 3′-UTR region by using Lipofectamine 2000 reagent. The cells were also transfected with 50 ng pRL-TK vector as an internal standard. 24 h after transfection, luciferase activity was measured by using a dual luciferase reporter assay (Promega). D , similar experiments were performed in MG63 cells as described in panel C except that miR-221 mimic was instead by miR-221 inhibitor. The results were presented as relative luciferase activity (firefly Luc/Renilla Luc). All experiments were repeated three times in triplicate. Columns, mean of three independent experiments; bars, SD. **, p<0.01.
    Figure Legend Snippet: A , putative miR-221-binding sites (red) in the 3′-UTRs of PTEN ( top ). The middle panel shows sequence alignment of the miR-221 sequences (red color) with a region of the PTEN 3′-UTR (red) from indicated species. The bottom shows a mutant of PTEN 3′-UTR for pMIR-REPORT. B , SOSP-9607 cells were transfected with miR-221 mimic, miR-221 inhibitor, scramble oligonucleotide or nothing (blank). And then indicated protein and mRNA were detected. Rows 1 to 7, the expression of PTEN, phospho-Akt (p-Akt), total-Akt (t-Akt), Cyclin D1 (CCND1), p27 and p57 were analyzed by Western blot; row 8, β-actin was used as a loading control; row 9, PTEN mRNA level was measured by RT-PCR; row 10, GAPDH was used as an control. C , SOSP-9607 cells were co-transfected with miR-221 mimic or scramble oligonucleotide, and pMIR-REPORT vector consisting of a luciferase gene containing the wild type (PTEN-3′-UTR) or mutated (PTEN-mut-3′-UTR) miR-221 binding sites in its 3′-UTR region by using Lipofectamine 2000 reagent. The cells were also transfected with 50 ng pRL-TK vector as an internal standard. 24 h after transfection, luciferase activity was measured by using a dual luciferase reporter assay (Promega). D , similar experiments were performed in MG63 cells as described in panel C except that miR-221 mimic was instead by miR-221 inhibitor. The results were presented as relative luciferase activity (firefly Luc/Renilla Luc). All experiments were repeated three times in triplicate. Columns, mean of three independent experiments; bars, SD. **, p<0.01.

    Techniques Used: Binding Assay, Sequencing, Mutagenesis, Transfection, Expressing, Western Blot, Reverse Transcription Polymerase Chain Reaction, Plasmid Preparation, Luciferase, Activity Assay, Reporter Assay

    A , SOSP-9607 cells were transfected with miR-221 mimic (221 Mi), scramble oligonucleotide (Scr) or cotransfected with miR-221 mimic and pcDNA-PTEN. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. B , SOSP-9607 cells were transfected with miR-221 mimic, scramble oligonucleotide or cotransfected with miR-221 mimic and LY294002. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. C , SOSP-9607 and MG 63 cells were treated as described in panel A. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. D , SOSP-9607 and MG 63 cells were all treated as described in panel B. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. E , both SOSP-9607 and MG 63 cells treated as described in panel A were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit (Promega) according to the manufacturer's instructions. F , both SOSP-9607 and MG 63 cells treated as described in panel B were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit. Columns, mean of three independent experiments; bars, SD; **, p<0.01, ***, p<0.001.
    Figure Legend Snippet: A , SOSP-9607 cells were transfected with miR-221 mimic (221 Mi), scramble oligonucleotide (Scr) or cotransfected with miR-221 mimic and pcDNA-PTEN. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. B , SOSP-9607 cells were transfected with miR-221 mimic, scramble oligonucleotide or cotransfected with miR-221 mimic and LY294002. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. C , SOSP-9607 and MG 63 cells were treated as described in panel A. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. D , SOSP-9607 and MG 63 cells were all treated as described in panel B. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. E , both SOSP-9607 and MG 63 cells treated as described in panel A were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit (Promega) according to the manufacturer's instructions. F , both SOSP-9607 and MG 63 cells treated as described in panel B were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit. Columns, mean of three independent experiments; bars, SD; **, p<0.01, ***, p<0.001.

    Techniques Used: Transfection, Expressing, Western Blot, Inhibition, Activity Assay, Caspase-Glo Assay

    total akt  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
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    Cell Signaling Technology Inc total akt
    A , putative miR-221-binding sites (red) in the 3′-UTRs of PTEN ( top ). The middle panel shows sequence alignment of the miR-221 sequences (red color) with a region of the PTEN 3′-UTR (red) from indicated species. The bottom shows a mutant of PTEN 3′-UTR for pMIR-REPORT. B , SOSP-9607 cells were transfected with miR-221 mimic, miR-221 inhibitor, scramble oligonucleotide or nothing (blank). And then indicated protein and mRNA were detected. Rows 1 to 7, the expression of PTEN, <t>phospho-Akt</t> (p-Akt), total-Akt <t>(t-Akt),</t> Cyclin D1 (CCND1), p27 and p57 were analyzed by Western blot; row 8, β-actin was used as a loading control; row 9, PTEN mRNA level was measured by RT-PCR; row 10, GAPDH was used as an control. C , SOSP-9607 cells were co-transfected with miR-221 mimic or scramble oligonucleotide, and pMIR-REPORT vector consisting of a luciferase gene containing the wild type (PTEN-3′-UTR) or mutated (PTEN-mut-3′-UTR) miR-221 binding sites in its 3′-UTR region by using Lipofectamine 2000 reagent. The cells were also transfected with 50 ng pRL-TK vector as an internal standard. 24 h after transfection, luciferase activity was measured by using a dual luciferase reporter assay (Promega). D , similar experiments were performed in MG63 cells as described in panel C except that miR-221 mimic was instead by miR-221 inhibitor. The results were presented as relative luciferase activity (firefly Luc/Renilla Luc). All experiments were repeated three times in triplicate. Columns, mean of three independent experiments; bars, SD. **, p<0.01.
    Total Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/total akt/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    total akt - by Bioz Stars, 2023-01
    95/100 stars

    Images

    1) Product Images from "MicroRNA-221 Induces Cell Survival and Cisplatin Resistance through PI3K/Akt Pathway in Human Osteosarcoma"

    Article Title: MicroRNA-221 Induces Cell Survival and Cisplatin Resistance through PI3K/Akt Pathway in Human Osteosarcoma

