anti akt  (Abcam)

 
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    Name:
    Anti AKT1 2 3 antibody EPR16798
    Description:

    Catalog Number:
    ab179463
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    Structured Review

    Abcam anti akt
    XIST modulates miR-34a downstream <t>MET-PI3K-AKT</t> signaling via miR-34a ( a - c ) KAT18 and FTC113 cells were co-transfected with si-XIST and miR-34a inhibitor; the protein levels of MET, p-PI3K, PI3K, p-AKT and AKT were examined using Immunoblotting assays. The data are presented as mean ± SD of three independent experiments. ** P

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    Images

    1) Product Images from "LncRNA XIST/miR-34a axis modulates the cell proliferation and tumor growth of thyroid cancer through MET-PI3K-AKT signaling"

    Article Title: LncRNA XIST/miR-34a axis modulates the cell proliferation and tumor growth of thyroid cancer through MET-PI3K-AKT signaling

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    doi: 10.1186/s13046-018-0950-9

    XIST modulates miR-34a downstream MET-PI3K-AKT signaling via miR-34a ( a - c ) KAT18 and FTC113 cells were co-transfected with si-XIST and miR-34a inhibitor; the protein levels of MET, p-PI3K, PI3K, p-AKT and AKT were examined using Immunoblotting assays. The data are presented as mean ± SD of three independent experiments. ** P
    Figure Legend Snippet: XIST modulates miR-34a downstream MET-PI3K-AKT signaling via miR-34a ( a - c ) KAT18 and FTC113 cells were co-transfected with si-XIST and miR-34a inhibitor; the protein levels of MET, p-PI3K, PI3K, p-AKT and AKT were examined using Immunoblotting assays. The data are presented as mean ± SD of three independent experiments. ** P

    Techniques Used: Transfection

    2) Product Images from "Assessing the Pharmacological and Therapeutic Efficacy of Traditional Chinese Medicine Liangxue Tongyu Prescription for Intracerebral Hemorrhagic Stroke in Neurological Disease Models"

    Article Title: Assessing the Pharmacological and Therapeutic Efficacy of Traditional Chinese Medicine Liangxue Tongyu Prescription for Intracerebral Hemorrhagic Stroke in Neurological Disease Models

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2018.01169

    The simplified PI3K-AKT pathway regulation of compounds in LP. Radix Paeoniae Rubra. RO, Rheum officinale Baill.; RG, Rehmannia glutinosa (Gaertn.) Li-bosch.; PN, Panax notoginseng (Burk.) F. H. Chen.; PS, Paeonia suffruticosa Andr.; AT, Acorus tatarinowii Schott.; BB, Bubalus bubalis Linnaeus.; PA, Pheretima aspergillum (E. Perrier).
    Figure Legend Snippet: The simplified PI3K-AKT pathway regulation of compounds in LP. Radix Paeoniae Rubra. RO, Rheum officinale Baill.; RG, Rehmannia glutinosa (Gaertn.) Li-bosch.; PN, Panax notoginseng (Burk.) F. H. Chen.; PS, Paeonia suffruticosa Andr.; AT, Acorus tatarinowii Schott.; BB, Bubalus bubalis Linnaeus.; PA, Pheretima aspergillum (E. Perrier).

    Techniques Used:

    Effects of Taurine, Geniposide, GRg1, and GRb1 in LP on L-Glu-damaged PC12 and normal PC12. (A) The PI3K and AKT mRNA level by RT-QPCR. (B) The p-AKT and p-PI3K protein level. β-Actin was measured as an internal control. The results are representative of three independent experiments. ∗ P
    Figure Legend Snippet: Effects of Taurine, Geniposide, GRg1, and GRb1 in LP on L-Glu-damaged PC12 and normal PC12. (A) The PI3K and AKT mRNA level by RT-QPCR. (B) The p-AKT and p-PI3K protein level. β-Actin was measured as an internal control. The results are representative of three independent experiments. ∗ P

    Techniques Used: Quantitative RT-PCR

    3) Product Images from "Transcriptome Profiling of Neovascularized Corneas Reveals miR-204 as a Multi-target Biotherapy Deliverable by rAAVs"

    Article Title: Transcriptome Profiling of Neovascularized Corneas Reveals miR-204 as a Multi-target Biotherapy Deliverable by rAAVs

    Journal: Molecular Therapy. Nucleic Acids

    doi: 10.1016/j.omtn.2017.12.019

    The Anti-angiogenic Effect of Overexpressing miR-204 Is Due in Part to Targeting the Angpt1/Tie2/PI3K/Akt Pathway (A) Real-time qPCR analysis of miR-204 expression in mouse corneas by intrastromal or subconjunctival injection. (B) Real-time qPCR analysis of angpt1 and vegf mRNA expression. (C) Western blot analysis of ANGPT1 and VEGF expression, and the phosphorylation states of key factors in the Tie2/PI3K/Akt pathway. n = 6/group. Error bars are ± SD. The notably large SD values observed are due to the variability inherent to in vivo experiments and the relatively small quantity of protein and mRNA obtained from mouse corneas. n.s., no significant difference. *p
    Figure Legend Snippet: The Anti-angiogenic Effect of Overexpressing miR-204 Is Due in Part to Targeting the Angpt1/Tie2/PI3K/Akt Pathway (A) Real-time qPCR analysis of miR-204 expression in mouse corneas by intrastromal or subconjunctival injection. (B) Real-time qPCR analysis of angpt1 and vegf mRNA expression. (C) Western blot analysis of ANGPT1 and VEGF expression, and the phosphorylation states of key factors in the Tie2/PI3K/Akt pathway. n = 6/group. Error bars are ± SD. The notably large SD values observed are due to the variability inherent to in vivo experiments and the relatively small quantity of protein and mRNA obtained from mouse corneas. n.s., no significant difference. *p

    Techniques Used: Real-time Polymerase Chain Reaction, Expressing, Injection, Western Blot, In Vivo

    4) Product Images from "YY1 targets tubulin polymerisation-promoting protein to inhibit migration, invasion and angiogenesis in pancreatic cancer via p38/MAPK and PI3K/AKT pathways"

    Article Title: YY1 targets tubulin polymerisation-promoting protein to inhibit migration, invasion and angiogenesis in pancreatic cancer via p38/MAPK and PI3K/AKT pathways

    Journal: British Journal of Cancer

    doi: 10.1038/s41416-019-0604-5

    a PANC-1 vector and PANC-1-TPPP cells (1.5 × 10 6 cells/100 μl) were separately injected into the tail vein of each mouse. Four weeks later, lung and liver metastases were evaluated by macroscopic observation and by histomorphology under microscopy. Scale bar = 200 μm. The arrows indicate the metastases. b Table listing the incidence of metastases in the nude mice treated with the vector or TPPP. c There were no statistically significant differences in the expression of EMT signalling pathway-related proteins between the two groups. d Effects of TPPP and its corresponding control group on MMP3, MMP7 and VEGF expression. e Effects of YY1, YY1 + TPPP and their corresponding control groups on MMP3 and MMP7 expression. f The expression of p38, p-p38, MAPK, p-MAPK, PI3K, p-PI3K, AKT and p-AKT in PANC-1 and BxPC-3 cells after TPPP overexpression
    Figure Legend Snippet: a PANC-1 vector and PANC-1-TPPP cells (1.5 × 10 6 cells/100 μl) were separately injected into the tail vein of each mouse. Four weeks later, lung and liver metastases were evaluated by macroscopic observation and by histomorphology under microscopy. Scale bar = 200 μm. The arrows indicate the metastases. b Table listing the incidence of metastases in the nude mice treated with the vector or TPPP. c There were no statistically significant differences in the expression of EMT signalling pathway-related proteins between the two groups. d Effects of TPPP and its corresponding control group on MMP3, MMP7 and VEGF expression. e Effects of YY1, YY1 + TPPP and their corresponding control groups on MMP3 and MMP7 expression. f The expression of p38, p-p38, MAPK, p-MAPK, PI3K, p-PI3K, AKT and p-AKT in PANC-1 and BxPC-3 cells after TPPP overexpression

    Techniques Used: Plasmid Preparation, Injection, Microscopy, Mouse Assay, Expressing, Over Expression

    a PANC-1 vector and PANC-1-TPPP cells (1.5 × 10 6 cells/100 μl) were separately injected into the tail vein of each mouse. Four weeks later, lung and liver metastases were evaluated by macroscopic observation and by histomorphology under microscopy. Scale bar = 200 μm. The arrows indicate the metastases. b Table listing the incidence of metastases in the nude mice treated with the vector or TPPP. c There were no statistically significant differences in the expression of EMT signalling pathway-related proteins between the two groups. d Effects of TPPP and its corresponding control group on MMP3, MMP7 and VEGF expression. e Effects of YY1, YY1 + TPPP and their corresponding control groups on MMP3 and MMP7 expression. f The expression of p38, p-p38, MAPK, p-MAPK, PI3K, p-PI3K, AKT and p-AKT in PANC-1 and BxPC-3 cells after TPPP overexpression
    Figure Legend Snippet: a PANC-1 vector and PANC-1-TPPP cells (1.5 × 10 6 cells/100 μl) were separately injected into the tail vein of each mouse. Four weeks later, lung and liver metastases were evaluated by macroscopic observation and by histomorphology under microscopy. Scale bar = 200 μm. The arrows indicate the metastases. b Table listing the incidence of metastases in the nude mice treated with the vector or TPPP. c There were no statistically significant differences in the expression of EMT signalling pathway-related proteins between the two groups. d Effects of TPPP and its corresponding control group on MMP3, MMP7 and VEGF expression. e Effects of YY1, YY1 + TPPP and their corresponding control groups on MMP3 and MMP7 expression. f The expression of p38, p-p38, MAPK, p-MAPK, PI3K, p-PI3K, AKT and p-AKT in PANC-1 and BxPC-3 cells after TPPP overexpression

    Techniques Used: Plasmid Preparation, Injection, Microscopy, Mouse Assay, Expressing, Over Expression

    5) Product Images from "Netrin-1 improves adipose-derived stem cell proliferation, migration, and treatment effect in type 2 diabetic mice with sciatic denervation"

    Article Title: Netrin-1 improves adipose-derived stem cell proliferation, migration, and treatment effect in type 2 diabetic mice with sciatic denervation

    Journal: Stem Cell Research & Therapy

    doi: 10.1186/s13287-018-1020-0

    Signaling pathway of Netrin-1 on ADSCs in vitro and in vivo. a Western blotting of P-AKT, AKT, P-PI3K, PI3K, P-P38, P38, P-eNOS, eNOS, P-NF-κB, NF-κB, JNK, and ERK1/2 in vitro. b Statistical analysis demonstrated that the phosphorylation of the signaling pathway of PI3K/AKT/eNOS/P-38/NF-κB was highly upregulated in the N-ADSCs group as compared to the ADSCs group in vitro, but not JNK or ERK1/2. c Western blotting of P-AKT, AKT, P-PI3K, PI3K, P-P38, P38, P-eNOS, eNOS, P-NF-κB, NF-κB, JNK, and ERK1/2 in vivo. d Statistical analysis demonstrated that the phosphorylation of the signaling pathway of PI3K/AKT/eNOS/P-38/NF-κB was highly upregulated in the N-ADSCs group as compared to the ADSCs group in vivo, but not JNK or ERK1/2; * P
    Figure Legend Snippet: Signaling pathway of Netrin-1 on ADSCs in vitro and in vivo. a Western blotting of P-AKT, AKT, P-PI3K, PI3K, P-P38, P38, P-eNOS, eNOS, P-NF-κB, NF-κB, JNK, and ERK1/2 in vitro. b Statistical analysis demonstrated that the phosphorylation of the signaling pathway of PI3K/AKT/eNOS/P-38/NF-κB was highly upregulated in the N-ADSCs group as compared to the ADSCs group in vitro, but not JNK or ERK1/2. c Western blotting of P-AKT, AKT, P-PI3K, PI3K, P-P38, P38, P-eNOS, eNOS, P-NF-κB, NF-κB, JNK, and ERK1/2 in vivo. d Statistical analysis demonstrated that the phosphorylation of the signaling pathway of PI3K/AKT/eNOS/P-38/NF-κB was highly upregulated in the N-ADSCs group as compared to the ADSCs group in vivo, but not JNK or ERK1/2; * P

    Techniques Used: In Vitro, In Vivo, Western Blot

    6) Product Images from "Focal Adhesion Kinase Functions as an Akt Downstream Target in Migration of Colorectal Cancer Cells 1"

    Article Title: Focal Adhesion Kinase Functions as an Akt Downstream Target in Migration of Colorectal Cancer Cells 1

    Journal: Translational Oncology

    doi:

    FAK, Src, and Akt play roles in colorectal cancer cell invasion. (A) Indicated cells were starved and plated at the same densities on Matrigel-coated culture insert membranes and subsequently let penetrate through toward serum in the culture medium for 36 hours. Then, the invaded cells were fixed, stained, and counted. (B) Histogram comparing the resulting counts of the invaded uninfected SW620 cells, SW620/GIPZ, DLD/GIPZ, and SW620shFAK or DLDshFAK#3 or #5, respectively. (C) Counts of invaded SW620 or DLD-1 cells treated with a vehicle (DMSO), AktIV inhibitor, Src inhibitor SU6656, or PI3 kinase inhibitor wortmannin. Data in histograms in panels B and C show statistical differences ( n = 3 for each) in the penetrated cell counts of either shFAK clones or the cells treated with the given inhibitors normalized to their relevant controls (i.e., either GIPZ- or DMSO-treated). * P
    Figure Legend Snippet: FAK, Src, and Akt play roles in colorectal cancer cell invasion. (A) Indicated cells were starved and plated at the same densities on Matrigel-coated culture insert membranes and subsequently let penetrate through toward serum in the culture medium for 36 hours. Then, the invaded cells were fixed, stained, and counted. (B) Histogram comparing the resulting counts of the invaded uninfected SW620 cells, SW620/GIPZ, DLD/GIPZ, and SW620shFAK or DLDshFAK#3 or #5, respectively. (C) Counts of invaded SW620 or DLD-1 cells treated with a vehicle (DMSO), AktIV inhibitor, Src inhibitor SU6656, or PI3 kinase inhibitor wortmannin. Data in histograms in panels B and C show statistical differences ( n = 3 for each) in the penetrated cell counts of either shFAK clones or the cells treated with the given inhibitors normalized to their relevant controls (i.e., either GIPZ- or DMSO-treated). * P

    Techniques Used: Staining, Clone Assay

    FAK functions downstream of Akt. (A) Western blots comparing protein expression levels of FAK and FAK phosphorylated at Y397 (P-FAK) or at Y925 (Y925-FAK) in DLD-1 cells transfected with control nonsilencing siRNA or with siRNA specific to PTEN. (B) Phosphorylation of FAK, Akt, and Src in DLD-1 cells treated with inhibitors. Besides antibodies against FAK phosphorylated at its Y397 and Y925, also antibodies against Akt and Src phosphorylated at S473 and Y416, respectively, were used. For experiments displayed in panels C to E, DLD/GIPZ or DLDshFAK#5 cells were infected with the adenoviral construct encoding inducible iAkt. Subsequently, the cells were scratched and incubated in the absence or presence of iAkt-activating 4-hydroxytamoxifen (HXT) or the Src specific inhibitor SU6656 as indicated. (C) Western blot showing protein levels of endogenous (endo) and ectopic (ecto) Akt and Akt phosphorylation; the blots were further probed with anti-FAK and anti-phospho-FAK specific antibodies. α-Tubulin was used as a loading control. Also shown are microscopic images of DLD/GIPZ control cells (D) and DLDshFAK#5 cells (E) after 3 days of migration under the assigned conditions. All pictures represent two (A) or three (B–E) independent sets of experiments.
    Figure Legend Snippet: FAK functions downstream of Akt. (A) Western blots comparing protein expression levels of FAK and FAK phosphorylated at Y397 (P-FAK) or at Y925 (Y925-FAK) in DLD-1 cells transfected with control nonsilencing siRNA or with siRNA specific to PTEN. (B) Phosphorylation of FAK, Akt, and Src in DLD-1 cells treated with inhibitors. Besides antibodies against FAK phosphorylated at its Y397 and Y925, also antibodies against Akt and Src phosphorylated at S473 and Y416, respectively, were used. For experiments displayed in panels C to E, DLD/GIPZ or DLDshFAK#5 cells were infected with the adenoviral construct encoding inducible iAkt. Subsequently, the cells were scratched and incubated in the absence or presence of iAkt-activating 4-hydroxytamoxifen (HXT) or the Src specific inhibitor SU6656 as indicated. (C) Western blot showing protein levels of endogenous (endo) and ectopic (ecto) Akt and Akt phosphorylation; the blots were further probed with anti-FAK and anti-phospho-FAK specific antibodies. α-Tubulin was used as a loading control. Also shown are microscopic images of DLD/GIPZ control cells (D) and DLDshFAK#5 cells (E) after 3 days of migration under the assigned conditions. All pictures represent two (A) or three (B–E) independent sets of experiments.

    Techniques Used: Western Blot, Expressing, Transfection, Infection, Construct, Incubation, Migration

    FAK is in complex with Src and Akt. Lysates of DLD/GIPZ cells or DLDshFAK#3 and #5 were immunoprecipitated with antibodies against FAK, Src, and Akt (IP column on the left) and probed for FAK, Src, or Akt on Western blots (WB column on the right). In the column denoted LB, a lysis buffer without cell lysate was precipitated; in the column denoted lys, 10% of the total cell lysate of the DLD/GIPZ cells were loaded. Staining with the anti-Akt and anti-Src antibodies was performed sequentially on the same blot; therefore, the residual Akt signal from the first detection is still visible on the membrane reprobed with the antibody against Src (first panel from the bottom). The asterisk indicates heavy chains of immunoglobulins. The collage represents two independent experiments.
    Figure Legend Snippet: FAK is in complex with Src and Akt. Lysates of DLD/GIPZ cells or DLDshFAK#3 and #5 were immunoprecipitated with antibodies against FAK, Src, and Akt (IP column on the left) and probed for FAK, Src, or Akt on Western blots (WB column on the right). In the column denoted LB, a lysis buffer without cell lysate was precipitated; in the column denoted lys, 10% of the total cell lysate of the DLD/GIPZ cells were loaded. Staining with the anti-Akt and anti-Src antibodies was performed sequentially on the same blot; therefore, the residual Akt signal from the first detection is still visible on the membrane reprobed with the antibody against Src (first panel from the bottom). The asterisk indicates heavy chains of immunoglobulins. The collage represents two independent experiments.

    Techniques Used: Immunoprecipitation, Western Blot, Lysis, Staining

    MMP-9 enzymatic activity is attenuated in the absence of FAK in colorectal cancer cells. Conditioned culture media of different cell lines and SW620 clones were tested for activity of MMP-9 in gelatin zymography enzymatic assays. MMP-2 activity was included as a loading control because it never changed its level under any conditions. (A) Comparison of MMP activities in the indicated cells lines. (B) Zymography of conditional media of SW620/GIPZ versus SW620shFAK#5 cells incubated in the absence or presence of Akt, Src, or PI3 kinase inhibitors. In the statistical analysis of the densitometric data provided ( n = 3 for each, * P
    Figure Legend Snippet: MMP-9 enzymatic activity is attenuated in the absence of FAK in colorectal cancer cells. Conditioned culture media of different cell lines and SW620 clones were tested for activity of MMP-9 in gelatin zymography enzymatic assays. MMP-2 activity was included as a loading control because it never changed its level under any conditions. (A) Comparison of MMP activities in the indicated cells lines. (B) Zymography of conditional media of SW620/GIPZ versus SW620shFAK#5 cells incubated in the absence or presence of Akt, Src, or PI3 kinase inhibitors. In the statistical analysis of the densitometric data provided ( n = 3 for each, * P

    Techniques Used: Activity Assay, Clone Assay, Zymography, Incubation

    7) Product Images from "Thyrotropin Regulates eNOS Expression in the Endothelium by PGRN Through Akt Pathway"

    Article Title: Thyrotropin Regulates eNOS Expression in the Endothelium by PGRN Through Akt Pathway

    Journal: Frontiers in Endocrinology

    doi: 10.3389/fendo.2018.00353

    Role of Akt in the induction by TSH of eNOS in HUVECs. (A) Protein expression of Akt in HUVECs stimulated by different concentrations of TSH (0, 0.1, 1, 10, and 100 mIU/ml) for 24 h; (B) Inhibition of Akt: HUVECs were pretreated with 1 μM of MK-2206 for 6 h or not, and then together with or without TSH (10 mIU/ml) for 24 h. Data were obtained from three separate experiments. HUVECs without stimulating with TSH (0 mIU/ml) served as control; M represented MK-2206; * P
    Figure Legend Snippet: Role of Akt in the induction by TSH of eNOS in HUVECs. (A) Protein expression of Akt in HUVECs stimulated by different concentrations of TSH (0, 0.1, 1, 10, and 100 mIU/ml) for 24 h; (B) Inhibition of Akt: HUVECs were pretreated with 1 μM of MK-2206 for 6 h or not, and then together with or without TSH (10 mIU/ml) for 24 h. Data were obtained from three separate experiments. HUVECs without stimulating with TSH (0 mIU/ml) served as control; M represented MK-2206; * P

    Techniques Used: Expressing, Inhibition

    Proposed mechanism of endothelial dysfunction induced by TSH. TSH up-regulated eNOS expression in HUVECs by PGRN through Akt pathway. Reduction in NO production and increase in superoxide anion indicated uncoupled eNOS.
    Figure Legend Snippet: Proposed mechanism of endothelial dysfunction induced by TSH. TSH up-regulated eNOS expression in HUVECs by PGRN through Akt pathway. Reduction in NO production and increase in superoxide anion indicated uncoupled eNOS.

    Techniques Used: Expressing

    8) Product Images from "Long Non-Coding RNA (lncRNA) Urothelial Carcinoma-Associated 1 (UCA1) Enhances Tamoxifen Resistance in Breast Cancer Cells via Inhibiting mTOR Signaling Pathway"

    Article Title: Long Non-Coding RNA (lncRNA) Urothelial Carcinoma-Associated 1 (UCA1) Enhances Tamoxifen Resistance in Breast Cancer Cells via Inhibiting mTOR Signaling Pathway

    Journal: Medical Science Monitor : International Medical Journal of Experimental and Clinical Research

    doi: 10.12659/MSM.900689

    UCA1 activates mTOR signaling pathway in breast cancer cells. ( A–D ) Western blot analysis images ( A, B ) and quantitation of the relative gray scale ( C, D ) of the expression of p-AKT and p-mTOR in MCF-7, LCC2 and LCC9 cells ( A, C ) and in LCC2 and LCC9 cells with or without transfection of UCA1 siRNA ( B, D ). ** p
    Figure Legend Snippet: UCA1 activates mTOR signaling pathway in breast cancer cells. ( A–D ) Western blot analysis images ( A, B ) and quantitation of the relative gray scale ( C, D ) of the expression of p-AKT and p-mTOR in MCF-7, LCC2 and LCC9 cells ( A, C ) and in LCC2 and LCC9 cells with or without transfection of UCA1 siRNA ( B, D ). ** p

    Techniques Used: Western Blot, Quantitation Assay, Expressing, Transfection

    9) Product Images from "Resveratrol decreases fructose-induced oxidative stress, mediated by NADPH oxidase via an AMPK-dependent mechanism"

    Article Title: Resveratrol decreases fructose-induced oxidative stress, mediated by NADPH oxidase via an AMPK-dependent mechanism

    Journal: British Journal of Pharmacology

    doi: 10.1111/bph.12648

    Resveratrol increases the activity of the AMPK-Akt-nNOS pathway in the NTS of rats with fructose-induced hypertension. (A–D) Immunoblot showing the levels of P-AMPK T172 , P-Akt S473 , P-nNOS S1416 and P-eNOS S1177 after treatment with resveratrol.
    Figure Legend Snippet: Resveratrol increases the activity of the AMPK-Akt-nNOS pathway in the NTS of rats with fructose-induced hypertension. (A–D) Immunoblot showing the levels of P-AMPK T172 , P-Akt S473 , P-nNOS S1416 and P-eNOS S1177 after treatment with resveratrol.

    Techniques Used: Activity Assay

    10) Product Images from "TRIB3 supports breast cancer stemness by suppressing FOXO1 degradation and enhancing SOX2 transcription"

    Article Title: TRIB3 supports breast cancer stemness by suppressing FOXO1 degradation and enhancing SOX2 transcription

    Journal: Nature Communications

    doi: 10.1038/s41467-019-13700-6

    TRIB3 abrogates the AKT-FOXO1 interaction. a Supervised clustering of MCF7 cells transfected with CTRL-shRNA or TRIB3-shRNA using the log2-transformed values for genes in the FOXO1 upstream pathway, including AMPK, ERK, PI3K, p38, and JNK clustered genes expressed in all samples. Each column represents a separate case. Z -scores from IPA depicting the subnetwork gene expression differences between CTRL-shRNA and TRIB3-shRNA cases. The Z -score heat map depicts the five FOXO1 upstream subnetworks. Each row represents the data for the subnetwork indicated in the right margin. b , c TRIB3 inhibited the activity of AKT1 in BCCs. The indicated stable expression cell extracts were prepared and the levels of the indicated proteins were detected by immunoblotting. d , e The effects of the AKT1 agonist or antagonist for TRIB3-FOXO1-SOX2 axis in BCCs. The indicated cells were treated with the AKT1 agonist SC79 or the antagonist MK2206 for 24 h. Cell extracts were prepared and the levels of the indicated proteins were detected by immunoblotting. f TRIB3 inhibited the AKT1-FOXO1 interaction by binding to AKT1. HMLE cell extracts were IP with an anti-AKT1 Ab and blotted with an anti-TRIB3 or anti-FOXO1 Ab in the presence of the indicated concentration of the TRIB3-GST protein. Data are shown as the mean ± SEM; P > 0.05 was considered not significant (NS); * P
    Figure Legend Snippet: TRIB3 abrogates the AKT-FOXO1 interaction. a Supervised clustering of MCF7 cells transfected with CTRL-shRNA or TRIB3-shRNA using the log2-transformed values for genes in the FOXO1 upstream pathway, including AMPK, ERK, PI3K, p38, and JNK clustered genes expressed in all samples. Each column represents a separate case. Z -scores from IPA depicting the subnetwork gene expression differences between CTRL-shRNA and TRIB3-shRNA cases. The Z -score heat map depicts the five FOXO1 upstream subnetworks. Each row represents the data for the subnetwork indicated in the right margin. b , c TRIB3 inhibited the activity of AKT1 in BCCs. The indicated stable expression cell extracts were prepared and the levels of the indicated proteins were detected by immunoblotting. d , e The effects of the AKT1 agonist or antagonist for TRIB3-FOXO1-SOX2 axis in BCCs. The indicated cells were treated with the AKT1 agonist SC79 or the antagonist MK2206 for 24 h. Cell extracts were prepared and the levels of the indicated proteins were detected by immunoblotting. f TRIB3 inhibited the AKT1-FOXO1 interaction by binding to AKT1. HMLE cell extracts were IP with an anti-AKT1 Ab and blotted with an anti-TRIB3 or anti-FOXO1 Ab in the presence of the indicated concentration of the TRIB3-GST protein. Data are shown as the mean ± SEM; P > 0.05 was considered not significant (NS); * P

    Techniques Used: Transfection, shRNA, Transformation Assay, Indirect Immunoperoxidase Assay, Expressing, Activity Assay, Binding Assay, Concentration Assay

    11) Product Images from "Tongxinluo Protects against Hypertensive Kidney Injury in Spontaneously-Hypertensive Rats by Inhibiting Oxidative Stress and Activating Forkhead Box O1 Signaling"

    Article Title: Tongxinluo Protects against Hypertensive Kidney Injury in Spontaneously-Hypertensive Rats by Inhibiting Oxidative Stress and Activating Forkhead Box O1 Signaling

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0145130

    Tongxinluo (TXL) altered forkhead box O1 (FoxO1) signaling in spontaneously hypertensive rat (SHR) kidneys. Western blot analysis of (A) FoxO1 and phospho-FoxO1, (B) ERK1/2 and phospho-ERK1/2, (C) p38 and phospho-p38, (D) PI3K and phosphor-PI3K, and (E) Akt and phosphor-Akt (F) AMPK and phosphor-AMPK, and (G)SIRT1 after 12 weeks of TXL treatment. Data are mean±SEM; n = 10 rats per group, # P
    Figure Legend Snippet: Tongxinluo (TXL) altered forkhead box O1 (FoxO1) signaling in spontaneously hypertensive rat (SHR) kidneys. Western blot analysis of (A) FoxO1 and phospho-FoxO1, (B) ERK1/2 and phospho-ERK1/2, (C) p38 and phospho-p38, (D) PI3K and phosphor-PI3K, and (E) Akt and phosphor-Akt (F) AMPK and phosphor-AMPK, and (G)SIRT1 after 12 weeks of TXL treatment. Data are mean±SEM; n = 10 rats per group, # P

    Techniques Used: Western Blot

    12) Product Images from "Concomitant Mycobacterium tuberculosis infection promotes lung tumor growth through enhancing Treg development"

    Article Title: Concomitant Mycobacterium tuberculosis infection promotes lung tumor growth through enhancing Treg development

    Journal: Oncology Reports

    doi: 10.3892/or.2017.5733

    mTORC1 activation contributes to the PD-L1 expression by H37Rv infection. (A) H37Rv stimulated macrophages were collected and processed for immunoblotting. (B) Quantification of PD-L1, phophorylated S6K and Akt expression in (A). All experiments are representative of three similar results. Statistical differences between groups are indicated by the P-values. *P
    Figure Legend Snippet: mTORC1 activation contributes to the PD-L1 expression by H37Rv infection. (A) H37Rv stimulated macrophages were collected and processed for immunoblotting. (B) Quantification of PD-L1, phophorylated S6K and Akt expression in (A). All experiments are representative of three similar results. Statistical differences between groups are indicated by the P-values. *P

    Techniques Used: Activation Assay, Expressing, Infection

    13) Product Images from "SH2B1 promotes NSCLC cell proliferation through PI3K/Akt/mTOR signaling cascade"

    Article Title: SH2B1 promotes NSCLC cell proliferation through PI3K/Akt/mTOR signaling cascade

    Journal: Cancer Cell International

    doi: 10.1186/s12935-018-0632-x

    SH2B1 regulates NSCLC cell proliferation through Akt/mTOR pathway in vitro. a , b The effect of SH2B1 on Akt/mTOR signaling. a The protein levels of SH2B1, p-Akt, p-mTOR and PTEN in different panels of A549 and H1299 cells were assayed by Western blotting. b The protein levels of Akt/mTOR pathway targets (p-Akt, p-mTOR and PTEN) in different panels of H1299, which were subjected or not subjected to a Akt inhibitor, 10 μm/l deguelin for 24H, were assayed by Western blotting. Experiments were repeated three times and representative pictures are shown for a and b . GAPDH is used as an internal control. c CCK8 assay indicated that deguelin impaired the effect of SH2B1 on cell proliferation. Results are presented as mean ± SD
    Figure Legend Snippet: SH2B1 regulates NSCLC cell proliferation through Akt/mTOR pathway in vitro. a , b The effect of SH2B1 on Akt/mTOR signaling. a The protein levels of SH2B1, p-Akt, p-mTOR and PTEN in different panels of A549 and H1299 cells were assayed by Western blotting. b The protein levels of Akt/mTOR pathway targets (p-Akt, p-mTOR and PTEN) in different panels of H1299, which were subjected or not subjected to a Akt inhibitor, 10 μm/l deguelin for 24H, were assayed by Western blotting. Experiments were repeated three times and representative pictures are shown for a and b . GAPDH is used as an internal control. c CCK8 assay indicated that deguelin impaired the effect of SH2B1 on cell proliferation. Results are presented as mean ± SD