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0053906

    A , putative miR-221-binding sites (red) in the 3′-UTRs of PTEN ( top ). The middle panel shows sequence alignment of the miR-221 sequences (red color) with a region of the PTEN 3′-UTR (red) from indicated species. The bottom shows a mutant of PTEN 3′-UTR for pMIR-REPORT. B , SOSP-9607 cells were transfected with miR-221 mimic, miR-221 inhibitor, scramble oligonucleotide or nothing (blank). And then indicated protein and mRNA were detected. Rows 1 to 7, the expression of PTEN, phospho-Akt (p-Akt), total-Akt (t-Akt), Cyclin D1 (CCND1), p27 and p57 were analyzed by Western blot; row 8, β-actin was used as a loading control; row 9, PTEN mRNA level was measured by RT-PCR; row 10, GAPDH was used as an control. C , SOSP-9607 cells were co-transfected with miR-221 mimic or scramble oligonucleotide, and pMIR-REPORT vector consisting of a luciferase gene containing the wild type (PTEN-3′-UTR) or mutated (PTEN-mut-3′-UTR) miR-221 binding sites in its 3′-UTR region by using Lipofectamine 2000 reagent. The cells were also transfected with 50 ng pRL-TK vector as an internal standard. 24 h after transfection, luciferase activity was measured by using a dual luciferase reporter assay (Promega). D , similar experiments were performed in MG63 cells as described in panel C except that miR-221 mimic was instead by miR-221 inhibitor. The results were presented as relative luciferase activity (firefly Luc/Renilla Luc). All experiments were repeated three times in triplicate. Columns, mean of three independent experiments; bars, SD. **, p<0.01.
    Figure Legend Snippet: A , putative miR-221-binding sites (red) in the 3′-UTRs of PTEN ( top ). The middle panel shows sequence alignment of the miR-221 sequences (red color) with a region of the PTEN 3′-UTR (red) from indicated species. The bottom shows a mutant of PTEN 3′-UTR for pMIR-REPORT. B , SOSP-9607 cells were transfected with miR-221 mimic, miR-221 inhibitor, scramble oligonucleotide or nothing (blank). And then indicated protein and mRNA were detected. Rows 1 to 7, the expression of PTEN, phospho-Akt (p-Akt), total-Akt (t-Akt), Cyclin D1 (CCND1), p27 and p57 were analyzed by Western blot; row 8, β-actin was used as a loading control; row 9, PTEN mRNA level was measured by RT-PCR; row 10, GAPDH was used as an control. C , SOSP-9607 cells were co-transfected with miR-221 mimic or scramble oligonucleotide, and pMIR-REPORT vector consisting of a luciferase gene containing the wild type (PTEN-3′-UTR) or mutated (PTEN-mut-3′-UTR) miR-221 binding sites in its 3′-UTR region by using Lipofectamine 2000 reagent. The cells were also transfected with 50 ng pRL-TK vector as an internal standard. 24 h after transfection, luciferase activity was measured by using a dual luciferase reporter assay (Promega). D , similar experiments were performed in MG63 cells as described in panel C except that miR-221 mimic was instead by miR-221 inhibitor. The results were presented as relative luciferase activity (firefly Luc/Renilla Luc). All experiments were repeated three times in triplicate. Columns, mean of three independent experiments; bars, SD. **, p<0.01.

    Techniques Used: Binding Assay, Sequencing, Mutagenesis, Transfection, Expressing, Western Blot, Reverse Transcription Polymerase Chain Reaction, Plasmid Preparation, Luciferase, Activity Assay, Reporter Assay

    A , SOSP-9607 cells were transfected with miR-221 mimic (221 Mi), scramble oligonucleotide (Scr) or cotransfected with miR-221 mimic and pcDNA-PTEN. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. B , SOSP-9607 cells were transfected with miR-221 mimic, scramble oligonucleotide or cotransfected with miR-221 mimic and LY294002. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. C , SOSP-9607 and MG 63 cells were treated as described in panel A. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. D , SOSP-9607 and MG 63 cells were all treated as described in panel B. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. E , both SOSP-9607 and MG 63 cells treated as described in panel A were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit (Promega) according to the manufacturer's instructions. F , both SOSP-9607 and MG 63 cells treated as described in panel B were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit. Columns, mean of three independent experiments; bars, SD; **, p<0.01, ***, p<0.001.
    Figure Legend Snippet: A , SOSP-9607 cells were transfected with miR-221 mimic (221 Mi), scramble oligonucleotide (Scr) or cotransfected with miR-221 mimic and pcDNA-PTEN. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. B , SOSP-9607 cells were transfected with miR-221 mimic, scramble oligonucleotide or cotransfected with miR-221 mimic and LY294002. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. C , SOSP-9607 and MG 63 cells were treated as described in panel A. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. D , SOSP-9607 and MG 63 cells were all treated as described in panel B. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. E , both SOSP-9607 and MG 63 cells treated as described in panel A were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit (Promega) according to the manufacturer's instructions. F , both SOSP-9607 and MG 63 cells treated as described in panel B were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit. Columns, mean of three independent experiments; bars, SD; **, p<0.01, ***, p<0.001.

    Techniques Used: Transfection, Expressing, Western Blot, Inhibition, Activity Assay, Caspase-Glo Assay

    total akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total akt
    Total Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/total akt/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
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    total akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total akt
    Adding FN or LAM increases the activation of <t>Akt</t> <t>and</t> <t>ERK</t> . (A) MSCs were induced for differentiation without (Control) or with FN or LAM, and western blotting was done for stage III cells. Quantification of western blotting shows FN or LAM increases the activation of (B) Akt and (C) Akt. (mean ± S.D.).
    Total Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 95 stars, based on 1 article reviews
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    1) Product Images from "Fibronectin and laminin promote differentiation of human mesenchymal stem cells into insulin producing cells through activating Akt and ERK"

    Article Title: Fibronectin and laminin promote differentiation of human mesenchymal stem cells into insulin producing cells through activating Akt and ERK

    Journal: Journal of Biomedical Science

    doi: 10.1186/1423-0127-17-56

    Adding FN or LAM increases the activation of Akt and ERK . (A) MSCs were induced for differentiation without (Control) or with FN or LAM, and western blotting was done for stage III cells. Quantification of western blotting shows FN or LAM increases the activation of (B) Akt and (C) Akt. (mean ± S.D.).
    Figure Legend Snippet: Adding FN or LAM increases the activation of Akt and ERK . (A) MSCs were induced for differentiation without (Control) or with FN or LAM, and western blotting was done for stage III cells. Quantification of western blotting shows FN or LAM increases the activation of (B) Akt and (C) Akt. (mean ± S.D.).

    Techniques Used: Activation Assay, Western Blot

    Cross-talk between PI3K-Akt and MEK-ERK pathways during differentiation of MSCs into IPCs . (A) MSCs were treated without (DMSO) or with 50 μM of PD98059 or LY294002 and MTT assay were performed at 48 hours. (B) MSCs were pretreated without (DMSO) or with PD98059 or LY294002 at stage III during differentiation with FN or LAM, and western blotting was done for stage IV cells. Quantification of Akt (C) and ERK (D) phosphorylation shows PD98059 and LY294002 increase the activation of Akt and ERK, respectively. Quantitative RT-PCR for (E) insulin and (F) Glut2 expression shows both PD98059 and LY294002 increase the expression of insulin and Glut2. (mean ± S.D.; **indicates significant difference ( P < 0.01) compared with control by student's t test.).
    Figure Legend Snippet: Cross-talk between PI3K-Akt and MEK-ERK pathways during differentiation of MSCs into IPCs . (A) MSCs were treated without (DMSO) or with 50 μM of PD98059 or LY294002 and MTT assay were performed at 48 hours. (B) MSCs were pretreated without (DMSO) or with PD98059 or LY294002 at stage III during differentiation with FN or LAM, and western blotting was done for stage IV cells. Quantification of Akt (C) and ERK (D) phosphorylation shows PD98059 and LY294002 increase the activation of Akt and ERK, respectively. Quantitative RT-PCR for (E) insulin and (F) Glut2 expression shows both PD98059 and LY294002 increase the expression of insulin and Glut2. (mean ± S.D.; **indicates significant difference ( P < 0.01) compared with control by student's t test.).

    Techniques Used: MTT Assay, Western Blot, Activation Assay, Quantitative RT-PCR, Expressing

    FN or LAM enhances IPC differentiation by activating Akt and ERK . (A) MSCs were pretreated without (DMSO) or with both PD98059 and LY294002 (PD+LY) at stage III during differentiation with FN or LAM, and western blotting was done for stage IV cells. Quantification of Akt (B) and ERK (C) phosphorylation shows adding both PD98059 and LY294002 decreases the activation of Akt and ERK. (D) Quantitative RT-PCR for insulin and Glut2 expression shows adding both PD98059 and LY294002 decreases the expression of insulin and Glut2. (mean ± S.D.).
    Figure Legend Snippet: FN or LAM enhances IPC differentiation by activating Akt and ERK . (A) MSCs were pretreated without (DMSO) or with both PD98059 and LY294002 (PD+LY) at stage III during differentiation with FN or LAM, and western blotting was done for stage IV cells. Quantification of Akt (B) and ERK (C) phosphorylation shows adding both PD98059 and LY294002 decreases the activation of Akt and ERK. (D) Quantitative RT-PCR for insulin and Glut2 expression shows adding both PD98059 and LY294002 decreases the expression of insulin and Glut2. (mean ± S.D.).

    Techniques Used: Western Blot, Activation Assay, Quantitative RT-PCR, Expressing

    The involvement of Akt and ERK activation in FN or LAM-induced enhancement of IPC differentiation . (A) MSCs were transduced with scrambled (-) or siRNA against ERK (siERK) and Akt (siAkt) and induced for IPC differentiation with FN or LAM, and western blotting was done for stage IV cells. Quantification of Akt (B) and ERK (C) phosphorylation after transduction with siERK and siAkt. Quantitative RT-PCR for (D) insulin and (E) Glut2 expression shows transduction with either siERK or siAkt increases the expression of insulin and Glut2, and transduction with both siERK and siAkt decreases the expression of insulin and Glut2. (mean ± S.D.; *p < 0.05 and **p < 0.01 compared with the scrambled as determined by the student's t test.).
    Figure Legend Snippet: The involvement of Akt and ERK activation in FN or LAM-induced enhancement of IPC differentiation . (A) MSCs were transduced with scrambled (-) or siRNA against ERK (siERK) and Akt (siAkt) and induced for IPC differentiation with FN or LAM, and western blotting was done for stage IV cells. Quantification of Akt (B) and ERK (C) phosphorylation after transduction with siERK and siAkt. Quantitative RT-PCR for (D) insulin and (E) Glut2 expression shows transduction with either siERK or siAkt increases the expression of insulin and Glut2, and transduction with both siERK and siAkt decreases the expression of insulin and Glut2. (mean ± S.D.; *p < 0.05 and **p < 0.01 compared with the scrambled as determined by the student's t test.).

    Techniques Used: Activation Assay, Transduction, Western Blot, Quantitative RT-PCR, Expressing

    total akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total akt
    Western blots of pS6 ribosomal protein, total S6 ribsomal protein, p4E-BP1, total 4E-BP1, pAkt, <t>total</t> <t>Akt</t> and α-Tubulin (loading control) in PI-103-treated and its recovery in HT29 and HCT116 Bax-ko cells.
    Total Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/total akt/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    total akt - by Bioz Stars, 2023-01
    95/100 stars

    Images

    1) Product Images from "Reduced Warburg Effect in Cancer Cells Undergoing Autophagy: Steady- State 1 H-MRS and Real-Time Hyperpolarized 13 C-MRS Studies"

    Article Title: Reduced Warburg Effect in Cancer Cells Undergoing Autophagy: Steady- State 1 H-MRS and Real-Time Hyperpolarized 13 C-MRS Studies

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0092645

    Western blots of pS6 ribosomal protein, total S6 ribsomal protein, p4E-BP1, total 4E-BP1, pAkt, total Akt and α-Tubulin (loading control) in PI-103-treated and its recovery in HT29 and HCT116 Bax-ko cells.
    Figure Legend Snippet: Western blots of pS6 ribosomal protein, total S6 ribsomal protein, p4E-BP1, total 4E-BP1, pAkt, total Akt and α-Tubulin (loading control) in PI-103-treated and its recovery in HT29 and HCT116 Bax-ko cells.

    Techniques Used: Western Blot

    phosphor akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt
    (A) <t>Vehicle-Hone1,</t> <t>fibulin-5-Hone1,</t> vehicle-TW01, and fibulin-5-TW01 transfected cells were serum-starved and treated with the indicated inhibitors, SB202190, PD98059, and LY294002 or solvent for 24 hour. The migration and invasion ratios of vehicle-Hone1 and fibulin-5-Hone1 transfected cells were determined as previously described. (B) The fibulin-5 expressing cells of Hone1 and TW01 were serum-starved for 24 hour and treated with or without LY294002 at the final concentration of 10 μM. The Total cell lysates of vehicle-Hone1, fibulin-5-Hone1, vehicle-TW01, and fibulin-5-TW01 transfected cells were immunoblotted for the unphosphorylated and phosphorylated forms of <t>AKT.</t> β-actin was used as the internal loading control. (C) A negative control and fibulin-5 siRNAs were transfected into Hone1 cells for 24 hour and western blotting was performed as in (B).
    Phosphor Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 95 stars, based on 1 article reviews
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    1) Product Images from "Oncogenic Fibulin-5 Promotes Nasopharyngeal Carcinoma Cell Metastasis through the FLJ10540/AKT Pathway and Correlates with Poor Prognosis"

    Article Title: Oncogenic Fibulin-5 Promotes Nasopharyngeal Carcinoma Cell Metastasis through the FLJ10540/AKT Pathway and Correlates with Poor Prognosis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0084218

    (A) Vehicle-Hone1, fibulin-5-Hone1, vehicle-TW01, and fibulin-5-TW01 transfected cells were serum-starved and treated with the indicated inhibitors, SB202190, PD98059, and LY294002 or solvent for 24 hour. The migration and invasion ratios of vehicle-Hone1 and fibulin-5-Hone1 transfected cells were determined as previously described. (B) The fibulin-5 expressing cells of Hone1 and TW01 were serum-starved for 24 hour and treated with or without LY294002 at the final concentration of 10 μM. The Total cell lysates of vehicle-Hone1, fibulin-5-Hone1, vehicle-TW01, and fibulin-5-TW01 transfected cells were immunoblotted for the unphosphorylated and phosphorylated forms of AKT. β-actin was used as the internal loading control. (C) A negative control and fibulin-5 siRNAs were transfected into Hone1 cells for 24 hour and western blotting was performed as in (B).
    Figure Legend Snippet: (A) Vehicle-Hone1, fibulin-5-Hone1, vehicle-TW01, and fibulin-5-TW01 transfected cells were serum-starved and treated with the indicated inhibitors, SB202190, PD98059, and LY294002 or solvent for 24 hour. The migration and invasion ratios of vehicle-Hone1 and fibulin-5-Hone1 transfected cells were determined as previously described. (B) The fibulin-5 expressing cells of Hone1 and TW01 were serum-starved for 24 hour and treated with or without LY294002 at the final concentration of 10 μM. The Total cell lysates of vehicle-Hone1, fibulin-5-Hone1, vehicle-TW01, and fibulin-5-TW01 transfected cells were immunoblotted for the unphosphorylated and phosphorylated forms of AKT. β-actin was used as the internal loading control. (C) A negative control and fibulin-5 siRNAs were transfected into Hone1 cells for 24 hour and western blotting was performed as in (B).

    Techniques Used: Transfection, Migration, Expressing, Concentration Assay, Negative Control, Western Blot

    (A) Hone1-expressing FLJ10540 cells were serum-starved for 24 hour and treated with or without AKT inhibitor. The Total cell lysates of vehicle-Hone and FLJ10540-Hone1, transfected cells were immunoblotted for the unphosphorylated and phosphorylated forms of AKT. β-actin was used as the internal loading control. (B) A negative control and FLJ10540 siRNAs were transfected into Hone1 cells for 24 hour and western blotting was performed as in (B). (C) Vehicle-Hone1 and FLJ10540-Hone1 transfected cells were serum-starved and treated with the AKT inhibitor for 24 hour. The migration and invasion ratios of vehicle-Hone1 and fibulin-5-Hone1 transfected cells were determined as previously described.
    Figure Legend Snippet: (A) Hone1-expressing FLJ10540 cells were serum-starved for 24 hour and treated with or without AKT inhibitor. The Total cell lysates of vehicle-Hone and FLJ10540-Hone1, transfected cells were immunoblotted for the unphosphorylated and phosphorylated forms of AKT. β-actin was used as the internal loading control. (B) A negative control and FLJ10540 siRNAs were transfected into Hone1 cells for 24 hour and western blotting was performed as in (B). (C) Vehicle-Hone1 and FLJ10540-Hone1 transfected cells were serum-starved and treated with the AKT inhibitor for 24 hour. The migration and invasion ratios of vehicle-Hone1 and fibulin-5-Hone1 transfected cells were determined as previously described.