    Techniques Used: In Vitro, Western Blot, CCK-8 Assay

    Clinical relevance of SH2B1 and its targets in NSCLC. a Representative expression levels of SH2B1, p-Akt (Ser 473), p-mTOR (Ser 2448) and PTEN in NSCLC by IHC staining. Scale bars, 10 μm. b Percentages of specimens showing high or low SH2B1 expression relative to levels of p-Akt (Ser 473), p-mTOR (Ser 2448) and PTEN (all P
    Figure Legend Snippet: Clinical relevance of SH2B1 and its targets in NSCLC. a Representative expression levels of SH2B1, p-Akt (Ser 473), p-mTOR (Ser 2448) and PTEN in NSCLC by IHC staining. Scale bars, 10 μm. b Percentages of specimens showing high or low SH2B1 expression relative to levels of p-Akt (Ser 473), p-mTOR (Ser 2448) and PTEN (all P

    Techniques Used: Expressing, Immunohistochemistry, Staining

    14) Product Images from "Activation of GABAB receptors inhibits protein kinase B /Glycogen Synthase Kinase 3 signaling"

    Article Title: Activation of GABAB receptors inhibits protein kinase B /Glycogen Synthase Kinase 3 signaling

    Journal: Molecular Brain

    doi: 10.1186/1756-6606-5-41

    Activation of GABA B receptors elevates Akt (Thr-308) phosphorylation in HEK293T cells expressing GABA B receptors, which can be blocked with pretreatment of PI3K inhibitor Wortmannin. A. Western blot analysis of phosphorylated Akt (Thr-308) or Akt (Ser-473) levels in extract prepared from HEK 293T cells transfected with GABA B receptor in the presence of GABA B receptor antagonist and/or agonist. Akt was used as a loading control. B-C. Densitometric analysis of phosphorylated Akt (Thr-308) (B) and Akt (Ser-473) (C). The intensity of phospho-Akt was quantified by densitometry (software: Image J, NIH). D. Western blot analysis of phosphorylated GSK-3α/β (Ser-21/Ser-9) or GSK-3α/β levels in extract prepared from HEK293T cells transfected with GABA B receptor pretreated with/without Wortmannin (100 nM, 24 h) in the presence or absence of GABA B receptor agonist SKF97541. E. Densitometric analysis of phosphorylated GSK-3α/β (Ser-21/Ser-9). The intensity of phosphor- GSK-3α/β (Ser-21/Ser-9) was quantified by densitometry (software: Image J, NIH). Data were analyzed by one-way or two-way ANOVA (* P
    Figure Legend Snippet: Activation of GABA B receptors elevates Akt (Thr-308) phosphorylation in HEK293T cells expressing GABA B receptors, which can be blocked with pretreatment of PI3K inhibitor Wortmannin. A. Western blot analysis of phosphorylated Akt (Thr-308) or Akt (Ser-473) levels in extract prepared from HEK 293T cells transfected with GABA B receptor in the presence of GABA B receptor antagonist and/or agonist. Akt was used as a loading control. B-C. Densitometric analysis of phosphorylated Akt (Thr-308) (B) and Akt (Ser-473) (C). The intensity of phospho-Akt was quantified by densitometry (software: Image J, NIH). D. Western blot analysis of phosphorylated GSK-3α/β (Ser-21/Ser-9) or GSK-3α/β levels in extract prepared from HEK293T cells transfected with GABA B receptor pretreated with/without Wortmannin (100 nM, 24 h) in the presence or absence of GABA B receptor agonist SKF97541. E. Densitometric analysis of phosphorylated GSK-3α/β (Ser-21/Ser-9). The intensity of phosphor- GSK-3α/β (Ser-21/Ser-9) was quantified by densitometry (software: Image J, NIH). Data were analyzed by one-way or two-way ANOVA (* P

    Techniques Used: Activation Assay, Expressing, Western Blot, Transfection, Software

    Schematic model of GABA B receptor mediated GSK-3 signaling. Activation of GABA B receptors enhances the phosphorylation of Akt and GSK-3α/β, which inactivates GSK-3 signaling. Activation of D2 receptors has the opposite effect as previously reported [ 37 ].
    Figure Legend Snippet: Schematic model of GABA B receptor mediated GSK-3 signaling. Activation of GABA B receptors enhances the phosphorylation of Akt and GSK-3α/β, which inactivates GSK-3 signaling. Activation of D2 receptors has the opposite effect as previously reported [ 37 ].

    Techniques Used: Activation Assay

    15) Product Images from "Palmitic Acid Promotes Virus Replication in Fish Cell by Modulating Autophagy Flux and TBK1-IRF3/7 Pathway"

    Article Title: Palmitic Acid Promotes Virus Replication in Fish Cell by Modulating Autophagy Flux and TBK1-IRF3/7 Pathway

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2020.01764

    Palmitic acid impacted autophagic flux in GS cells. (A) Accumulation of GFP-LC3 (green) were observed after palmitic acid treatment. GS cells were transfected with C1-EGFP-LC3 plasmid, then incubated with or without 0.4 mM palmitic acid. Cells were fixed with 4% polyformaldehyde and staining with Hoechst33342. Fluorescence was observed under the fluorescence microscope (Zeiss). (B) Representative image of phospho-Akt (Ser473) [p-Akt (ser473)], and phospho-mTOR (p-mTOR) detection was performed to verify Akt and mTOR inhibition by 1% BSA or palmitic acid (0.4 mM) treatment. β-tubulin was used as the internal control. (C) The expression levels of LC3, and p62 in cell lysates were evaluated after the incubation of 1% BSA or palmitic acid (0.4 mM) for 24 h. Western blot assay was carried out, and β-tubulin was used as the internal control. (D) GS cells were incubated with 1% BSA, 0.2 mM palmitic acid, or 0.4 mM palmitic acid for 24 h, and CQ was added for the last 4 h treatment. Western blot assay was carried out to detect the LC3-II and β-tubulin levels in cell lysate. Band intensity was calculated using Image J software, and the LC3-II protein level was presented by the ratio of LC3-II/β-tubulin. (E) Autophagic flux was measured. Briefly, after measuring the LC3-II protein level (LC3-II/β-tubulin) in each group, the histogram was made referring to the ratio of LC3-II level in cells treated with CQ to that of untreated cells. Setting the ratio in 1% BSA treated group as 1-fold. The data are represented as mean ± SD, and the statistical significances were determined with Student's t -test, n = 3. The significance level was defined as * p
    Figure Legend Snippet: Palmitic acid impacted autophagic flux in GS cells. (A) Accumulation of GFP-LC3 (green) were observed after palmitic acid treatment. GS cells were transfected with C1-EGFP-LC3 plasmid, then incubated with or without 0.4 mM palmitic acid. Cells were fixed with 4% polyformaldehyde and staining with Hoechst33342. Fluorescence was observed under the fluorescence microscope (Zeiss). (B) Representative image of phospho-Akt (Ser473) [p-Akt (ser473)], and phospho-mTOR (p-mTOR) detection was performed to verify Akt and mTOR inhibition by 1% BSA or palmitic acid (0.4 mM) treatment. β-tubulin was used as the internal control. (C) The expression levels of LC3, and p62 in cell lysates were evaluated after the incubation of 1% BSA or palmitic acid (0.4 mM) for 24 h. Western blot assay was carried out, and β-tubulin was used as the internal control. (D) GS cells were incubated with 1% BSA, 0.2 mM palmitic acid, or 0.4 mM palmitic acid for 24 h, and CQ was added for the last 4 h treatment. Western blot assay was carried out to detect the LC3-II and β-tubulin levels in cell lysate. Band intensity was calculated using Image J software, and the LC3-II protein level was presented by the ratio of LC3-II/β-tubulin. (E) Autophagic flux was measured. Briefly, after measuring the LC3-II protein level (LC3-II/β-tubulin) in each group, the histogram was made referring to the ratio of LC3-II level in cells treated with CQ to that of untreated cells. Setting the ratio in 1% BSA treated group as 1-fold. The data are represented as mean ± SD, and the statistical significances were determined with Student's t -test, n = 3. The significance level was defined as * p

    Techniques Used: Transfection, Plasmid Preparation, Incubation, Staining, Fluorescence, Microscopy, Inhibition, Expressing, Western Blot, Software

    16) Product Images from "Overexpression of retinoblastoma-binding protein 4 contributes to the radiosensitivity of AGS gastric cancer cells via phosphoinositide3-kinase/protein kinase B pathway suppression"

    Article Title: Overexpression of retinoblastoma-binding protein 4 contributes to the radiosensitivity of AGS gastric cancer cells via phosphoinositide3-kinase/protein kinase B pathway suppression

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2018.9153

    RbAp48 in combination with radiation inhibits the PI3K/Akt pathway. Western blot analysis was performed to assess the expression levels of (A) p-PI3K, PI3K, (B) p-Akt and Akt in AGS cells. **P
    Figure Legend Snippet: RbAp48 in combination with radiation inhibits the PI3K/Akt pathway. Western blot analysis was performed to assess the expression levels of (A) p-PI3K, PI3K, (B) p-Akt and Akt in AGS cells. **P

    Techniques Used: Western Blot, Expressing

    si-RbAp48 represses cell apoptosis, and RbAp48 in combination with radiation promotes cell apoptosis via PI3K/Akt pathway inhibition. (A) Flow cytometry analysis was performed and (B) the percentage of apoptotic cells was calculated. IGF-1 was used as a PI3K/Akt pathway agonist. *P
    Figure Legend Snippet: si-RbAp48 represses cell apoptosis, and RbAp48 in combination with radiation promotes cell apoptosis via PI3K/Akt pathway inhibition. (A) Flow cytometry analysis was performed and (B) the percentage of apoptotic cells was calculated. IGF-1 was used as a PI3K/Akt pathway agonist. *P

    Techniques Used: Inhibition, Flow Cytometry, Cytometry

    17) Product Images from "Silencing Livin improved the sensitivity of colon cancer cells to 5-fluorouracil by regulating crosstalk between apoptosis and autophagy"

    Article Title: Silencing Livin improved the sensitivity of colon cancer cells to 5-fluorouracil by regulating crosstalk between apoptosis and autophagy

    Journal: Oncology Letters

    doi: 10.3892/ol.2018.8282

    Inhibition of Bcl-2 and the Akt signaling pathway were involved in silenced-Livin-induced cell death. (A) STRING analysis revealed Livin and associated protein-protein interactions (confidence mode; http://string-db.org/ ). Within this cluster, Bcl-2 and Akt, which were located in the key nodes and mutually interacted, were selected for further analysis. (B) HCT116 and SW620 cells were incubated with 20 µM 5-FU for 24 h, harvested and subjected to western blot analysis to detect the protein expression level of Bcl-2, p-Akt and T-Akt from the control, NC and shLivin groups. Images are representative of three independent experiments. Histograms represent p-Akt, T-Akt and Bcl-2 protein expression levels quantified by western blotting and the optical analysis software ImageJ in (C) HCT116 and (D) SW620 cells (*P
    Figure Legend Snippet: Inhibition of Bcl-2 and the Akt signaling pathway were involved in silenced-Livin-induced cell death. (A) STRING analysis revealed Livin and associated protein-protein interactions (confidence mode; http://string-db.org/ ). Within this cluster, Bcl-2 and Akt, which were located in the key nodes and mutually interacted, were selected for further analysis. (B) HCT116 and SW620 cells were incubated with 20 µM 5-FU for 24 h, harvested and subjected to western blot analysis to detect the protein expression level of Bcl-2, p-Akt and T-Akt from the control, NC and shLivin groups. Images are representative of three independent experiments. Histograms represent p-Akt, T-Akt and Bcl-2 protein expression levels quantified by western blotting and the optical analysis software ImageJ in (C) HCT116 and (D) SW620 cells (*P

    Techniques Used: Inhibition, Incubation, Western Blot, Expressing, Software

    18) Product Images from "Luteolin attenuates doxorubicin-induced cardiotoxicity by modulating the PHLPP1/AKT/Bcl-2 signalling pathway"

    Article Title: Luteolin attenuates doxorubicin-induced cardiotoxicity by modulating the PHLPP1/AKT/Bcl-2 signalling pathway

    Journal: PeerJ

    doi: 10.7717/peerj.8845

    Chemicals-target gene network linking the protective effects of LUT against cardiotoxicity to potential signalling pathways and related protein expression. (A) Blue circles represent the enriched KEGG main pathway, and green rectangles represent the top putative target proteins. (B–D) Representative phlpp1 and GAPDH protein ratio. (E–G) p-AKT and AKT protein ratio. ∗ p
    Figure Legend Snippet: Chemicals-target gene network linking the protective effects of LUT against cardiotoxicity to potential signalling pathways and related protein expression. (A) Blue circles represent the enriched KEGG main pathway, and green rectangles represent the top putative target proteins. (B–D) Representative phlpp1 and GAPDH protein ratio. (E–G) p-AKT and AKT protein ratio. ∗ p

    Techniques Used: Expressing

    19) Product Images from "SH2B1 promotes NSCLC cell proliferation through PI3K/Akt/mTOR signaling cascade"

    Article Title: SH2B1 promotes NSCLC cell proliferation through PI3K/Akt/mTOR signaling cascade

    Journal: Cancer Cell International

    doi: 10.1186/s12935-018-0632-x

    SH2B1 regulates NSCLC cell proliferation through Akt/mTOR pathway in vitro. a , b The effect of SH2B1 on Akt/mTOR signaling. a The protein levels of SH2B1, p-Akt, p-mTOR and PTEN in different panels of A549 and H1299 cells were assayed by Western blotting. b The protein levels of Akt/mTOR pathway targets (p-Akt, p-mTOR and PTEN) in different panels of H1299, which were subjected or not subjected to a Akt inhibitor, 10 μm/l deguelin for 24H, were assayed by Western blotting. Experiments were repeated three times and representative pictures are shown for a and b . GAPDH is used as an internal control. c CCK8 assay indicated that deguelin impaired the effect of SH2B1 on cell proliferation. Results are presented as mean ± SD
    Figure Legend Snippet: SH2B1 regulates NSCLC cell proliferation through Akt/mTOR pathway in vitro. a , b The effect of SH2B1 on Akt/mTOR signaling. a The protein levels of SH2B1, p-Akt, p-mTOR and PTEN in different panels of A549 and H1299 cells were assayed by Western blotting. b The protein levels of Akt/mTOR pathway targets (p-Akt, p-mTOR and PTEN) in different panels of H1299, which were subjected or not subjected to a Akt inhibitor, 10 μm/l deguelin for 24H, were assayed by Western blotting. Experiments were repeated three times and representative pictures are shown for a and b . GAPDH is used as an internal control. c CCK8 assay indicated that deguelin impaired the effect of SH2B1 on cell proliferation. Results are presented as mean ± SD

    Techniques Used: In Vitro, Western Blot, CCK-8 Assay

    Clinical relevance of SH2B1 and its targets in NSCLC. a Representative expression levels of SH2B1, p-Akt (Ser 473), p-mTOR (Ser 2448) and PTEN in NSCLC by IHC staining. Scale bars, 10 μm. b Percentages of specimens showing high or low SH2B1 expression relative to levels of p-Akt (Ser 473), p-mTOR (Ser 2448) and PTEN (all P
    Figure Legend Snippet: Clinical relevance of SH2B1 and its targets in NSCLC. a Representative expression levels of SH2B1, p-Akt (Ser 473), p-mTOR (Ser 2448) and PTEN in NSCLC by IHC staining. Scale bars, 10 μm. b Percentages of specimens showing high or low SH2B1 expression relative to levels of p-Akt (Ser 473), p-mTOR (Ser 2448) and PTEN (all P

    Techniques Used: Expressing, Immunohistochemistry, Staining

    20) Product Images from "Overexpression of retinoblastoma-binding protein 4 contributes to the radiosensitivity of AGS gastric cancer cells via phosphoinositide3-kinase/protein kinase B pathway suppression"