    Techniques Used: Expressing, Transfection, Negative Control, Western Blot, Migration

    total akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total akt
    Representative immunoblots (A) and quantitative analysis (B) of rBCEC4 lysates incubated with vehicle (Ctr) or EPC-CM (CM) in presence of either LY294002 (CM+LY) or PD98509 (CM+PD). Exposure of rBCEC4 to EPC-CM resulted in a marked increase of both phosphorylated <t>AKT</t> and phosphorylated ERK (pAKT and pERK) with regards to the <t>total</t> <t>AKT</t> and ERK levels <t>(tAKT</t> and tERK). Concomitant incubation with EPC-CM and the corresponding inhibitors almost completely blocked the phosphorylation of AKT and ERK. Data are given as mean + s.e.m. and values are presented as percentage of corresponding controls. *: p < 0.05.
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    Images

    1) Product Images from "The Secretome of Endothelial Progenitor Cells Promotes Brain Endothelial Cell Activity through PI3-Kinase and MAP-Kinase"

    Article Title: The Secretome of Endothelial Progenitor Cells Promotes Brain Endothelial Cell Activity through PI3-Kinase and MAP-Kinase

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0095731

    Representative immunoblots (A) and quantitative analysis (B) of rBCEC4 lysates incubated with vehicle (Ctr) or EPC-CM (CM) in presence of either LY294002 (CM+LY) or PD98509 (CM+PD). Exposure of rBCEC4 to EPC-CM resulted in a marked increase of both phosphorylated AKT and phosphorylated ERK (pAKT and pERK) with regards to the total AKT and ERK levels (tAKT and tERK). Concomitant incubation with EPC-CM and the corresponding inhibitors almost completely blocked the phosphorylation of AKT and ERK. Data are given as mean + s.e.m. and values are presented as percentage of corresponding controls. *: p < 0.05.
    Figure Legend Snippet: Representative immunoblots (A) and quantitative analysis (B) of rBCEC4 lysates incubated with vehicle (Ctr) or EPC-CM (CM) in presence of either LY294002 (CM+LY) or PD98509 (CM+PD). Exposure of rBCEC4 to EPC-CM resulted in a marked increase of both phosphorylated AKT and phosphorylated ERK (pAKT and pERK) with regards to the total AKT and ERK levels (tAKT and tERK). Concomitant incubation with EPC-CM and the corresponding inhibitors almost completely blocked the phosphorylation of AKT and ERK. Data are given as mean + s.e.m. and values are presented as percentage of corresponding controls. *: p < 0.05.

    Techniques Used: Western Blot, Incubation

    rBCEC4 incubated with EPC-CM (CM) displayed higher viable cell numbers assessed with the Presto Blue assay as compared to control (Ctr). The EPC-CM induced higher viable cell number was inhibited by AKT (CM+LY) as well as ERK (CM+PD) phosphorylation inhibitors ([5 µM] and [10 µM], respectively). Data are given as mean + s.e.m. and values are presented as percentage of control. *: p < 0.05.
    Figure Legend Snippet: rBCEC4 incubated with EPC-CM (CM) displayed higher viable cell numbers assessed with the Presto Blue assay as compared to control (Ctr). The EPC-CM induced higher viable cell number was inhibited by AKT (CM+LY) as well as ERK (CM+PD) phosphorylation inhibitors ([5 µM] and [10 µM], respectively). Data are given as mean + s.e.m. and values are presented as percentage of control. *: p < 0.05.

    Techniques Used: Incubation

    Representative microphotographs (upper panels) and quantitative analysis (lower panel) of rBCEC4 wound healing capacity. rBCEC4 incubated with EPC-CM (CM) displayed higher migration rate in the wound healing-scratch test as compared to control (Ctr). Scale bar: 100 µm. EPC-CM induced migration was inhibited by AKT (CM+LY) as well as ERK (CM+PD) phosphorylation inhibitors ([5 µM] and [10 µM], respectively). Data are given as mean + s.e.m. and values are presented as percentage of control. *: p < 0.05.
    Figure Legend Snippet: Representative microphotographs (upper panels) and quantitative analysis (lower panel) of rBCEC4 wound healing capacity. rBCEC4 incubated with EPC-CM (CM) displayed higher migration rate in the wound healing-scratch test as compared to control (Ctr). Scale bar: 100 µm. EPC-CM induced migration was inhibited by AKT (CM+LY) as well as ERK (CM+PD) phosphorylation inhibitors ([5 µM] and [10 µM], respectively). Data are given as mean + s.e.m. and values are presented as percentage of control. *: p < 0.05.

    Techniques Used: Incubation, Migration

    Representative microphotographs of tubular network formation by microvascular endothelial cells on growth factor reduced Matrigel. EPC-CM incubation (CM) strikingly promoted the tube-like structure formation as compared to control medium (Ctr). Supplementation of EPC-CM with the inhibitor of AKT phosphorylation (CM+LY) ([5 µM]) substantially attenuated EPC-CM induced tube formation. Similarly, addition of the inhibitor of ERK phosphorylation (CM+PD) ([10 µM]) resulted in a decrease of tube formation, however, to a lesser degree as compared to the CM+LY group. Scale bar: 100 µm.
    Figure Legend Snippet: Representative microphotographs of tubular network formation by microvascular endothelial cells on growth factor reduced Matrigel. EPC-CM incubation (CM) strikingly promoted the tube-like structure formation as compared to control medium (Ctr). Supplementation of EPC-CM with the inhibitor of AKT phosphorylation (CM+LY) ([5 µM]) substantially attenuated EPC-CM induced tube formation. Similarly, addition of the inhibitor of ERK phosphorylation (CM+PD) ([10 µM]) resulted in a decrease of tube formation, however, to a lesser degree as compared to the CM+LY group. Scale bar: 100 µm.

    Techniques Used: Incubation

    Quantitative analysis of tubular network formation by microvascular endothelial cells on growth factor reduced Matrigel. EPC-CM incubation (CM) significantly promoted total area covered by the tube-like structures (A), total sprout length (B) and branching (C) as compared to control medium (Ctr). Supplementation of EPC-CM with the inhibitor of AKT phosphorylation (CM+LY) ([5 µM]) substantially attenuated all three parameters while the addition of the inhibitor of ERK phosphorylation (CM+PD) ([10 µM]) resulted in a significant decrease of covered area and total tube length but had no significant effect on the reduction of the number of branches. Data are given as mean + s.e.m. and values are presented as percentage of corresponding controls. *: p < 0.05.
    Figure Legend Snippet: Quantitative analysis of tubular network formation by microvascular endothelial cells on growth factor reduced Matrigel. EPC-CM incubation (CM) significantly promoted total area covered by the tube-like structures (A), total sprout length (B) and branching (C) as compared to control medium (Ctr). Supplementation of EPC-CM with the inhibitor of AKT phosphorylation (CM+LY) ([5 µM]) substantially attenuated all three parameters while the addition of the inhibitor of ERK phosphorylation (CM+PD) ([10 µM]) resulted in a significant decrease of covered area and total tube length but had no significant effect on the reduction of the number of branches. Data are given as mean + s.e.m. and values are presented as percentage of corresponding controls. *: p < 0.05.