    Article Title: Overexpression of retinoblastoma-binding protein 4 contributes to the radiosensitivity of AGS gastric cancer cells via phosphoinositide3-kinase/protein kinase B pathway suppression

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2018.9153

    RbAp48 in combination with radiation inhibits the PI3K/Akt pathway. Western blot analysis was performed to assess the expression levels of (A) p-PI3K, PI3K, (B) p-Akt and Akt in AGS cells. **P
    Figure Legend Snippet: RbAp48 in combination with radiation inhibits the PI3K/Akt pathway. Western blot analysis was performed to assess the expression levels of (A) p-PI3K, PI3K, (B) p-Akt and Akt in AGS cells. **P

    Techniques Used: Western Blot, Expressing

    si-RbAp48 represses cell apoptosis, and RbAp48 in combination with radiation promotes cell apoptosis via PI3K/Akt pathway inhibition. (A) Flow cytometry analysis was performed and (B) the percentage of apoptotic cells was calculated. IGF-1 was used as a PI3K/Akt pathway agonist. *P
    Figure Legend Snippet: si-RbAp48 represses cell apoptosis, and RbAp48 in combination with radiation promotes cell apoptosis via PI3K/Akt pathway inhibition. (A) Flow cytometry analysis was performed and (B) the percentage of apoptotic cells was calculated. IGF-1 was used as a PI3K/Akt pathway agonist. *P

    Techniques Used: Inhibition, Flow Cytometry, Cytometry

    21) Product Images from "Isoflurane reduces pain and inhibits apoptosis of myocardial cells through the phosphoinositide 3-kinase/protein kinase B signaling pathway in mice during cardiac surgery"

    Article Title: Isoflurane reduces pain and inhibits apoptosis of myocardial cells through the phosphoinositide 3-kinase/protein kinase B signaling pathway in mice during cardiac surgery

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2018.8642

    Expression levels of PI3K and AKT in myocardial cells isolated from mice with myocardial ischemia following heart bypass surgery and isoflurane treatment. Data are presented as the mean + standard error of the mean of three independent experiments. **P
    Figure Legend Snippet: Expression levels of PI3K and AKT in myocardial cells isolated from mice with myocardial ischemia following heart bypass surgery and isoflurane treatment. Data are presented as the mean + standard error of the mean of three independent experiments. **P

    Techniques Used: Expressing, Isolation, Mouse Assay

    22) Product Images from "Erzhi Pill® Protected Experimental Liver Injury Against Apoptosis via the PI3K/Akt/Raptor/Rictor Pathway"

    Article Title: Erzhi Pill® Protected Experimental Liver Injury Against Apoptosis via the PI3K/Akt/Raptor/Rictor Pathway

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2018.00283

    Western blotting of PI3K, Akt, and PTEN. (A) Western blotting of PI3K, Akt, p-Akt, and PTEN. (B) Quantitative analysis of Akt and p-Akt. (C) Ratio of p-Akt/Akt. (D) Quantitative analysis of PI3K. (E) Quantitative analysis of PTEN. Data are presented as mean ± SEM ( n = 3). ∗ p
    Figure Legend Snippet: Western blotting of PI3K, Akt, and PTEN. (A) Western blotting of PI3K, Akt, p-Akt, and PTEN. (B) Quantitative analysis of Akt and p-Akt. (C) Ratio of p-Akt/Akt. (D) Quantitative analysis of PI3K. (E) Quantitative analysis of PTEN. Data are presented as mean ± SEM ( n = 3). ∗ p

    Techniques Used: Western Blot

    23) Product Images from "Resibufogenin inhibits ovarian clear cell carcinoma (OCCC) growth in vivo, and migration of OCCC cells in vitro, by down-regulating the PI3K/AKT and actin cytoskeleton signaling pathways"

    Article Title: Resibufogenin inhibits ovarian clear cell carcinoma (OCCC) growth in vivo, and migration of OCCC cells in vitro, by down-regulating the PI3K/AKT and actin cytoskeleton signaling pathways

    Journal: American Journal of Translational Research

    doi:

    KEGG pathway enrichment analyses of genes that were found to be differentially expressed upon resibufogenin treatment. A. Distribution of TOV-21G transcriptome sequences among KEGG pathways. All 13 apoptosis and migration-related pathways are shown. LgP is the negative logarithm of P -value; larger LgP values indicate smaller P -values. B. The differentially expressed genes that participate in the PI3K-AKT signaling pathway mapped in KEGG. C. The differentially expressed genes that participate in actin cytoskeleton pathway mapped in KEGG. The tree displays the log-transformed value of average fold changes. Red indicates up-regulated gene expression levels, whereas blue indicates down-regulated expression levels of genes. D. The differentially expressed genes that participated in the actin cytoskeleton signaling pathway mapped in KEGG. E. The brief graph of the differentially expressed genes that participated in the actin cytoskeleton signaling pathway mapped in KEGG.
    Figure Legend Snippet: KEGG pathway enrichment analyses of genes that were found to be differentially expressed upon resibufogenin treatment. A. Distribution of TOV-21G transcriptome sequences among KEGG pathways. All 13 apoptosis and migration-related pathways are shown. LgP is the negative logarithm of P -value; larger LgP values indicate smaller P -values. B. The differentially expressed genes that participate in the PI3K-AKT signaling pathway mapped in KEGG. C. The differentially expressed genes that participate in actin cytoskeleton pathway mapped in KEGG. The tree displays the log-transformed value of average fold changes. Red indicates up-regulated gene expression levels, whereas blue indicates down-regulated expression levels of genes. D. The differentially expressed genes that participated in the actin cytoskeleton signaling pathway mapped in KEGG. E. The brief graph of the differentially expressed genes that participated in the actin cytoskeleton signaling pathway mapped in KEGG.

    Techniques Used: Migration, Transformation Assay, Expressing

    Resibufogenin down-regulates expression of genes in the PI3K/AKT and actin cytoskeleton pathways. ES-2 and TOV-21G cells were divided into 2 groups: the control group, and the resibufogenin-treated group (20 μM). qRT-PCR was performed to detect the mRNAs levels of PI3K (A and E), MDM2 (B and F), GRLF1 (C and G), Myosin-II (D and H), RTK (I and J), and SOS (K and L) after 12 hours of treatment. *P
    Figure Legend Snippet: Resibufogenin down-regulates expression of genes in the PI3K/AKT and actin cytoskeleton pathways. ES-2 and TOV-21G cells were divided into 2 groups: the control group, and the resibufogenin-treated group (20 μM). qRT-PCR was performed to detect the mRNAs levels of PI3K (A and E), MDM2 (B and F), GRLF1 (C and G), Myosin-II (D and H), RTK (I and J), and SOS (K and L) after 12 hours of treatment. *P

    Techniques Used: Expressing, Quantitative RT-PCR

    Resibufogenin inhibits proliferation and invasion of OCCC cells in vivo through the PI3K/AKT and actin cytoskeleton pathways. Representative photomicrographs showing immunohistochemically stained xenograft tumor sections (100 × and 400 × magnification) showing PI3K, AKT and MDM2 expression.
    Figure Legend Snippet: Resibufogenin inhibits proliferation and invasion of OCCC cells in vivo through the PI3K/AKT and actin cytoskeleton pathways. Representative photomicrographs showing immunohistochemically stained xenograft tumor sections (100 × and 400 × magnification) showing PI3K, AKT and MDM2 expression.

    Techniques Used: In Vivo, Staining, Expressing

    Resibufogenin down-regulates expression of proteins in the PI3K/AKT and actin cytoskeleton pathways in vitro . ES-2 and TOV-21G cells were divided into 2 groups: the control group, and the resibufogenin-treated group (20 μM). Western blotting assay was performed to detect the protein levels of PI3K (A and B), AKT (A), MDM2 (D), and Myosin-II (D) after 24 hours of treatment. The relative expression levels of the indicated proteins (relative to the expression level of actin) were quantitated using densitometry and are depicted bar graphically in (B, C, E, and F). *P
    Figure Legend Snippet: Resibufogenin down-regulates expression of proteins in the PI3K/AKT and actin cytoskeleton pathways in vitro . ES-2 and TOV-21G cells were divided into 2 groups: the control group, and the resibufogenin-treated group (20 μM). Western blotting assay was performed to detect the protein levels of PI3K (A and B), AKT (A), MDM2 (D), and Myosin-II (D) after 24 hours of treatment. The relative expression levels of the indicated proteins (relative to the expression level of actin) were quantitated using densitometry and are depicted bar graphically in (B, C, E, and F). *P

    Techniques Used: Expressing, In Vitro, Western Blot

    Schematic diagram of the proposed mechanism by which resibufogenin inhibits proliferation and invasion in OCCC cells. Resibufogenin decreases the levels of PI3K, AKT, MDM2, and Myosin in the PI3K/AKT and actin cytoskeleton signaling pathways.
    Figure Legend Snippet: Schematic diagram of the proposed mechanism by which resibufogenin inhibits proliferation and invasion in OCCC cells. Resibufogenin decreases the levels of PI3K, AKT, MDM2, and Myosin in the PI3K/AKT and actin cytoskeleton signaling pathways.

    Techniques Used:

    24) Product Images from "Netrin-1 improves adipose-derived stem cell proliferation, migration, and treatment effect in type 2 diabetic mice with sciatic denervation"

    Article Title: Netrin-1 improves adipose-derived stem cell proliferation, migration, and treatment effect in type 2 diabetic mice with sciatic denervation

    Journal: Stem Cell Research & Therapy

    doi: 10.1186/s13287-018-1020-0

    Signaling pathway of Netrin-1 on ADSCs in vitro and in vivo. a Western blotting of P-AKT, AKT, P-PI3K, PI3K, P-P38, P38, P-eNOS, eNOS, P-NF-κB, NF-κB, JNK, and ERK1/2 in vitro. b Statistical analysis demonstrated that the phosphorylation of the signaling pathway of PI3K/AKT/eNOS/P-38/NF-κB was highly upregulated in the N-ADSCs group as compared to the ADSCs group in vitro, but not JNK or ERK1/2. c Western blotting of P-AKT, AKT, P-PI3K, PI3K, P-P38, P38, P-eNOS, eNOS, P-NF-κB, NF-κB, JNK, and ERK1/2 in vivo. d Statistical analysis demonstrated that the phosphorylation of the signaling pathway of PI3K/AKT/eNOS/P-38/NF-κB was highly upregulated in the N-ADSCs group as compared to the ADSCs group in vivo, but not JNK or ERK1/2; * P
    Figure Legend Snippet: Signaling pathway of Netrin-1 on ADSCs in vitro and in vivo. a Western blotting of P-AKT, AKT, P-PI3K, PI3K, P-P38, P38, P-eNOS, eNOS, P-NF-κB, NF-κB, JNK, and ERK1/2 in vitro. b Statistical analysis demonstrated that the phosphorylation of the signaling pathway of PI3K/AKT/eNOS/P-38/NF-κB was highly upregulated in the N-ADSCs group as compared to the ADSCs group in vitro, but not JNK or ERK1/2. c Western blotting of P-AKT, AKT, P-PI3K, PI3K, P-P38, P38, P-eNOS, eNOS, P-NF-κB, NF-κB, JNK, and ERK1/2 in vivo. d Statistical analysis demonstrated that the phosphorylation of the signaling pathway of PI3K/AKT/eNOS/P-38/NF-κB was highly upregulated in the N-ADSCs group as compared to the ADSCs group in vivo, but not JNK or ERK1/2; * P

    Techniques Used: In Vitro, In Vivo, Western Blot

    25) Product Images from "Efficacy of combined icotinib and pemetrexed in EGFR mutant lung adenocarcinoma cell line xenografts"

    Article Title: Efficacy of combined icotinib and pemetrexed in EGFR mutant lung adenocarcinoma cell line xenografts

    Journal: Thoracic Cancer

    doi: 10.1111/1759-7714.12818

    Expression of thymidylate synthase (TS) and related EGFR signaling pathway proteins in tumor xenografts after the administration of different treatments ( n = 6 mice/group). Groups: control; Ico, icotinib; Ico‐Pem, sequential Ico followed by Pem; Ico + Pem, concurrent Ico and Pem; Pem, pemetrexed; Pem‐Ico, sequential Pem followed by Ico. ( a ) The effects of different combinations of Ico and Pem on TS expression and EGFR, AKT, and MAPK phosphorylation in tumor tissues was detected by Western blotting. The relative ( b ) TS ( c ) phospho‐EGFR, ( d ) phospho‐AKT, and ( e ) phospho‐MAPK expression levels. Data are shown as the mean ± standard deviation of triplicate measurements. P
    Figure Legend Snippet: Expression of thymidylate synthase (TS) and related EGFR signaling pathway proteins in tumor xenografts after the administration of different treatments ( n = 6 mice/group). Groups: control; Ico, icotinib; Ico‐Pem, sequential Ico followed by Pem; Ico + Pem, concurrent Ico and Pem; Pem, pemetrexed; Pem‐Ico, sequential Pem followed by Ico. ( a ) The effects of different combinations of Ico and Pem on TS expression and EGFR, AKT, and MAPK phosphorylation in tumor tissues was detected by Western blotting. The relative ( b ) TS ( c ) phospho‐EGFR, ( d ) phospho‐AKT, and ( e ) phospho‐MAPK expression levels. Data are shown as the mean ± standard deviation of triplicate measurements. P

    Techniques Used: Expressing, Mouse Assay, End-sequence Profiling, Western Blot, Standard Deviation

    26) Product Images from "miR-185 suppresses progression of Ewing’s sarcoma via inhibiting the PI3K/AKT and Wnt/β-catenin pathways"

    Article Title: miR-185 suppresses progression of Ewing’s sarcoma via inhibiting the PI3K/AKT and Wnt/β-catenin pathways

    Journal: OncoTargets and therapy

    doi: 10.2147/OTT.S167771

    Overexpression of miR-185 suppresses the PI3K/Akt/mTOR and Wnt/β-catenin pathways in RD-ES cells. Notes: After transfection for 48 hours, Western blot assays of PI3K/Akt/mTOR pathway-related proteins ( A ) and Wnt/β-catenin pathway-related proteins ( B ) were conducted in RD-ES cells. Levels of proteins were normalized to GAPDH, and the relative expression of the corresponding protein in miR-185 overexpressed cells was normalized to the NC. ( C ) After transfection for 48 hours, immunohistochemistry assay was performed to detect the expression of β-catenin and E-cad. The magnification was ×400. Data are presented as the mean ± standard deviation (n=3). Results were obtained in three replicates. miR-185, transfected with pCMV-MIR-miR-185 vector; NC, negative control, transfected with pCMV-MIR empty vector. * P
    Figure Legend Snippet: Overexpression of miR-185 suppresses the PI3K/Akt/mTOR and Wnt/β-catenin pathways in RD-ES cells. Notes: After transfection for 48 hours, Western blot assays of PI3K/Akt/mTOR pathway-related proteins ( A ) and Wnt/β-catenin pathway-related proteins ( B ) were conducted in RD-ES cells. Levels of proteins were normalized to GAPDH, and the relative expression of the corresponding protein in miR-185 overexpressed cells was normalized to the NC. ( C ) After transfection for 48 hours, immunohistochemistry assay was performed to detect the expression of β-catenin and E-cad. The magnification was ×400. Data are presented as the mean ± standard deviation (n=3). Results were obtained in three replicates. miR-185, transfected with pCMV-MIR-miR-185 vector; NC, negative control, transfected with pCMV-MIR empty vector. * P

    Techniques Used: Over Expression, Transfection, Western Blot, Expressing, Immunohistochemistry, Standard Deviation, Plasmid Preparation, Negative Control

    27) Product Images from "SKA3 promotes cell proliferation and migration in cervical cancer by activating the PI3K/Akt signaling pathway"

    Article Title: SKA3 promotes cell proliferation and migration in cervical cancer by activating the PI3K/Akt signaling pathway