    Techniques Used: Incubation

    mouse anti phospho akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc mouse anti phospho akt
    <t>Double</t> <t>immunostaining</t> showed that a subpopulation of BDNF immunoreactive cells in L6 DRG during cystitis (A, green staining, white arrows) was co-localized with <t>p-Akt</t> (B: red staining). A number of BDNF positive cells (C, green arrows) did not express p-Akt. Bar = 60 µm. Five L6 DRGs from animals with cystitis were analyzed and consistent results were achieved.
    Mouse Anti Phospho Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "In Vivo Regulation of Brain-Derived Neurotrophic Factor in Dorsal Root Ganglia Is Mediated by Nerve Growth Factor-Triggered Akt Activation during Cystitis"

    Article Title: In Vivo Regulation of Brain-Derived Neurotrophic Factor in Dorsal Root Ganglia Is Mediated by Nerve Growth Factor-Triggered Akt Activation during Cystitis

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0081547

    Double immunostaining showed that a subpopulation of BDNF immunoreactive cells in L6 DRG during cystitis (A, green staining, white arrows) was co-localized with p-Akt (B: red staining). A number of BDNF positive cells (C, green arrows) did not express p-Akt. Bar = 60 µm. Five L6 DRGs from animals with cystitis were analyzed and consistent results were achieved.
    Figure Legend Snippet: Double immunostaining showed that a subpopulation of BDNF immunoreactive cells in L6 DRG during cystitis (A, green staining, white arrows) was co-localized with p-Akt (B: red staining). A number of BDNF positive cells (C, green arrows) did not express p-Akt. Bar = 60 µm. Five L6 DRGs from animals with cystitis were analyzed and consistent results were achieved.

    Techniques Used: Double Immunostaining, Staining

    total akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total akt
    Total Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    total akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total akt
    Phosphorylated forms of <t>Akt</t> <t>and</t> <t>ERK1/2</t> are present in the caudal hindbrain . (a) Western Blot analysis of protein extracts of whole embryos (left column) and isolated caudal hindbrain (right column). Phosphorylated (activated) forms of both Akt and ERK1/2 were present in protein extracts from the caudal hindbrain. Total forms of Akt and ERK1/2 were used as loading controls. pERK1/2 immunodetection is shown in red (b, d-e, h-k) or in green fluorescence in (f). In situ hybridization with vHnf1-Hoxb1 (c) and vHnf1 (g) to position the caudal hindbrain. (i-k) Control experiments to show the specificity of pErk staining: embryos incubated with DMSO (i) or with SU5402 (j), and assayed for pErk (note that specific pErk staining in the MHB and in the caudal hindbrain disappears upon SU5402 treatment); (k) embryos treated as in (i) but without pErk-Ab incubation, as negative control. Whole-mount embryos (b-d, f-g, i-k), or flat-mounted hindbrains (e, h) at indicated stages. ANR, anterior neural ridge; cHB, caudal hindbrain; FB, forebrain; HB, hindbrain; im, intermediate mesoderm; MHB, midbrain-hindbrain boundary; pm, precardiac mesoderm; ps: primitive strike; psm, presomitic mesoderm. Anterior is at the top.
    Total Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "FGF signaling controls caudal hindbrain specification through Ras-ERK1/2 pathway"

    Article Title: FGF signaling controls caudal hindbrain specification through Ras-ERK1/2 pathway

    Journal: BMC Developmental Biology

    doi: 10.1186/1471-213X-9-61

    Phosphorylated forms of Akt and ERK1/2 are present in the caudal hindbrain . (a) Western Blot analysis of protein extracts of whole embryos (left column) and isolated caudal hindbrain (right column). Phosphorylated (activated) forms of both Akt and ERK1/2 were present in protein extracts from the caudal hindbrain. Total forms of Akt and ERK1/2 were used as loading controls. pERK1/2 immunodetection is shown in red (b, d-e, h-k) or in green fluorescence in (f). In situ hybridization with vHnf1-Hoxb1 (c) and vHnf1 (g) to position the caudal hindbrain. (i-k) Control experiments to show the specificity of pErk staining: embryos incubated with DMSO (i) or with SU5402 (j), and assayed for pErk (note that specific pErk staining in the MHB and in the caudal hindbrain disappears upon SU5402 treatment); (k) embryos treated as in (i) but without pErk-Ab incubation, as negative control. Whole-mount embryos (b-d, f-g, i-k), or flat-mounted hindbrains (e, h) at indicated stages. ANR, anterior neural ridge; cHB, caudal hindbrain; FB, forebrain; HB, hindbrain; im, intermediate mesoderm; MHB, midbrain-hindbrain boundary; pm, precardiac mesoderm; ps: primitive strike; psm, presomitic mesoderm. Anterior is at the top.
    Figure Legend Snippet: Phosphorylated forms of Akt and ERK1/2 are present in the caudal hindbrain . (a) Western Blot analysis of protein extracts of whole embryos (left column) and isolated caudal hindbrain (right column). Phosphorylated (activated) forms of both Akt and ERK1/2 were present in protein extracts from the caudal hindbrain. Total forms of Akt and ERK1/2 were used as loading controls. pERK1/2 immunodetection is shown in red (b, d-e, h-k) or in green fluorescence in (f). In situ hybridization with vHnf1-Hoxb1 (c) and vHnf1 (g) to position the caudal hindbrain. (i-k) Control experiments to show the specificity of pErk staining: embryos incubated with DMSO (i) or with SU5402 (j), and assayed for pErk (note that specific pErk staining in the MHB and in the caudal hindbrain disappears upon SU5402 treatment); (k) embryos treated as in (i) but without pErk-Ab incubation, as negative control. Whole-mount embryos (b-d, f-g, i-k), or flat-mounted hindbrains (e, h) at indicated stages. ANR, anterior neural ridge; cHB, caudal hindbrain; FB, forebrain; HB, hindbrain; im, intermediate mesoderm; MHB, midbrain-hindbrain boundary; pm, precardiac mesoderm; ps: primitive strike; psm, presomitic mesoderm. Anterior is at the top.

    Techniques Used: Western Blot, Isolation, Immunodetection, Fluorescence, In Situ Hybridization, Staining, Incubation, Negative Control

    MKP3 is dependent on ERK1/2 but not Akt activation . (A) Beads soaked with specific inhibitors were placed in the caudal hindbrain or in the presumptive MHB of HH7 + -8 explanted embryos. Pharmacological treatments were as follows: DMSO (a), FGFR inhibitor SU5402 (b), ERK1/2 inhibitor PD184352 (c), PI3K inhibitor LY294002 (d). Explants were incubated during 6 h at 38°C. (B) Jurkat cells (left side lanes) and HH7-8 explanted embryos (right side lanes) were treated with DMSO, SU5402, PD184352 or LY294002 and analyzed by western blot for total and phosphorylated forms of Akt and ERK1/2. PD184352 treatment impeded ERK1/2 phosphorylation without affecting the PI3K-Akt pathway and, conversely, LY294002 treatment abolished Akt phosphorylation without affecting the Ras-ERK1/2 pathway. Embryos are shown in whole-mount with anterior to the top.
    Figure Legend Snippet: MKP3 is dependent on ERK1/2 but not Akt activation . (A) Beads soaked with specific inhibitors were placed in the caudal hindbrain or in the presumptive MHB of HH7 + -8 explanted embryos. Pharmacological treatments were as follows: DMSO (a), FGFR inhibitor SU5402 (b), ERK1/2 inhibitor PD184352 (c), PI3K inhibitor LY294002 (d). Explants were incubated during 6 h at 38°C. (B) Jurkat cells (left side lanes) and HH7-8 explanted embryos (right side lanes) were treated with DMSO, SU5402, PD184352 or LY294002 and analyzed by western blot for total and phosphorylated forms of Akt and ERK1/2. PD184352 treatment impeded ERK1/2 phosphorylation without affecting the PI3K-Akt pathway and, conversely, LY294002 treatment abolished Akt phosphorylation without affecting the Ras-ERK1/2 pathway. Embryos are shown in whole-mount with anterior to the top.

    Techniques Used: Activation Assay, Incubation, Western Blot

    MafB and Krox20 are dependent on ERK1/2 but not on Akt activation . HH7 + -8 embryos (a-d, f-i,k-m) or HH9 (e, j) were explanted and beads soaked in specific inhibitors were placed in the caudal hindbrain. Afterwards, embryos were analyzed for Krox20 , MafB or Fgf3 expression. Pharmacological treatments were as follows: DMSO (a, f,k), FGFR inhibitor SU5402 (b, e,g,j,l), ERK1/2 inhibitor PD184352 (c, h,m), or PI3K inhibitor LY294002 (d, i), during 6 h. Embryos are shown in whole-mount with anterior to the top.
    Figure Legend Snippet: MafB and Krox20 are dependent on ERK1/2 but not on Akt activation . HH7 + -8 embryos (a-d, f-i,k-m) or HH9 (e, j) were explanted and beads soaked in specific inhibitors were placed in the caudal hindbrain. Afterwards, embryos were analyzed for Krox20 , MafB or Fgf3 expression. Pharmacological treatments were as follows: DMSO (a, f,k), FGFR inhibitor SU5402 (b, e,g,j,l), ERK1/2 inhibitor PD184352 (c, h,m), or PI3K inhibitor LY294002 (d, i), during 6 h. Embryos are shown in whole-mount with anterior to the top.

    Techniques Used: Activation Assay, Expressing

    anti total akt antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti total akt antibody
    ( a ) Relative expression ratios of <t>p-Akt</t> was normalized to <t>total</t> <t>Akt.</t> **p<0.01. ( b ) The expression of eNOS protein for MSCs was examined by fluorescence microscopy. Cells were stained with primary anti-eNOS antibody followed by FITC-conjugated immunoglobulin (green color fluorescence). Cell nuclei was stained by DAPI. Scale bar = 10 µm. Semi-quantitative measurement of fluorescence intensity revealed a significantly higher level of eNOS expression compared with the control. *p<0.01: greater than control (TCPS).
    Anti Total Akt Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "In Vitro Study of a Novel Nanogold-Collagen Composite to Enhance the Mesenchymal Stem Cell Behavior for Vascular Regeneration"

    Article Title: In Vitro Study of a Novel Nanogold-Collagen Composite to Enhance the Mesenchymal Stem Cell Behavior for Vascular Regeneration

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0104019

    ( a ) Relative expression ratios of p-Akt was normalized to total Akt. **p<0.01. ( b ) The expression of eNOS protein for MSCs was examined by fluorescence microscopy. Cells were stained with primary anti-eNOS antibody followed by FITC-conjugated immunoglobulin (green color fluorescence). Cell nuclei was stained by DAPI. Scale bar = 10 µm. Semi-quantitative measurement of fluorescence intensity revealed a significantly higher level of eNOS expression compared with the control. *p<0.01: greater than control (TCPS).
    Figure Legend Snippet: ( a ) Relative expression ratios of p-Akt was normalized to total Akt. **p<0.01. ( b ) The expression of eNOS protein for MSCs was examined by fluorescence microscopy. Cells were stained with primary anti-eNOS antibody followed by FITC-conjugated immunoglobulin (green color fluorescence). Cell nuclei was stained by DAPI. Scale bar = 10 µm. Semi-quantitative measurement of fluorescence intensity revealed a significantly higher level of eNOS expression compared with the control. *p<0.01: greater than control (TCPS).

    Techniques Used: Expressing, Fluorescence, Microscopy, Staining

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    • total akt  (Cell Signaling Technology Inc)
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    Cell Signaling Technology Inc total akt
    A , putative miR-221-binding sites (red) in the 3′-UTRs of PTEN ( top ). The middle panel shows sequence alignment of the miR-221 sequences (red color) with a region of the PTEN 3′-UTR (red) from indicated species. The bottom shows a mutant of PTEN 3′-UTR for pMIR-REPORT. B , SOSP-9607 cells were transfected with miR-221 mimic, miR-221 inhibitor, scramble oligonucleotide or nothing (blank). And then indicated protein and mRNA were detected. Rows 1 to 7, the expression of PTEN, <t>phospho-Akt</t> (p-Akt), total-Akt <t>(t-Akt),</t> Cyclin D1 (CCND1), p27 and p57 were analyzed by Western blot; row 8, β-actin was used as a loading control; row 9, PTEN mRNA level was measured by RT-PCR; row 10, GAPDH was used as an control. C , SOSP-9607 cells were co-transfected with miR-221 mimic or scramble oligonucleotide, and pMIR-REPORT vector consisting of a luciferase gene containing the wild type (PTEN-3′-UTR) or mutated (PTEN-mut-3′-UTR) miR-221 binding sites in its 3′-UTR region by using Lipofectamine 2000 reagent. The cells were also transfected with 50 ng pRL-TK vector as an internal standard. 24 h after transfection, luciferase activity was measured by using a dual luciferase reporter assay (Promega). D , similar experiments were performed in MG63 cells as described in panel C except that miR-221 mimic was instead by miR-221 inhibitor. The results were presented as relative luciferase activity (firefly Luc/Renilla Luc). All experiments were repeated three times in triplicate. Columns, mean of three independent experiments; bars, SD. **, p<0.01.
    Total Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phosphor akt  (Cell Signaling Technology Inc)
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    Cell Signaling Technology Inc phosphor akt
    (A) <t>Vehicle-Hone1,</t> <t>fibulin-5-Hone1,</t> vehicle-TW01, and fibulin-5-TW01 transfected cells were serum-starved and treated with the indicated inhibitors, SB202190, PD98059, and LY294002 or solvent for 24 hour. The migration and invasion ratios of vehicle-Hone1 and fibulin-5-Hone1 transfected cells were determined as previously described. (B) The fibulin-5 expressing cells of Hone1 and TW01 were serum-starved for 24 hour and treated with or without LY294002 at the final concentration of 10 μM. The Total cell lysates of vehicle-Hone1, fibulin-5-Hone1, vehicle-TW01, and fibulin-5-TW01 transfected cells were immunoblotted for the unphosphorylated and phosphorylated forms of <t>AKT.</t> β-actin was used as the internal loading control. (C) A negative control and fibulin-5 siRNAs were transfected into Hone1 cells for 24 hour and western blotting was performed as in (B).
    Phosphor Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    mouse anti phospho akt  (Cell Signaling Technology Inc)
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    Cell Signaling Technology Inc mouse anti phospho akt
    <t>Double</t> <t>immunostaining</t> showed that a subpopulation of BDNF immunoreactive cells in L6 DRG during cystitis (A, green staining, white arrows) was co-localized with <t>p-Akt</t> (B: red staining). A number of BDNF positive cells (C, green arrows) did not express p-Akt. Bar = 60 µm. Five L6 DRGs from animals with cystitis were analyzed and consistent results were achieved.
    Mouse Anti Phospho Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti total akt antibody  (Cell Signaling Technology Inc)
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    Cell Signaling Technology Inc anti total akt antibody
    ( a ) Relative expression ratios of <t>p-Akt</t> was normalized to <t>total</t> <t>Akt.</t> **p<0.01. ( b ) The expression of eNOS protein for MSCs was examined by fluorescence microscopy. Cells were stained with primary anti-eNOS antibody followed by FITC-conjugated immunoglobulin (green color fluorescence). Cell nuclei was stained by DAPI. Scale bar = 10 µm. Semi-quantitative measurement of fluorescence intensity revealed a significantly higher level of eNOS expression compared with the control. *p<0.01: greater than control (TCPS).
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    Image Search Results