    Journal: Cancer Cell International

    doi: 10.1186/s12935-018-0670-4

    Overexpression of SKA3 promotes cell cycle progression by activating the PI3K–Akt pathway. a Representative western blot results of proteins related to the PI3K–Akt pathway and the cell cycle in HeLa cells with stable SKA3 overexpression, SKA3 knockdown and control plasmid expression. b Activity of E2F1 in HeLa cells with stable SKA3 overexpression, SKA3 knockdown and control plasmid expression by immunofluorescence. c Representative images of IHC staining for proteins related to the cell cycle (cyclin D1 and CDK4) in tumor sections with SKA3 overexpression, SKA3 knockdown and control plasmid expression (*p
    Figure Legend Snippet: Overexpression of SKA3 promotes cell cycle progression by activating the PI3K–Akt pathway. a Representative western blot results of proteins related to the PI3K–Akt pathway and the cell cycle in HeLa cells with stable SKA3 overexpression, SKA3 knockdown and control plasmid expression. b Activity of E2F1 in HeLa cells with stable SKA3 overexpression, SKA3 knockdown and control plasmid expression by immunofluorescence. c Representative images of IHC staining for proteins related to the cell cycle (cyclin D1 and CDK4) in tumor sections with SKA3 overexpression, SKA3 knockdown and control plasmid expression (*p

    Techniques Used: Over Expression, Western Blot, Plasmid Preparation, Expressing, Activity Assay, Immunofluorescence, Immunohistochemistry, Staining

    An inhibitor of Akt blocked the cell proliferation abilities induced by SKA3 overexpression in HeLa cells. a The proliferation curves for HeLa cells with control vector expression, SKA3 overexpression, vector expression + inhibitor treatment and SKA3 overexpression + inhibitor treatment according to a CCK8 assay. b Representative images of clone formation in HeLa cells with control vector expression, SKA3 overexpression, vector expression + inhibitor treatment and SKA3 overexpression + inhibitor treatment. c Clone formation assay in HeLa cells with control vector expression, SKA3 overexpression, vector expression + inhibitor treatment and SKA3 overexpression + inhibitor treatment. d Representative cell cycle data were measured by flow cytometry in HeLa cells with control vector expression, SKA3 overexpression and SKA3 overexpression + inhibitor treatment. e Representative western blot analyses of proteins related to the PI3K–Akt pathway and the cell cycle in HeLa cells with control vector expression, SKA3 overexpression and SKA3 overexpression + inhibitor treatment. f Activity of E2F1 in HeLa cells with control vector expression, SKA3 overexpression and SKA3 overexpression + inhibitor treatment
    Figure Legend Snippet: An inhibitor of Akt blocked the cell proliferation abilities induced by SKA3 overexpression in HeLa cells. a The proliferation curves for HeLa cells with control vector expression, SKA3 overexpression, vector expression + inhibitor treatment and SKA3 overexpression + inhibitor treatment according to a CCK8 assay. b Representative images of clone formation in HeLa cells with control vector expression, SKA3 overexpression, vector expression + inhibitor treatment and SKA3 overexpression + inhibitor treatment. c Clone formation assay in HeLa cells with control vector expression, SKA3 overexpression, vector expression + inhibitor treatment and SKA3 overexpression + inhibitor treatment. d Representative cell cycle data were measured by flow cytometry in HeLa cells with control vector expression, SKA3 overexpression and SKA3 overexpression + inhibitor treatment. e Representative western blot analyses of proteins related to the PI3K–Akt pathway and the cell cycle in HeLa cells with control vector expression, SKA3 overexpression and SKA3 overexpression + inhibitor treatment. f Activity of E2F1 in HeLa cells with control vector expression, SKA3 overexpression and SKA3 overexpression + inhibitor treatment

    Techniques Used: Over Expression, Plasmid Preparation, Expressing, CCK-8 Assay, Tube Formation Assay, Flow Cytometry, Cytometry, Western Blot, Activity Assay

    28) Product Images from "SIL1 functions as an oncogene in glioma by AKT/mTOR signaling pathway"

    Article Title: SIL1 functions as an oncogene in glioma by AKT/mTOR signaling pathway

    Journal: OncoTargets and therapy

    doi: 10.2147/OTT.S167552

    Downregulation of SIL1 inhibited AKT/mTOR signaling pathway. ( A ) Western blot image and ( B ) quantification analysis indicated that siSIL1 reduced the phosphorylation level of AKT and mTOR without affecting protein expression, as well as decreasing expression of the downstream effector p70S6K. Protein expression was normalized to siNC group. Note: * P
    Figure Legend Snippet: Downregulation of SIL1 inhibited AKT/mTOR signaling pathway. ( A ) Western blot image and ( B ) quantification analysis indicated that siSIL1 reduced the phosphorylation level of AKT and mTOR without affecting protein expression, as well as decreasing expression of the downstream effector p70S6K. Protein expression was normalized to siNC group. Note: * P

    Techniques Used: Western Blot, Expressing

    29) Product Images from "Epigenetic inactivation of HOXD10 is associated with human colon cancer via inhibiting the RHOC/AKT/MAPK signaling pathway"

    Article Title: Epigenetic inactivation of HOXD10 is associated with human colon cancer via inhibiting the RHOC/AKT/MAPK signaling pathway

    Journal: Cell Communication and Signaling : CCS

    doi: 10.1186/s12964-018-0316-0

    The expression of HOXD10 displayed contrary tendency with protein RHOC. a HOXD10 stainings were gradually weakening while RHOC expression showed a reverse trend in para-carcinoma (× 100), well- (× 400), moderately- (× 400) and poorly-differentiated carcinoma (× 400), observed by immunohistochemistry (left). Statistical plot illustrates IHC staining scores in SW480 and LoVo cells (right). b Suppressed protein expression levels of RHOC, phosphorylated AKT, and phosphorylated ERK (1/2), and unchanged expression of AKT and ERK (1/2) in SW480 and LoVo cells compared with the control groups (left). Statistical plot showed the relative protein expression in RHOC/AKT/ERK in SW480 and LoVo cells (right). * P
    Figure Legend Snippet: The expression of HOXD10 displayed contrary tendency with protein RHOC. a HOXD10 stainings were gradually weakening while RHOC expression showed a reverse trend in para-carcinoma (× 100), well- (× 400), moderately- (× 400) and poorly-differentiated carcinoma (× 400), observed by immunohistochemistry (left). Statistical plot illustrates IHC staining scores in SW480 and LoVo cells (right). b Suppressed protein expression levels of RHOC, phosphorylated AKT, and phosphorylated ERK (1/2), and unchanged expression of AKT and ERK (1/2) in SW480 and LoVo cells compared with the control groups (left). Statistical plot showed the relative protein expression in RHOC/AKT/ERK in SW480 and LoVo cells (right). * P

    Techniques Used: Expressing, Immunohistochemistry, Staining

    30) Product Images from "NUMB maintains bone mass by promoting degradation of PTEN and GLI1 via ubiquitination in osteoblasts"

    Article Title: NUMB maintains bone mass by promoting degradation of PTEN and GLI1 via ubiquitination in osteoblasts

    Journal: Bone Research

    doi: 10.1038/s41413-018-0030-y

    Numb and Numbl in osteoblasts maintain the physiological bone mass. a When expressed normally in osteoblasts, the NUMB-NEDD4-PTEN tri-complexes produce, leading to ubiquitin-mediated proteasomal degradation of PTEN. At the same time, GLI1 tends to be degraded in proteasomes. Akt and Hedgehog signals are moderate in osteoblasts. b When Numb is suppressed, PTEN and GLI1 accumulate in the cytoplasm where they inhibit Akt to suppress bone formation and activate Hedgehog to enhance bone resorption, respectively
    Figure Legend Snippet: Numb and Numbl in osteoblasts maintain the physiological bone mass. a When expressed normally in osteoblasts, the NUMB-NEDD4-PTEN tri-complexes produce, leading to ubiquitin-mediated proteasomal degradation of PTEN. At the same time, GLI1 tends to be degraded in proteasomes. Akt and Hedgehog signals are moderate in osteoblasts. b When Numb is suppressed, PTEN and GLI1 accumulate in the cytoplasm where they inhibit Akt to suppress bone formation and activate Hedgehog to enhance bone resorption, respectively

    Techniques Used:

    31) Product Images from "Administration of follicle-stimulating hormone induces autophagy via upregulation of HIF-1α in mouse granulosa cells"

    Article Title: Administration of follicle-stimulating hormone induces autophagy via upregulation of HIF-1α in mouse granulosa cells

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2017.371

    FSH regulates the AKT-mTOR pathway. ( a ) FSH increased the conversion of LC3-I into LC3-II and decreased the p62 protein level in MGCs at 12 h. The level of p-mTOR and p-S6K1 was increased at 1.5 h and decreased at 3, 6, 9, and 12 h compared to that in the control group. α-Tubulin was used as a loading control. ( b ) Quantitative analysis of protein level of LC3-II/LC3-I ratio and p62 in a , top. ( c ) Quantitative analysis of protein level of p-mTOR in a , bottom. ( d ) The effects of MHY1485 on MGCs autophagy induced by FSH injection at 12 h. The protein level of p-mTOR and p-S6K1 was increased after MHY1485 treatment. LC3-II/LC3-I ratio was decreased and the level of p62 was increased after MHY1485 treatment. α-Tubulin was used as a loading control. ( e ) Quantitative analysis of protein level of LC3-II/LC3-I ratio and p62 in d , top. ( f ) Quantitative analysis of protein level of p-mTOR in d , bottom. Data are presented as means±S.E of three experiments. * P
    Figure Legend Snippet: FSH regulates the AKT-mTOR pathway. ( a ) FSH increased the conversion of LC3-I into LC3-II and decreased the p62 protein level in MGCs at 12 h. The level of p-mTOR and p-S6K1 was increased at 1.5 h and decreased at 3, 6, 9, and 12 h compared to that in the control group. α-Tubulin was used as a loading control. ( b ) Quantitative analysis of protein level of LC3-II/LC3-I ratio and p62 in a , top. ( c ) Quantitative analysis of protein level of p-mTOR in a , bottom. ( d ) The effects of MHY1485 on MGCs autophagy induced by FSH injection at 12 h. The protein level of p-mTOR and p-S6K1 was increased after MHY1485 treatment. LC3-II/LC3-I ratio was decreased and the level of p62 was increased after MHY1485 treatment. α-Tubulin was used as a loading control. ( e ) Quantitative analysis of protein level of LC3-II/LC3-I ratio and p62 in d , top. ( f ) Quantitative analysis of protein level of p-mTOR in d , bottom. Data are presented as means±S.E of three experiments. * P

    Techniques Used: Injection

    32) Product Images from "Matrine attenuates high‐fat diet‐induced in vivo and ox‐LDL‐induced in vitro vascular injury by regulating the PKCα/eNOS and PI3K/Akt/eNOS pathways, et al. Matrine attenuates high‐fat diet‐induced in vivo and ox‐LDL‐induced in vitro vascular injury by regulating the PKCα/eNOS and PI3K/Akt/eNOS pathways"

    Article Title: Matrine attenuates high‐fat diet‐induced in vivo and ox‐LDL‐induced in vitro vascular injury by regulating the PKCα/eNOS and PI3K/Akt/eNOS pathways, et al. Matrine attenuates high‐fat diet‐induced in vivo and ox‐LDL‐induced in vitro vascular injury by regulating the PKCα/eNOS and PI3K/Akt/eNOS pathways

    Journal: Journal of Cellular and Molecular Medicine

    doi: 10.1111/jcmm.14180

    Effects of matrine on eNOS activity and PI3K/Akt/eNOS pathway‐related protein expression in ox‐LDL exposed HUVECs. A, Changes in eNOS activity in HUVECs exposed to ox‐LDL with or without matrine pretreatment along with matrine and/or LY‐294002/L‐NAME as measured using an eNOS activity assay kit. B‐E, Phosphorylation levels of Ser473Akt, Ser1177eNOS, Thr495eNOS, total Akt and the eNOS protein were measured by Western blotting. Representative images of three experiments; densitometric analysis of phosphorylated proteins was normalized to that of total proteins. Data are expressed as the mean ± SD of three independent experiments, * P
    Figure Legend Snippet: Effects of matrine on eNOS activity and PI3K/Akt/eNOS pathway‐related protein expression in ox‐LDL exposed HUVECs. A, Changes in eNOS activity in HUVECs exposed to ox‐LDL with or without matrine pretreatment along with matrine and/or LY‐294002/L‐NAME as measured using an eNOS activity assay kit. B‐E, Phosphorylation levels of Ser473Akt, Ser1177eNOS, Thr495eNOS, total Akt and the eNOS protein were measured by Western blotting. Representative images of three experiments; densitometric analysis of phosphorylated proteins was normalized to that of total proteins. Data are expressed as the mean ± SD of three independent experiments, * P

    Techniques Used: Activity Assay, Expressing, Western Blot

    33) Product Images from "Achyranthes bidentata Polypeptide Protects Schwann Cells From Apoptosis in Hydrogen Peroxide-Induced Oxidative Stress"

    Article Title: Achyranthes bidentata Polypeptide Protects Schwann Cells From Apoptosis in Hydrogen Peroxide-Induced Oxidative Stress

    Journal: Frontiers in Neuroscience

    doi: 10.3389/fnins.2018.00868

    ABPPk treatment activates the PI3K/AKT and ERK1/2 pathways in SCs. (A) SCs were treated with 400 μM H 2 O 2 with or without 0.5 μg/ml ABPPk. The cells were collected and analyzed by Western blot for the expression of p-PI3K and PI3K, p-AKT and AKT, and p-ERK1/2 and ERK1/2. (B) Histogram shows data of p-PI3K/PI3K, p-AKT/AKT, and p-ERK/ERK levels from Western blot analyses. GAPDH was used as the protein loading control and band density normalization. ABPPk vs. control: P
    Figure Legend Snippet: ABPPk treatment activates the PI3K/AKT and ERK1/2 pathways in SCs. (A) SCs were treated with 400 μM H 2 O 2 with or without 0.5 μg/ml ABPPk. The cells were collected and analyzed by Western blot for the expression of p-PI3K and PI3K, p-AKT and AKT, and p-ERK1/2 and ERK1/2. (B) Histogram shows data of p-PI3K/PI3K, p-AKT/AKT, and p-ERK/ERK levels from Western blot analyses. GAPDH was used as the protein loading control and band density normalization. ABPPk vs. control: P

    Techniques Used: Western Blot, Expressing

    Effects of the LY294002 and PD98059, PI3K inhibitor, and ERK1/2 inhibitor, on oxidative damage attenuated by ABPPk in SCs. (A) Western blot shows the p-PI3K/PI3K, p-AKT/AKT, and p-ERK/ERK in SCs pretreated with LY294002 (10 μM) and PD98059 (10 μM) for 30 min before the treatment of H 2 O 2 (400 μM) and ABPPk (0.5 μg/ml) for 24 h. (B) Densitometric analyses illustrates the results of p-PI3K/PI3K, p-AKT/AKT, and p-ERK/ERK. H 2 O 2 vs control: ∗ P
    Figure Legend Snippet: Effects of the LY294002 and PD98059, PI3K inhibitor, and ERK1/2 inhibitor, on oxidative damage attenuated by ABPPk in SCs. (A) Western blot shows the p-PI3K/PI3K, p-AKT/AKT, and p-ERK/ERK in SCs pretreated with LY294002 (10 μM) and PD98059 (10 μM) for 30 min before the treatment of H 2 O 2 (400 μM) and ABPPk (0.5 μg/ml) for 24 h. (B) Densitometric analyses illustrates the results of p-PI3K/PI3K, p-AKT/AKT, and p-ERK/ERK. H 2 O 2 vs control: ∗ P

    Techniques Used: Western Blot

    The protective ABPPk on apoptosis induced by H 2 O 2 are partly impaired through the inhibition of the PI3K/AKT and ERK1/2 pathways. (A) Protein expression levels of cleaved caspase-3. (B) Quantification data of apoptotic markers cleaved caspase-3 in each group. H 2 O 2 vs control: ∗ P
    Figure Legend Snippet: The protective ABPPk on apoptosis induced by H 2 O 2 are partly impaired through the inhibition of the PI3K/AKT and ERK1/2 pathways. (A) Protein expression levels of cleaved caspase-3. (B) Quantification data of apoptotic markers cleaved caspase-3 in each group. H 2 O 2 vs control: ∗ P

    Techniques Used: Inhibition, Expressing

    34) Product Images from "Hsa_circ_0018818 knockdown suppresses tumorigenesis in non-small cell lung cancer by sponging miR-767-3p"

    Article Title: Hsa_circ_0018818 knockdown suppresses tumorigenesis in non-small cell lung cancer by sponging miR-767-3p

    Journal: Aging (Albany NY)

    doi: 10.18632/aging.103089

    Hsa_circ_0018818 shRNA1 suppresses NSCLC tumor growth in vivo . Mice were subcutaneously injected NC1-H1650 transfected with vector-control or hsa_circ_0018818 shRNA1 or left untreated (Blank), after which tumors were allowed to grow for 4 weeks. ( A ) Volumes of tumors collected at the indicted times after transplantation. ( B ) Images of tumors (left) and tumor weights (right) after 4 weeks. ( C ) RT-qPCR analysis of hsa_circ_0018818 gene expression in tumor tissues. ( D ) Western blot analysis of NID1, Akt, ERK, p-Akt and p-ERK levels in tumor tissues. ( E – G ) Relative levels of NID1, p-Akt and p-ERK expression normalized to β-actin expression. **P
    Figure Legend Snippet: Hsa_circ_0018818 shRNA1 suppresses NSCLC tumor growth in vivo . Mice were subcutaneously injected NC1-H1650 transfected with vector-control or hsa_circ_0018818 shRNA1 or left untreated (Blank), after which tumors were allowed to grow for 4 weeks. ( A ) Volumes of tumors collected at the indicted times after transplantation. ( B ) Images of tumors (left) and tumor weights (right) after 4 weeks. ( C ) RT-qPCR analysis of hsa_circ_0018818 gene expression in tumor tissues. ( D ) Western blot analysis of NID1, Akt, ERK, p-Akt and p-ERK levels in tumor tissues. ( E – G ) Relative levels of NID1, p-Akt and p-ERK expression normalized to β-actin expression. **P

    Techniques Used: In Vivo, Mouse Assay, Injection, Transfection, Plasmid Preparation, Transplantation Assay, Quantitative RT-PCR, Expressing, Western Blot

    Silencing Hsa_circ_0018818 inhibits NSCLC progression by inactivating EMT process and PI3K/Akt signaling. ( A ) Western blot analysis of NID1, E-cadherin, Vimentin, Twist-2, Akt, ERK, p-Akt and p-ERK expression in NCI-H1650 cells. ( B – G ) Relative levels of NID1, Vimentin, E-cadherin, Twist-2,p-Akt and p-ERK expression in NCI-H1650 cells normalized to β-actin expression. **P
    Figure Legend Snippet: Silencing Hsa_circ_0018818 inhibits NSCLC progression by inactivating EMT process and PI3K/Akt signaling. ( A ) Western blot analysis of NID1, E-cadherin, Vimentin, Twist-2, Akt, ERK, p-Akt and p-ERK expression in NCI-H1650 cells. ( B – G ) Relative levels of NID1, Vimentin, E-cadherin, Twist-2,p-Akt and p-ERK expression in NCI-H1650 cells normalized to β-actin expression. **P

    Techniques Used: Western Blot, Expressing

    35) Product Images from "miR-564 inhibits hepatocellular carcinoma cell proliferation and invasion by targeting the GRB2-ERK1/2-AKT axis"

    Article Title: miR-564 inhibits hepatocellular carcinoma cell proliferation and invasion by targeting the GRB2-ERK1/2-AKT axis

    Journal: Oncotarget

    doi: 10.18632/oncotarget.22504

    miR-564 regulates signaling pathways downstream of GRB2 ( A ) Expression levels of GRB2, E-cadherin, N-cadherin, p-AKT, AKT, vimentin, p-ERK1/2 and ERK1/2 in the miR-NC + vector, miR-NC + GRB2, miR-564 + vector, miR-564 + GRB2, GRB2-scramble and shGRB2 groups were measured by western blot. ( B – C ) The ratio of each protein to GAPDH. All assays were repeated three times, and the mean values were used for comparisons. * P
    Figure Legend Snippet: miR-564 regulates signaling pathways downstream of GRB2 ( A ) Expression levels of GRB2, E-cadherin, N-cadherin, p-AKT, AKT, vimentin, p-ERK1/2 and ERK1/2 in the miR-NC + vector, miR-NC + GRB2, miR-564 + vector, miR-564 + GRB2, GRB2-scramble and shGRB2 groups were measured by western blot. ( B – C ) The ratio of each protein to GAPDH. All assays were repeated three times, and the mean values were used for comparisons. * P

    Techniques Used: Expressing, Plasmid Preparation, Western Blot

    36) Product Images from "miR-448 targets Rab2B and is pivotal in the suppression of pancreatic cancer"

    Article Title: miR-448 targets Rab2B and is pivotal in the suppression of pancreatic cancer

    Journal: Oncology Reports

    doi: 10.3892/or.2018.6562

    miR-448 mimics affect the expression of cell cycle regulators and inhibit the Akt/mTOR/S6K1 pathway. (A) Ectopic expression of miR-448 inhibited the expression of Cyclin D1 but upregulated the expression of p21 and p27. The phosphorylation of (B) Akt, (C) mTOR and (D) S6K1 was suppressed by miR-448 mimics. Data are shown as the mean ± standard deviation of three independent experiments. **P
    Figure Legend Snippet: miR-448 mimics affect the expression of cell cycle regulators and inhibit the Akt/mTOR/S6K1 pathway. (A) Ectopic expression of miR-448 inhibited the expression of Cyclin D1 but upregulated the expression of p21 and p27. The phosphorylation of (B) Akt, (C) mTOR and (D) S6K1 was suppressed by miR-448 mimics. Data are shown as the mean ± standard deviation of three independent experiments. **P

    Techniques Used: Expressing, Standard Deviation

    37) Product Images from "Apigenin suppresses the apoptosis of H9C2 rat cardiomyocytes subjected to myocardial ischemia-reperfusion injury via upregulation of the PI3K/Akt pathway"

    Article Title: Apigenin suppresses the apoptosis of H9C2 rat cardiomyocytes subjected to myocardial ischemia-reperfusion injury via upregulation of the PI3K/Akt pathway

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2018.9115

    Apigenin affects the PI3K/Akt pathway. H9C2 cells were treated with MI/R, and 1, 6 and 25 µM apigenin + MI/R. Western blot analysis was conducted to measure the expression levels of (A) p-PI3K and PI3K and (B) p-Akt and Akt in H9C2 cells. *P
    Figure Legend Snippet: Apigenin affects the PI3K/Akt pathway. H9C2 cells were treated with MI/R, and 1, 6 and 25 µM apigenin + MI/R. Western blot analysis was conducted to measure the expression levels of (A) p-PI3K and PI3K and (B) p-Akt and Akt in H9C2 cells. *P

    Techniques Used: Western Blot, Expressing

    38) Product Images from "Resibufogenin inhibits ovarian clear cell carcinoma (OCCC) growth in vivo, and migration of OCCC cells in vitro, by down-regulating the PI3K/AKT and actin cytoskeleton signaling pathways"

    Article Title: Resibufogenin inhibits ovarian clear cell carcinoma (OCCC) growth in vivo, and migration of OCCC cells in vitro, by down-regulating the PI3K/AKT and actin cytoskeleton signaling pathways

    Journal: American Journal of Translational Research

    doi:

    KEGG pathway enrichment analyses of genes that were found to be differentially expressed upon resibufogenin treatment. A. Distribution of TOV-21G transcriptome sequences among KEGG pathways. All 13 apoptosis and migration-related pathways are shown. LgP is the negative logarithm of P -value; larger LgP values indicate smaller P -values. B. The differentially expressed genes that participate in the PI3K-AKT signaling pathway mapped in KEGG. C. The differentially expressed genes that participate in actin cytoskeleton pathway mapped in KEGG. The tree displays the log-transformed value of average fold changes. Red indicates up-regulated gene expression levels, whereas blue indicates down-regulated expression levels of genes. D. The differentially expressed genes that participated in the actin cytoskeleton signaling pathway mapped in KEGG. E. The brief graph of the differentially expressed genes that participated in the actin cytoskeleton signaling pathway mapped in KEGG.
    Figure Legend Snippet: KEGG pathway enrichment analyses of genes that were found to be differentially expressed upon resibufogenin treatment. A. Distribution of TOV-21G transcriptome sequences among KEGG pathways. All 13 apoptosis and migration-related pathways are shown. LgP is the negative logarithm of P -value; larger LgP values indicate smaller P -values. B. The differentially expressed genes that participate in the PI3K-AKT signaling pathway mapped in KEGG. C. The differentially expressed genes that participate in actin cytoskeleton pathway mapped in KEGG. The tree displays the log-transformed value of average fold changes. Red indicates up-regulated gene expression levels, whereas blue indicates down-regulated expression levels of genes. D. The differentially expressed genes that participated in the actin cytoskeleton signaling pathway mapped in KEGG. E. The brief graph of the differentially expressed genes that participated in the actin cytoskeleton signaling pathway mapped in KEGG.

    Techniques Used: Migration, Transformation Assay, Expressing

    Resibufogenin down-regulates expression of genes in the PI3K/AKT and actin cytoskeleton pathways. ES-2 and TOV-21G cells were divided into 2 groups: the control group, and the resibufogenin-treated group (20 μM). qRT-PCR was performed to detect the mRNAs levels of PI3K (A and E), MDM2 (B and F), GRLF1 (C and G), Myosin-II (D and H), RTK (I and J), and SOS (K and L) after 12 hours of treatment. *P
    Figure Legend Snippet: Resibufogenin down-regulates expression of genes in the PI3K/AKT and actin cytoskeleton pathways. ES-2 and TOV-21G cells were divided into 2 groups: the control group, and the resibufogenin-treated group (20 μM). qRT-PCR was performed to detect the mRNAs levels of PI3K (A and E), MDM2 (B and F), GRLF1 (C and G), Myosin-II (D and H), RTK (I and J), and SOS (K and L) after 12 hours of treatment. *P

    Techniques Used: Expressing, Quantitative RT-PCR

    Resibufogenin inhibits proliferation and invasion of OCCC cells in vivo through the PI3K/AKT and actin cytoskeleton pathways. Representative photomicrographs showing immunohistochemically stained xenograft tumor sections (100 × and 400 × magnification) showing PI3K, AKT and MDM2 expression.
    Figure Legend Snippet: Resibufogenin inhibits proliferation and invasion of OCCC cells in vivo through the PI3K/AKT and actin cytoskeleton pathways. Representative photomicrographs showing immunohistochemically stained xenograft tumor sections (100 × and 400 × magnification) showing PI3K, AKT and MDM2 expression.

    Techniques Used: In Vivo, Staining, Expressing

    Resibufogenin down-regulates expression of proteins in the PI3K/AKT and actin cytoskeleton pathways in vitro . ES-2 and TOV-21G cells were divided into 2 groups: the control group, and the resibufogenin-treated group (20 μM). Western blotting assay was performed to detect the protein levels of PI3K (A and B), AKT (A), MDM2 (D), and Myosin-II (D) after 24 hours of treatment. The relative expression levels of the indicated proteins (relative to the expression level of actin) were quantitated using densitometry and are depicted bar graphically in (B, C, E, and F). *P
    Figure Legend Snippet: Resibufogenin down-regulates expression of proteins in the PI3K/AKT and actin cytoskeleton pathways in vitro . ES-2 and TOV-21G cells were divided into 2 groups: the control group, and the resibufogenin-treated group (20 μM). Western blotting assay was performed to detect the protein levels of PI3K (A and B), AKT (A), MDM2 (D), and Myosin-II (D) after 24 hours of treatment. The relative expression levels of the indicated proteins (relative to the expression level of actin) were quantitated using densitometry and are depicted bar graphically in (B, C, E, and F). *P

    Techniques Used: Expressing, In Vitro, Western Blot

    Schematic diagram of the proposed mechanism by which resibufogenin inhibits proliferation and invasion in OCCC cells. Resibufogenin decreases the levels of PI3K, AKT, MDM2, and Myosin in the PI3K/AKT and actin cytoskeleton signaling pathways.
    Figure Legend Snippet: Schematic diagram of the proposed mechanism by which resibufogenin inhibits proliferation and invasion in OCCC cells. Resibufogenin decreases the levels of PI3K, AKT, MDM2, and Myosin in the PI3K/AKT and actin cytoskeleton signaling pathways.

    Techniques Used:

    39) Product Images from "Cul4 E3 ubiquitin ligase regulates ovarian cancer drug resistance by targeting the antiapoptotic protein BIRC3"

    Article Title: Cul4 E3 ubiquitin ligase regulates ovarian cancer drug resistance by targeting the antiapoptotic protein BIRC3

    Journal: Cell Death & Disease

    doi: 10.1038/s41419-018-1200-y

    Upregulation of BIRC3 in ovarian cancer requires the STAT3 pathway. a Western blot detection of AKT, phosphorylated AKT, BIRC3, Caspace 3, and cleaved caspase-3 in A2780CP cells in the absence or presence of PI3K inhibitor LY294002 (40 μM) or cisplatin (12.5 μM). GAPDH serves as a loading control. A2780CP cells were cultured in six-well plates and pretreated with the LY294002 for 1 h before cisplatin addition. Total protein was extracted 24 h after treatment. Similar results were obtained from three independent experiments. b Western blot detection of STAT3, phosphorylated STAT3, BIRC3, Caspace 3, and cleaved caspase-3 in A2780CP cells in the absence or presence of STAT3 inhibitor S3I-201 (100 μM) or cisplatin (12.5 μM). GAPDH serves as loading control. A2780CP cells were cultured in six-well plates and pretreated with the STAT3 inhibitor S3I-201 for 1 h before cisplatin treatment. Total protein was extracted 24 h after cisplatin treatment. Similar results were obtained from three independent experiments. c and d Western blot detection of ( c ) DDB1, ( d ) Cul4A, ( c and d ) BIRC3, BIRC7, AKT, phosphorylated AKT, STAT3, phosphorylated STAT3, Caspace 3, and cleaved caspase-3 in A2780CP cells with ( c ) DDB1 or ( d ) Cul4A knockdown. GAPDH serves as a loading control. A2780CP cells were cultured in six-well plates and transfected with shRNA against DDB1 or Cul4A. Total protein was extracted 48 h after transfection. Similar results were obtained from three independent experiments. e and f Western blot detection of ( e ) DDB1, ( f ) Cul4A, and ( e and f ) STAT1 in A2780CP cells with ( c ) DDB1 or ( d ) Cul4A knockdown. GAPDH serves as a loading control. Knockdown procedure of Cul4A and DDB1 with shRNAs in A2780 cells is same as described above. g Immunoblot detection of STAT1 and STAT3 in input (lower panel) or immunoprecipitated (upper panel) samples in control or CRL4 (Cul4A/DDB1) knockdown A2780CP cells. GAPDH serves as a loading control. For immunoprecipitation, 2 μg antibody was used in each group. Precipitated STAT3 levels were quantified with Image J software and normalized to the control group (NT). h A model of CRL4 regulation on BIRC3 expression leading to chemoresistance in ovarian cancer
    Figure Legend Snippet: Upregulation of BIRC3 in ovarian cancer requires the STAT3 pathway. a Western blot detection of AKT, phosphorylated AKT, BIRC3, Caspace 3, and cleaved caspase-3 in A2780CP cells in the absence or presence of PI3K inhibitor LY294002 (40 μM) or cisplatin (12.5 μM). GAPDH serves as a loading control. A2780CP cells were cultured in six-well plates and pretreated with the LY294002 for 1 h before cisplatin addition. Total protein was extracted 24 h after treatment. Similar results were obtained from three independent experiments. b Western blot detection of STAT3, phosphorylated STAT3, BIRC3, Caspace 3, and cleaved caspase-3 in A2780CP cells in the absence or presence of STAT3 inhibitor S3I-201 (100 μM) or cisplatin (12.5 μM). GAPDH serves as loading control. A2780CP cells were cultured in six-well plates and pretreated with the STAT3 inhibitor S3I-201 for 1 h before cisplatin treatment. Total protein was extracted 24 h after cisplatin treatment. Similar results were obtained from three independent experiments. c and d Western blot detection of ( c ) DDB1, ( d ) Cul4A, ( c and d ) BIRC3, BIRC7, AKT, phosphorylated AKT, STAT3, phosphorylated STAT3, Caspace 3, and cleaved caspase-3 in A2780CP cells with ( c ) DDB1 or ( d ) Cul4A knockdown. GAPDH serves as a loading control. A2780CP cells were cultured in six-well plates and transfected with shRNA against DDB1 or Cul4A. Total protein was extracted 48 h after transfection. Similar results were obtained from three independent experiments. e and f Western blot detection of ( e ) DDB1, ( f ) Cul4A, and ( e and f ) STAT1 in A2780CP cells with ( c ) DDB1 or ( d ) Cul4A knockdown. GAPDH serves as a loading control. Knockdown procedure of Cul4A and DDB1 with shRNAs in A2780 cells is same as described above. g Immunoblot detection of STAT1 and STAT3 in input (lower panel) or immunoprecipitated (upper panel) samples in control or CRL4 (Cul4A/DDB1) knockdown A2780CP cells. GAPDH serves as a loading control. For immunoprecipitation, 2 μg antibody was used in each group. Precipitated STAT3 levels were quantified with Image J software and normalized to the control group (NT). h A model of CRL4 regulation on BIRC3 expression leading to chemoresistance in ovarian cancer