    A , putative miR-221-binding sites (red) in the 3′-UTRs of PTEN ( top ). The middle panel shows sequence alignment of the miR-221 sequences (red color) with a region of the PTEN 3′-UTR (red) from indicated species. The bottom shows a mutant of PTEN 3′-UTR for pMIR-REPORT. B , SOSP-9607 cells were transfected with miR-221 mimic, miR-221 inhibitor, scramble oligonucleotide or nothing (blank). And then indicated protein and mRNA were detected. Rows 1 to 7, the expression of PTEN, phospho-Akt (p-Akt), total-Akt (t-Akt), Cyclin D1 (CCND1), p27 and p57 were analyzed by Western blot; row 8, β-actin was used as a loading control; row 9, PTEN mRNA level was measured by RT-PCR; row 10, GAPDH was used as an control. C , SOSP-9607 cells were co-transfected with miR-221 mimic or scramble oligonucleotide, and pMIR-REPORT vector consisting of a luciferase gene containing the wild type (PTEN-3′-UTR) or mutated (PTEN-mut-3′-UTR) miR-221 binding sites in its 3′-UTR region by using Lipofectamine 2000 reagent. The cells were also transfected with 50 ng pRL-TK vector as an internal standard. 24 h after transfection, luciferase activity was measured by using a dual luciferase reporter assay (Promega). D , similar experiments were performed in MG63 cells as described in panel C except that miR-221 mimic was instead by miR-221 inhibitor. The results were presented as relative luciferase activity (firefly Luc/Renilla Luc). All experiments were repeated three times in triplicate. Columns, mean of three independent experiments; bars, SD. **, p<0.01.

    Journal: PLoS ONE

    Article Title: MicroRNA-221 Induces Cell Survival and Cisplatin Resistance through PI3K/Akt Pathway in Human Osteosarcoma

    doi: 10.1371/journal.pone.0053906

    Figure Lengend Snippet: A , putative miR-221-binding sites (red) in the 3′-UTRs of PTEN ( top ). The middle panel shows sequence alignment of the miR-221 sequences (red color) with a region of the PTEN 3′-UTR (red) from indicated species. The bottom shows a mutant of PTEN 3′-UTR for pMIR-REPORT. B , SOSP-9607 cells were transfected with miR-221 mimic, miR-221 inhibitor, scramble oligonucleotide or nothing (blank). And then indicated protein and mRNA were detected. Rows 1 to 7, the expression of PTEN, phospho-Akt (p-Akt), total-Akt (t-Akt), Cyclin D1 (CCND1), p27 and p57 were analyzed by Western blot; row 8, β-actin was used as a loading control; row 9, PTEN mRNA level was measured by RT-PCR; row 10, GAPDH was used as an control. C , SOSP-9607 cells were co-transfected with miR-221 mimic or scramble oligonucleotide, and pMIR-REPORT vector consisting of a luciferase gene containing the wild type (PTEN-3′-UTR) or mutated (PTEN-mut-3′-UTR) miR-221 binding sites in its 3′-UTR region by using Lipofectamine 2000 reagent. The cells were also transfected with 50 ng pRL-TK vector as an internal standard. 24 h after transfection, luciferase activity was measured by using a dual luciferase reporter assay (Promega). D , similar experiments were performed in MG63 cells as described in panel C except that miR-221 mimic was instead by miR-221 inhibitor. The results were presented as relative luciferase activity (firefly Luc/Renilla Luc). All experiments were repeated three times in triplicate. Columns, mean of three independent experiments; bars, SD. **, p<0.01.

    Article Snippet: The membranes were blocked with TBST containing 5% non-fat dry milk for 1 h and incubated with primary antibody against PTEN (abcam, China), phospho-Akt (Cell Signaling Technology, Canada), total-AKT (Cell Signaling Technology, Canada), cyclin D1 (abcam, China), Bcl-2 (abcam, China), p27 (Santa Cruz, USA), p57 (abcam, China), β-Actin (Santa Cruz, USA) overnight at 4°C.

    Techniques: Binding Assay, Sequencing, Mutagenesis, Transfection, Expressing, Western Blot, Reverse Transcription Polymerase Chain Reaction, Plasmid Preparation, Luciferase, Activity Assay, Reporter Assay

    A , SOSP-9607 cells were transfected with miR-221 mimic (221 Mi), scramble oligonucleotide (Scr) or cotransfected with miR-221 mimic and pcDNA-PTEN. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. B , SOSP-9607 cells were transfected with miR-221 mimic, scramble oligonucleotide or cotransfected with miR-221 mimic and LY294002. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. C , SOSP-9607 and MG 63 cells were treated as described in panel A. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. D , SOSP-9607 and MG 63 cells were all treated as described in panel B. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. E , both SOSP-9607 and MG 63 cells treated as described in panel A were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit (Promega) according to the manufacturer's instructions. F , both SOSP-9607 and MG 63 cells treated as described in panel B were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit. Columns, mean of three independent experiments; bars, SD; **, p<0.01, ***, p<0.001.

    Journal: PLoS ONE

    Article Title: MicroRNA-221 Induces Cell Survival and Cisplatin Resistance through PI3K/Akt Pathway in Human Osteosarcoma

    doi: 10.1371/journal.pone.0053906

    Figure Lengend Snippet: A , SOSP-9607 cells were transfected with miR-221 mimic (221 Mi), scramble oligonucleotide (Scr) or cotransfected with miR-221 mimic and pcDNA-PTEN. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. B , SOSP-9607 cells were transfected with miR-221 mimic, scramble oligonucleotide or cotransfected with miR-221 mimic and LY294002. The scramble group was used as a control. The expression of PTEN and phospho-Akt (p-Akt) were analyzed by western blot. β-actin was used as a loading control. C , SOSP-9607 and MG 63 cells were treated as described in panel A. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. D , SOSP-9607 and MG 63 cells were all treated as described in panel B. Then the cells were treated with or without cisplatin for 48 h and viability evaluation were examined. Data were presented as the percentage of viability inhibition measured in cells treated without cisplatin. E , both SOSP-9607 and MG 63 cells treated as described in panel A were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit (Promega) according to the manufacturer's instructions. F , both SOSP-9607 and MG 63 cells treated as described in panel B were seeded into 96-well plates and 24 h later were treated with or without cisplatin for 24 h. Caspase3 activity was measured using Caspase-Glo® 3/7 assay kit. Columns, mean of three independent experiments; bars, SD; **, p<0.01, ***, p<0.001.

    Article Snippet: The membranes were blocked with TBST containing 5% non-fat dry milk for 1 h and incubated with primary antibody against PTEN (abcam, China), phospho-Akt (Cell Signaling Technology, Canada), total-AKT (Cell Signaling Technology, Canada), cyclin D1 (abcam, China), Bcl-2 (abcam, China), p27 (Santa Cruz, USA), p57 (abcam, China), β-Actin (Santa Cruz, USA) overnight at 4°C.