    Techniques Used: Western Blot, Cell Culture, Transfection, shRNA, Immunoprecipitation, Software, Expressing

    40) Product Images from "PTBP1 promotes the growth of breast cancer cells through the PTEN/Akt pathway and autophagy. PTBP1 promotes the growth of breast cancer cells through the PTEN/Akt pathway and autophagy"

    Article Title: PTBP1 promotes the growth of breast cancer cells through the PTEN/Akt pathway and autophagy. PTBP1 promotes the growth of breast cancer cells through the PTEN/Akt pathway and autophagy

    Journal: Journal of Cellular Physiology

    doi: 10.1002/jcp.26823

    Increased expression levels of PTBP1 and p‐Akt were demonstrated in clinical tumor samples from breast cancer patients. (a) PTBP1, p‐Akt, and Akt expressions were analyzed in 137 breast cancer samples as determined by western blot. Actin was used as the control. (b) The relationship between PTBP1 and p‐Akt was significant. P
    Figure Legend Snippet: Increased expression levels of PTBP1 and p‐Akt were demonstrated in clinical tumor samples from breast cancer patients. (a) PTBP1, p‐Akt, and Akt expressions were analyzed in 137 breast cancer samples as determined by western blot. Actin was used as the control. (b) The relationship between PTBP1 and p‐Akt was significant. P

    Techniques Used: Expressing, Western Blot

    Knockdown of PTBP1 leads to upregulation of PTEN and decreased expression of p‐Akt and cell growth. (a) To validate the effct of PTBP1 on P‐Akt western blot analysis was performed. Expression of p‐Akt decreased in PTBP1‐knockdown cells compared with control. GADPH was used as a loading control. (b) With the overexpression of PTBP1, the expression of p‐Akt increased compared with control using western blot assay. GADPH was used as a loading control. (c) To validate the effct of PTBP1 on PTEN, western blot analysis was performed. The expression of PTEN increased in PTBP1‐knockdown cells compared with the control. GADPH was used as a loading control. (d) The overexpression of PTBP1 decreased the expression of PTEN compared with the controls using western blot assay. GADPH was used as a loading control. (e) To validate the effct of PTBP1 on autophagy, the expression level of LC3BI and LC3BII was examined by western blot analysis. Knockdown of PTBP1 induced the transition of the LC3BI to LC3BII. GADPH was used as a loading control. (f) Overexpression of PTBP1 reduced the transition of the LC3BI to LC3BII using western blot analysis. GADPH was used as a loading control. GADPH, glyceraldehyde‐3‐phosphate dehydrogenase; p‐AkPTBP1, polypyrimidine tract binding protein 1; PTEN, phosphatase and tensin homolog
    Figure Legend Snippet: Knockdown of PTBP1 leads to upregulation of PTEN and decreased expression of p‐Akt and cell growth. (a) To validate the effct of PTBP1 on P‐Akt western blot analysis was performed. Expression of p‐Akt decreased in PTBP1‐knockdown cells compared with control. GADPH was used as a loading control. (b) With the overexpression of PTBP1, the expression of p‐Akt increased compared with control using western blot assay. GADPH was used as a loading control. (c) To validate the effct of PTBP1 on PTEN, western blot analysis was performed. The expression of PTEN increased in PTBP1‐knockdown cells compared with the control. GADPH was used as a loading control. (d) The overexpression of PTBP1 decreased the expression of PTEN compared with the controls using western blot assay. GADPH was used as a loading control. (e) To validate the effct of PTBP1 on autophagy, the expression level of LC3BI and LC3BII was examined by western blot analysis. Knockdown of PTBP1 induced the transition of the LC3BI to LC3BII. GADPH was used as a loading control. (f) Overexpression of PTBP1 reduced the transition of the LC3BI to LC3BII using western blot analysis. GADPH was used as a loading control. GADPH, glyceraldehyde‐3‐phosphate dehydrogenase; p‐AkPTBP1, polypyrimidine tract binding protein 1; PTEN, phosphatase and tensin homolog

    Techniques Used: Expressing, Western Blot, Over Expression, Binding Assay

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    Immunoprecipitation:

    Article Title: The role of the ShcD and RET interaction in neuroblastoma survival and migration
    Article Snippet: .. The following primary antibodies were used for immunoblotting, immunoprecipitation and immunofluorescence: anti-RET (sc-9996; Santa Cruz, USA), anti-MYC (ab9106; Abcam, UK), anti-MYC tag (ab18185; Abcam), anti-phospho-tyrosine (ab179530; Abcam), anti-ShcD (sc-165482; Santa Cruz, USA), anti-AKT1/2/3 (ab179463; Abcam), anti-phospho-AKT1/2/3 (sc-7985; Santa Cruz), anti-PKC (ab179522; Abcam), anti-GFP (sc-9996; Santa Cruz), anti-phospho-RET (sc-20252; Santa Cruz), anti-ERK1/2 (9102S; Cell Signalling), anti-phospho-ERK1/2 (4370S; Cell Signalling), anti-β actin (4970S; Cell Signalling), anti-GAPDH (ab37168; Abcam), anti-RET (ab134100; Abcam) and anti-RAB7 (ab198337). .. Horseradish peroxidase-conjugated anti-goat (ab97023, Abcam), anti-mouse (7076S; Cell Signalling) and anti-rabbit (7074S; Cell Signalling) secondary antibodies were used for immunoblotting.

    Incubation:

    Article Title: LncRNA XIST/miR-34a axis modulates the cell proliferation and tumor growth of thyroid cancer through MET-PI3K-AKT signaling
    Article Snippet: .. The blots were probed with the following antibodies at 4 °C overnight: anti-MET (ab51067, Abcam, Cambridge, MA, USA), anti-p-PI3K (phospho Y607, ab182651, Abcam), anti-PI3K (ab86714, Abcam), anti-p-AKT (phospho S473, ab81283, Abcam), anti-AKT (ab179463, Abcam) and anti-GAPDH (ab8245, Abcam) and incubated with HRP-conjugated secondary antibody (1:5000). .. Signals were visualized using ECL Substrates (Millipore, USA).

    Article Title: Opening of mitoKATP improves cardiac function and inhibits apoptosis via the AKT-Foxo1 signaling pathway in diabetic cardiomyopathy
    Article Snippet: .. The membranes were blocked in 5% non-fat milk or 5% BSA in 1X TBST (Solarbo) for 2 h at room temperature, then incubated overnight at 4°C with primary antibodies as follows: p-AKT (1:5,000; rabbit monoclonal, ab81283, Abcam, Cambridge, UK), t-AKT (1:10,000; rabbit monoclonal, ab179463, Abcam), p-Foxo1 (1:500; rabbit polyclonal, ab131339, Abcam), t-Foxo1 (1:500; rabbit polyclonal, ab39670, Abcam), GAPDH (1:30,000; rabbit monoclonal, ab181602, Abcam), and caspase 3 (1:1,000; rabbit polyclonal, 9662, Cell Signaling Technology Inc., Danvers, MA, USA). .. The membranes were washed in 1X TBST on a shaker at 10 × g for 15 min, and then incubated at room temperature with HRP-conjugated secondary antibodies for 60 min.

    Article Title: Sericin enhances the insulin-PI3K/AKT signaling pathway in the liver of a type 2 diabetes rat model
    Article Snippet: .. The sections were then incubated with primary antibodies against IR (1:100; cat. no. ab131238), IRS-1 (1:100; cat. no. ab131487; both Abcam, Cambridge, MA USA), PI3K (1:100; cat. no. 611398; BD Biosciences, San Jose, CA, USA) and AKT (1:200; cat. no. ab179463; Abcam) at 4°C overnight. .. Next, the sections were incubated with goat anti-rabbit IgG secondary antibodies, which was provided by the rabbit streptavidin-biotin assay system (cat. no. SP-9001; Zhongshan Jinqiao Biotechnology Co., Ltd., Beijing, China) according to the manufacturer's protocol, and then counterstained with DAB for 5–8 min at room temperature.

    Article Title: Stromal cell-derived factor-1α and transforming growth factor-β1 synergistically facilitate migration and chondrogenesis of synovium-derived stem cells through MAPK pathways
    Article Snippet: .. After blocking the membrane with 5% milk solution in 0.1% TBS-Tween 20 for 1 h at room temperature, the membranes were incubated overnight at 4°C with the following primary antibodies: anti-CXCR4 (ab124824, 1:75, Abcam, Cambridge, UK), anti-phospho-Akt (ab183758, 1:1000, Abcam), anti-Akt antibodies (ab179463, 1:10000, Abcam), anti-phospho-ERK (ab201015, 1:1000, Abcam), anti-ERK (ab184699, 1:10000, Abcam), anti-phospho-JNK (ab124956, 1:1000, Abcam), anti-JNK (ab179461, 1:1000, Abcam), anti-phospho-p38 (ab4822, 1:1000, Abcam), anti-p38 (ab170099, 1:1000, Abcam), anti-vimentin (ab92547, 1:1000, Abcam) and anti-β-actin (ab8226, 1:2500, Abcam). .. Membranes were washed in 0.1% TBS-Tween 20 and incubated for 1 h with appropriate HRP-conjugated secondary antibody (1:5000, Santa Cruz Biotechnology, Santa Cruz, CA, USA) and protein bands were visualized using the enhanced chemiluminescence method (Pierce, IL).

    Immunofluorescence:

    Article Title: The role of the ShcD and RET interaction in neuroblastoma survival and migration
    Article Snippet: .. The following primary antibodies were used for immunoblotting, immunoprecipitation and immunofluorescence: anti-RET (sc-9996; Santa Cruz, USA), anti-MYC (ab9106; Abcam, UK), anti-MYC tag (ab18185; Abcam), anti-phospho-tyrosine (ab179530; Abcam), anti-ShcD (sc-165482; Santa Cruz, USA), anti-AKT1/2/3 (ab179463; Abcam), anti-phospho-AKT1/2/3 (sc-7985; Santa Cruz), anti-PKC (ab179522; Abcam), anti-GFP (sc-9996; Santa Cruz), anti-phospho-RET (sc-20252; Santa Cruz), anti-ERK1/2 (9102S; Cell Signalling), anti-phospho-ERK1/2 (4370S; Cell Signalling), anti-β actin (4970S; Cell Signalling), anti-GAPDH (ab37168; Abcam), anti-RET (ab134100; Abcam) and anti-RAB7 (ab198337). .. Horseradish peroxidase-conjugated anti-goat (ab97023, Abcam), anti-mouse (7076S; Cell Signalling) and anti-rabbit (7074S; Cell Signalling) secondary antibodies were used for immunoblotting.

    Blocking Assay:

    Article Title: Stromal cell-derived factor-1α and transforming growth factor-β1 synergistically facilitate migration and chondrogenesis of synovium-derived stem cells through MAPK pathways
    Article Snippet: .. After blocking the membrane with 5% milk solution in 0.1% TBS-Tween 20 for 1 h at room temperature, the membranes were incubated overnight at 4°C with the following primary antibodies: anti-CXCR4 (ab124824, 1:75, Abcam, Cambridge, UK), anti-phospho-Akt (ab183758, 1:1000, Abcam), anti-Akt antibodies (ab179463, 1:10000, Abcam), anti-phospho-ERK (ab201015, 1:1000, Abcam), anti-ERK (ab184699, 1:10000, Abcam), anti-phospho-JNK (ab124956, 1:1000, Abcam), anti-JNK (ab179461, 1:1000, Abcam), anti-phospho-p38 (ab4822, 1:1000, Abcam), anti-p38 (ab170099, 1:1000, Abcam), anti-vimentin (ab92547, 1:1000, Abcam) and anti-β-actin (ab8226, 1:2500, Abcam). .. Membranes were washed in 0.1% TBS-Tween 20 and incubated for 1 h with appropriate HRP-conjugated secondary antibody (1:5000, Santa Cruz Biotechnology, Santa Cruz, CA, USA) and protein bands were visualized using the enhanced chemiluminescence method (Pierce, IL).

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  • 99
    Abcam anti akt
    XIST modulates miR-34a downstream <t>MET-PI3K-AKT</t> signaling via miR-34a ( a - c ) KAT18 and FTC113 cells were co-transfected with si-XIST and miR-34a inhibitor; the protein levels of MET, p-PI3K, PI3K, p-AKT and AKT were examined using Immunoblotting assays. The data are presented as mean ± SD of three independent experiments. ** P
    Anti Akt, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 163 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti akt/product/Abcam
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    Abcam rabbit anti akt antibody
    (A) The mRNA expression levels of GH, GHSR, <t>IGF-1</t> and <t>Akt</t> in myocardial tissues in various groups [control, sham, H/R and ghrelin (ghrelin + H/R)], which was determined by reverse transcription-polymerase chain reaction. (B) The protein expression levels of GH, GHSR, IGF-1, Akt and p-Akt in myocardial tissues in various groups, which was evaluated by western blot analysis. GH, growth hormone; GHSR, growth hormone secretagogue receptor; IGF-1, insulin-like growth factor-1; Akt, protein kinase B; p-Akt, phosphorylated Akt; H/R, hypoxia/reoxygenation. * P
    Rabbit Anti Akt Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti akt antibody/product/Abcam
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    akt  (Abcam)
    99
    Abcam akt
    In vivo anti-cancer efficacy of tunicamycin treatment in colon-bearing mice. (A) Tunicamycin treatment inhibited tumor growth in a 25-day observation. (B) Immunohistochemistry demonstrated the effect of tunicamycin treatment on apoptosis (bad), caspase-3 and caspase-9 expression levels in tumor tissues. (C) Effect of tunicamycin treatment on mTOR and Bcl-2 expression levels in tumor tissues after 25 days. (D) Effect of tunicamycin treatment on Ki67 and PCNA expression levels in tumor tissues after 25 days. (E) Tunicamycin treatment decreased ERK, <t>JNK</t> and <t>AKT</t> expression in tumor tissues after 25 days. (F) Tunicamycin treatment prolonged the survival rate of SW620-bearing mice in a 120-day experiment. Data are expressed as mean ± standard deviation of triplicate experiments. **P
    Akt, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam rabbit anti mouse akt
    (a), (b), (c), and (d): the protein expression of P110 α , P85 α , <t>AKT,</t> and <t>C-JUN</t> on Treg cells in the tumor microenvironment by IF assay. (e): the protein expression of P110 α , P85 α , AKT, and C-JUN on Treg cells in the tumor microenvironment by WB. (f), (g), (h), and (i): the protein expression of P110 α , AKT, C-JUN, and P85 α in the Treg cells in the tumor microenvironment was expressed as the ratio of the gray level of each protein to the β -actin band.
    Rabbit Anti Mouse Akt, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    XIST modulates miR-34a downstream MET-PI3K-AKT signaling via miR-34a ( a - c ) KAT18 and FTC113 cells were co-transfected with si-XIST and miR-34a inhibitor; the protein levels of MET, p-PI3K, PI3K, p-AKT and AKT were examined using Immunoblotting assays. The data are presented as mean ± SD of three independent experiments. ** P

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: LncRNA XIST/miR-34a axis modulates the cell proliferation and tumor growth of thyroid cancer through MET-PI3K-AKT signaling

    doi: 10.1186/s13046-018-0950-9

    Figure Lengend Snippet: XIST modulates miR-34a downstream MET-PI3K-AKT signaling via miR-34a ( a - c ) KAT18 and FTC113 cells were co-transfected with si-XIST and miR-34a inhibitor; the protein levels of MET, p-PI3K, PI3K, p-AKT and AKT were examined using Immunoblotting assays. The data are presented as mean ± SD of three independent experiments. ** P

    Article Snippet: The blots were probed with the following antibodies at 4 °C overnight: anti-MET (ab51067, Abcam, Cambridge, MA, USA), anti-p-PI3K (phospho Y607, ab182651, Abcam), anti-PI3K (ab86714, Abcam), anti-p-AKT (phospho S473, ab81283, Abcam), anti-AKT (ab179463, Abcam) and anti-GAPDH (ab8245, Abcam) and incubated with HRP-conjugated secondary antibody (1:5000).

    Techniques: Transfection

    (A) The mRNA expression levels of GH, GHSR, IGF-1 and Akt in myocardial tissues in various groups [control, sham, H/R and ghrelin (ghrelin + H/R)], which was determined by reverse transcription-polymerase chain reaction. (B) The protein expression levels of GH, GHSR, IGF-1, Akt and p-Akt in myocardial tissues in various groups, which was evaluated by western blot analysis. GH, growth hormone; GHSR, growth hormone secretagogue receptor; IGF-1, insulin-like growth factor-1; Akt, protein kinase B; p-Akt, phosphorylated Akt; H/R, hypoxia/reoxygenation. * P

    Journal: International Journal of Molecular Medicine

    Article Title: Ghrelin protects the myocardium with hypoxia/reoxygenation treatment through upregulating the expression of growth hormone, growth hormone secretagogue receptor and insulin-like growth factor-1, and promoting the phosphorylation of protein kinase B

    doi: 10.3892/ijmm.2018.3886

    Figure Lengend Snippet: (A) The mRNA expression levels of GH, GHSR, IGF-1 and Akt in myocardial tissues in various groups [control, sham, H/R and ghrelin (ghrelin + H/R)], which was determined by reverse transcription-polymerase chain reaction. (B) The protein expression levels of GH, GHSR, IGF-1, Akt and p-Akt in myocardial tissues in various groups, which was evaluated by western blot analysis. GH, growth hormone; GHSR, growth hormone secretagogue receptor; IGF-1, insulin-like growth factor-1; Akt, protein kinase B; p-Akt, phosphorylated Akt; H/R, hypoxia/reoxygenation. * P

    Article Snippet: Mouse anti-GH antibody (cat. no. ab9821; dilution, 1:1,200), rabbit anti-IGF-1 antibody (cat. no. ab182408; dilution, 1:1,000), rabbit anti-Akt antibody (cat. no. ab81283; dilution, 1:1,000) and rabbit anti-p-Akt antibody (cat. no. ab38449; dilution, 1:1,000) were purchased from Abcam (Cambridge, MA, USA).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Western Blot

    The expression levels of GH, GHSR, IGF-1, Akt and p-Akt in primary cardiac myocytes in various groups. (A) The mRNA expression levels of GH, GHSR, IGF-1 and Akt in primary cardiac myocytes in various groups [control, H/R, empty (empty pLVX-Puro plasmid + H/R) and ghrelin (ghrelin-pLVX-Puro plasmid + H/R)], which was determined by reverse transcription-polymerase chain reaction. (B) The protein expression levels of GH, GHSR, IGF-1, Akt and p-Akt in primary cardiac myocytes in various groups, which was evaluated by western blot analysis. GH, growth hormone; GHSR, growth hormone secretagogue receptor; IGF-1, insulin-like growth factor-1; Akt, protein kinase B; p-Akt, phosphorylated Akt. * P

    Journal: International Journal of Molecular Medicine

    Article Title: Ghrelin protects the myocardium with hypoxia/reoxygenation treatment through upregulating the expression of growth hormone, growth hormone secretagogue receptor and insulin-like growth factor-1, and promoting the phosphorylation of protein kinase B

    doi: 10.3892/ijmm.2018.3886

    Figure Lengend Snippet: The expression levels of GH, GHSR, IGF-1, Akt and p-Akt in primary cardiac myocytes in various groups. (A) The mRNA expression levels of GH, GHSR, IGF-1 and Akt in primary cardiac myocytes in various groups [control, H/R, empty (empty pLVX-Puro plasmid + H/R) and ghrelin (ghrelin-pLVX-Puro plasmid + H/R)], which was determined by reverse transcription-polymerase chain reaction. (B) The protein expression levels of GH, GHSR, IGF-1, Akt and p-Akt in primary cardiac myocytes in various groups, which was evaluated by western blot analysis. GH, growth hormone; GHSR, growth hormone secretagogue receptor; IGF-1, insulin-like growth factor-1; Akt, protein kinase B; p-Akt, phosphorylated Akt. * P

    Article Snippet: Mouse anti-GH antibody (cat. no. ab9821; dilution, 1:1,200), rabbit anti-IGF-1 antibody (cat. no. ab182408; dilution, 1:1,000), rabbit anti-Akt antibody (cat. no. ab81283; dilution, 1:1,000) and rabbit anti-p-Akt antibody (cat. no. ab38449; dilution, 1:1,000) were purchased from Abcam (Cambridge, MA, USA).

    Techniques: Expressing, Plasmid Preparation, Reverse Transcription Polymerase Chain Reaction, Western Blot

    The immunohistochemical staining images of GH, GHSR, IGF-1 and Akt in myocardial tissues in various groups [control, sham, H/R and ghrelin (ghrelin + H/R)]. The corresponding protein and the nuclei are shown by brown (arrows) and bluish violet, respectively. GH, growth hormone; GHSR, growth hormone secretagogue receptor; IGF-1, insulin-like growth factor-1; Akt, protein kinase B; H/R, hypoxia/reoxygenation. Magnification, ×200.

    Journal: International Journal of Molecular Medicine

    Article Title: Ghrelin protects the myocardium with hypoxia/reoxygenation treatment through upregulating the expression of growth hormone, growth hormone secretagogue receptor and insulin-like growth factor-1, and promoting the phosphorylation of protein kinase B

    doi: 10.3892/ijmm.2018.3886

    Figure Lengend Snippet: The immunohistochemical staining images of GH, GHSR, IGF-1 and Akt in myocardial tissues in various groups [control, sham, H/R and ghrelin (ghrelin + H/R)]. The corresponding protein and the nuclei are shown by brown (arrows) and bluish violet, respectively. GH, growth hormone; GHSR, growth hormone secretagogue receptor; IGF-1, insulin-like growth factor-1; Akt, protein kinase B; H/R, hypoxia/reoxygenation. Magnification, ×200.

    Article Snippet: Mouse anti-GH antibody (cat. no. ab9821; dilution, 1:1,200), rabbit anti-IGF-1 antibody (cat. no. ab182408; dilution, 1:1,000), rabbit anti-Akt antibody (cat. no. ab81283; dilution, 1:1,000) and rabbit anti-p-Akt antibody (cat. no. ab38449; dilution, 1:1,000) were purchased from Abcam (Cambridge, MA, USA).

    Techniques: Immunohistochemistry, Staining

    In vivo anti-cancer efficacy of tunicamycin treatment in colon-bearing mice. (A) Tunicamycin treatment inhibited tumor growth in a 25-day observation. (B) Immunohistochemistry demonstrated the effect of tunicamycin treatment on apoptosis (bad), caspase-3 and caspase-9 expression levels in tumor tissues. (C) Effect of tunicamycin treatment on mTOR and Bcl-2 expression levels in tumor tissues after 25 days. (D) Effect of tunicamycin treatment on Ki67 and PCNA expression levels in tumor tissues after 25 days. (E) Tunicamycin treatment decreased ERK, JNK and AKT expression in tumor tissues after 25 days. (F) Tunicamycin treatment prolonged the survival rate of SW620-bearing mice in a 120-day experiment. Data are expressed as mean ± standard deviation of triplicate experiments. **P

    Journal: Molecular Medicine Reports

    Article Title: Tunicamycin inhibits colon carcinoma growth and aggressiveness via modulation of the ERK-JNK-mediated AKT/mTOR signaling pathway

    doi: 10.3892/mmr.2018.8444

    Figure Lengend Snippet: In vivo anti-cancer efficacy of tunicamycin treatment in colon-bearing mice. (A) Tunicamycin treatment inhibited tumor growth in a 25-day observation. (B) Immunohistochemistry demonstrated the effect of tunicamycin treatment on apoptosis (bad), caspase-3 and caspase-9 expression levels in tumor tissues. (C) Effect of tunicamycin treatment on mTOR and Bcl-2 expression levels in tumor tissues after 25 days. (D) Effect of tunicamycin treatment on Ki67 and PCNA expression levels in tumor tissues after 25 days. (E) Tunicamycin treatment decreased ERK, JNK and AKT expression in tumor tissues after 25 days. (F) Tunicamycin treatment prolonged the survival rate of SW620-bearing mice in a 120-day experiment. Data are expressed as mean ± standard deviation of triplicate experiments. **P

    Article Snippet: The sections were rinsed with PBS and placed in a solution containing primary antibodies directed against Ki67 (1:1,000; ab16667; Abcam), PCNA (1:1,000; ab18197; Abcam), Caspase3 (1:2,000; ab90437; Abcam), Caspase9 (1:1,000; ab32539; Abcam), Bcl-2 (1:1,000; ab692; Abcam), ERK (1:2,000; ab196883; Abcam), JNK (1:1,000; ab179461; Abcam), mTOR (1:1,000; ab87540; Abcam) and AKT (1:1,000; ab8978; Abcam) incubated overnight at 4°C.

    Techniques: In Vivo, Mouse Assay, Immunohistochemistry, Expressing, Standard Deviation

    Tunicamycin regulates growth and apoptosis of clonal tumor cells through the ERK-JNK-mediated AKT/mTOR signaling pathway. (A) Tunicamycin inhibits total and phosphorylated AKT expression in SW620 cells. (B) Tunicamycin inhibits mTOR expression in SW620 cells. Effects of ERK overexpression on expression of (C) total and phosphorylated AKT and (D) mTOR in SW620 cells. (E) Tunicamycin blocked ERK overexpression-induced growth and (F) ERK overexpression-inhibited apoptosis in SW620 cells. Data are expressed as the mean ± standard deviation of triplicate experiments. **P

    Journal: Molecular Medicine Reports

    Article Title: Tunicamycin inhibits colon carcinoma growth and aggressiveness via modulation of the ERK-JNK-mediated AKT/mTOR signaling pathway

    doi: 10.3892/mmr.2018.8444

    Figure Lengend Snippet: Tunicamycin regulates growth and apoptosis of clonal tumor cells through the ERK-JNK-mediated AKT/mTOR signaling pathway. (A) Tunicamycin inhibits total and phosphorylated AKT expression in SW620 cells. (B) Tunicamycin inhibits mTOR expression in SW620 cells. Effects of ERK overexpression on expression of (C) total and phosphorylated AKT and (D) mTOR in SW620 cells. (E) Tunicamycin blocked ERK overexpression-induced growth and (F) ERK overexpression-inhibited apoptosis in SW620 cells. Data are expressed as the mean ± standard deviation of triplicate experiments. **P

    Article Snippet: The sections were rinsed with PBS and placed in a solution containing primary antibodies directed against Ki67 (1:1,000; ab16667; Abcam), PCNA (1:1,000; ab18197; Abcam), Caspase3 (1:2,000; ab90437; Abcam), Caspase9 (1:1,000; ab32539; Abcam), Bcl-2 (1:1,000; ab692; Abcam), ERK (1:2,000; ab196883; Abcam), JNK (1:1,000; ab179461; Abcam), mTOR (1:1,000; ab87540; Abcam) and AKT (1:1,000; ab8978; Abcam) incubated overnight at 4°C.

    Techniques: Expressing, Over Expression, Standard Deviation

    (a), (b), (c), and (d): the protein expression of P110 α , P85 α , AKT, and C-JUN on Treg cells in the tumor microenvironment by IF assay. (e): the protein expression of P110 α , P85 α , AKT, and C-JUN on Treg cells in the tumor microenvironment by WB. (f), (g), (h), and (i): the protein expression of P110 α , AKT, C-JUN, and P85 α in the Treg cells in the tumor microenvironment was expressed as the ratio of the gray level of each protein to the β -actin band.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: The Antitumor Effect of Xihuang Pill on Treg Cells Decreased in Tumor Microenvironment of 4T1 Breast Tumor-Bearing Mice by PI3K/AKT~AP-1 Signaling Pathway

    doi: 10.1155/2018/6714829

    Figure Lengend Snippet: (a), (b), (c), and (d): the protein expression of P110 α , P85 α , AKT, and C-JUN on Treg cells in the tumor microenvironment by IF assay. (e): the protein expression of P110 α , P85 α , AKT, and C-JUN on Treg cells in the tumor microenvironment by WB. (f), (g), (h), and (i): the protein expression of P110 α , AKT, C-JUN, and P85 α in the Treg cells in the tumor microenvironment was expressed as the ratio of the gray level of each protein to the β -actin band.

    Article Snippet: The above antibodies were as follows: primary antibodies: Rabbit anti-mouse β -actin, Rabbit anti-mouse PI3K P110α (all 1 : 100, CST, USA), Rabbit anti-mouse C-JUN antibody, Rabbit anti-mouse AKT, and Rabbit anti-mouse PI3K P85α (all 1 : 100, Abcam, USA); secondary fluorescently labeled antibodies: Donkey anti-rabbit antibody (Alexa Fluor 488) and Donkey anti-rabbit antibody (Cy3) (all 1 : 200, Jackson, USA).

    Techniques: Expressing, Western Blot

    RT-q PCR amplification curve and gene expression relative quantitative analysis. (a), (b), (c), and (d): amplification curves of P110 α , P85 α , AKT, and C-JUN. (e), (f), (g), and (h): the relative mRNA expression of P110 α , P85 α , AKT, and C-JUN.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: The Antitumor Effect of Xihuang Pill on Treg Cells Decreased in Tumor Microenvironment of 4T1 Breast Tumor-Bearing Mice by PI3K/AKT~AP-1 Signaling Pathway

    doi: 10.1155/2018/6714829

    Figure Lengend Snippet: RT-q PCR amplification curve and gene expression relative quantitative analysis. (a), (b), (c), and (d): amplification curves of P110 α , P85 α , AKT, and C-JUN. (e), (f), (g), and (h): the relative mRNA expression of P110 α , P85 α , AKT, and C-JUN.

    Article Snippet: The above antibodies were as follows: primary antibodies: Rabbit anti-mouse β -actin, Rabbit anti-mouse PI3K P110α (all 1 : 100, CST, USA), Rabbit anti-mouse C-JUN antibody, Rabbit anti-mouse AKT, and Rabbit anti-mouse PI3K P85α (all 1 : 100, Abcam, USA); secondary fluorescently labeled antibodies: Donkey anti-rabbit antibody (Alexa Fluor 488) and Donkey anti-rabbit antibody (Cy3) (all 1 : 200, Jackson, USA).

    Techniques: Polymerase Chain Reaction, Amplification, Expressing