    Techniques: Transfection, Expressing, Western Blot, Inhibition, Activity Assay, Caspase-Glo Assay

    (A) Vehicle-Hone1, fibulin-5-Hone1, vehicle-TW01, and fibulin-5-TW01 transfected cells were serum-starved and treated with the indicated inhibitors, SB202190, PD98059, and LY294002 or solvent for 24 hour. The migration and invasion ratios of vehicle-Hone1 and fibulin-5-Hone1 transfected cells were determined as previously described. (B) The fibulin-5 expressing cells of Hone1 and TW01 were serum-starved for 24 hour and treated with or without LY294002 at the final concentration of 10 μM. The Total cell lysates of vehicle-Hone1, fibulin-5-Hone1, vehicle-TW01, and fibulin-5-TW01 transfected cells were immunoblotted for the unphosphorylated and phosphorylated forms of AKT. β-actin was used as the internal loading control. (C) A negative control and fibulin-5 siRNAs were transfected into Hone1 cells for 24 hour and western blotting was performed as in (B).

    Journal: PLoS ONE

    Article Title: Oncogenic Fibulin-5 Promotes Nasopharyngeal Carcinoma Cell Metastasis through the FLJ10540/AKT Pathway and Correlates with Poor Prognosis

    doi: 10.1371/journal.pone.0084218

    Figure Lengend Snippet: (A) Vehicle-Hone1, fibulin-5-Hone1, vehicle-TW01, and fibulin-5-TW01 transfected cells were serum-starved and treated with the indicated inhibitors, SB202190, PD98059, and LY294002 or solvent for 24 hour. The migration and invasion ratios of vehicle-Hone1 and fibulin-5-Hone1 transfected cells were determined as previously described. (B) The fibulin-5 expressing cells of Hone1 and TW01 were serum-starved for 24 hour and treated with or without LY294002 at the final concentration of 10 μM. The Total cell lysates of vehicle-Hone1, fibulin-5-Hone1, vehicle-TW01, and fibulin-5-TW01 transfected cells were immunoblotted for the unphosphorylated and phosphorylated forms of AKT. β-actin was used as the internal loading control. (C) A negative control and fibulin-5 siRNAs were transfected into Hone1 cells for 24 hour and western blotting was performed as in (B).

    Article Snippet: Antibodies included against fibulin-5 (Epitomics), FLJ10540 (generated by us) [ , ], DDK (Origene), phosphor-AKT and AKT (Cell Signaling Technology, Beverely, MA, USA), lamin A/C, and β-actin (monoclonal; Santa Cruz Biotechnology, Santa Cruz, CA, USA) were applied.

    Techniques: Transfection, Migration, Expressing, Concentration Assay, Negative Control, Western Blot

    (A) Hone1-expressing FLJ10540 cells were serum-starved for 24 hour and treated with or without AKT inhibitor. The Total cell lysates of vehicle-Hone and FLJ10540-Hone1, transfected cells were immunoblotted for the unphosphorylated and phosphorylated forms of AKT. β-actin was used as the internal loading control. (B) A negative control and FLJ10540 siRNAs were transfected into Hone1 cells for 24 hour and western blotting was performed as in (B). (C) Vehicle-Hone1 and FLJ10540-Hone1 transfected cells were serum-starved and treated with the AKT inhibitor for 24 hour. The migration and invasion ratios of vehicle-Hone1 and fibulin-5-Hone1 transfected cells were determined as previously described.

    Journal: PLoS ONE

    Article Title: Oncogenic Fibulin-5 Promotes Nasopharyngeal Carcinoma Cell Metastasis through the FLJ10540/AKT Pathway and Correlates with Poor Prognosis

    doi: 10.1371/journal.pone.0084218

    Figure Lengend Snippet: (A) Hone1-expressing FLJ10540 cells were serum-starved for 24 hour and treated with or without AKT inhibitor. The Total cell lysates of vehicle-Hone and FLJ10540-Hone1, transfected cells were immunoblotted for the unphosphorylated and phosphorylated forms of AKT. β-actin was used as the internal loading control. (B) A negative control and FLJ10540 siRNAs were transfected into Hone1 cells for 24 hour and western blotting was performed as in (B). (C) Vehicle-Hone1 and FLJ10540-Hone1 transfected cells were serum-starved and treated with the AKT inhibitor for 24 hour. The migration and invasion ratios of vehicle-Hone1 and fibulin-5-Hone1 transfected cells were determined as previously described.

    Article Snippet: Antibodies included against fibulin-5 (Epitomics), FLJ10540 (generated by us) [ , ], DDK (Origene), phosphor-AKT and AKT (Cell Signaling Technology, Beverely, MA, USA), lamin A/C, and β-actin (monoclonal; Santa Cruz Biotechnology, Santa Cruz, CA, USA) were applied.

    Techniques: Expressing, Transfection, Negative Control, Western Blot, Migration

    Double immunostaining showed that a subpopulation of BDNF immunoreactive cells in L6 DRG during cystitis (A, green staining, white arrows) was co-localized with p-Akt (B: red staining). A number of BDNF positive cells (C, green arrows) did not express p-Akt. Bar = 60 µm. Five L6 DRGs from animals with cystitis were analyzed and consistent results were achieved.

    Journal: PLoS ONE

    Article Title: In Vivo Regulation of Brain-Derived Neurotrophic Factor in Dorsal Root Ganglia Is Mediated by Nerve Growth Factor-Triggered Akt Activation during Cystitis

    doi: 10.1371/journal.pone.0081547

    Figure Lengend Snippet: Double immunostaining showed that a subpopulation of BDNF immunoreactive cells in L6 DRG during cystitis (A, green staining, white arrows) was co-localized with p-Akt (B: red staining). A number of BDNF positive cells (C, green arrows) did not express p-Akt. Bar = 60 µm. Five L6 DRGs from animals with cystitis were analyzed and consistent results were achieved.

    Article Snippet: In double immunostaining, we used mouse anti-phospho-Akt (1:400, Cell Signaling Technology Inc. Danvers, MA) co-staining with rabbit anti-BDNF, or rabbit anti-TrkA (1:750, Santa Cruz Biotechnology, Inc., CA) co-staining with sheep anti-BDNF (1:500, Millipore, Billerica, MA).

    Techniques: Double Immunostaining, Staining

    ( a ) Relative expression ratios of p-Akt was normalized to total Akt. **p<0.01. ( b ) The expression of eNOS protein for MSCs was examined by fluorescence microscopy. Cells were stained with primary anti-eNOS antibody followed by FITC-conjugated immunoglobulin (green color fluorescence). Cell nuclei was stained by DAPI. Scale bar = 10 µm. Semi-quantitative measurement of fluorescence intensity revealed a significantly higher level of eNOS expression compared with the control. *p<0.01: greater than control (TCPS).

    Journal: PLoS ONE

    Article Title: In Vitro Study of a Novel Nanogold-Collagen Composite to Enhance the Mesenchymal Stem Cell Behavior for Vascular Regeneration

    doi: 10.1371/journal.pone.0104019

    Figure Lengend Snippet: ( a ) Relative expression ratios of p-Akt was normalized to total Akt. **p<0.01. ( b ) The expression of eNOS protein for MSCs was examined by fluorescence microscopy. Cells were stained with primary anti-eNOS antibody followed by FITC-conjugated immunoglobulin (green color fluorescence). Cell nuclei was stained by DAPI. Scale bar = 10 µm. Semi-quantitative measurement of fluorescence intensity revealed a significantly higher level of eNOS expression compared with the control. *p<0.01: greater than control (TCPS).

    Article Snippet: After then, membrane was blocked with 5% non-fat dry milk in PBS for 1 h at room temperature before overnight incubation at 4°C with the primary anti-phospho-FAK (Tyr-576/577) antibody (1∶500 dilution, Cell Signaling), anti-phospho-Akt (Ser-473) antibody (1∶500 dilution, Cell Signaling) and loading controls [anti-total-FAK antibody (1∶2000 dilution, Cell signaling); anti-total-Akt antibody (1:2000 dilution, Cell Signaling] to ensure standard of loading control.

    Techniques: Expressing, Fluorescence, Microscopy, Staining