pathscan total akt1 sandwich elisa kit  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pathscan total akt1 sandwich elisa kit
    Effect of insulin, Na 2 S, and Na 2 S 4 on phosphorylation of insulin receptor β-subunit ( a ), phosphorylation of IRS-1 ( b ), <t>Akt1</t> phosphorylation at Ser 473 ( c ), and cAMP in the adipose tissue ( d ) in vivo. NaCl (control), Na 2 S (100 μmol/kg), or Na 2 S 4 (100 μmol/kg) were administered iv. 15 min before insulin (0.5 U/kg ip.). Samples of mesenteric adipose tissue were collected 30 min after insulin injection. ** p < 0.01, *** p < 0.001 vs. control group receiving only NaCl, # p < 0.05 vs. group receiving only insulin.
    Pathscan Total Akt1 Sandwich Elisa Kit, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Effect of Exogenous Hydrogen Sulfide and Polysulfide Donors on Insulin Sensitivity of the Adipose Tissue"

    Article Title: Effect of Exogenous Hydrogen Sulfide and Polysulfide Donors on Insulin Sensitivity of the Adipose Tissue

    Journal: Biomolecules

    doi: 10.3390/biom12050646

    Effect of insulin, Na 2 S, and Na 2 S 4 on phosphorylation of insulin receptor β-subunit ( a ), phosphorylation of IRS-1 ( b ), Akt1 phosphorylation at Ser 473 ( c ), and cAMP in the adipose tissue ( d ) in vivo. NaCl (control), Na 2 S (100 μmol/kg), or Na 2 S 4 (100 μmol/kg) were administered iv. 15 min before insulin (0.5 U/kg ip.). Samples of mesenteric adipose tissue were collected 30 min after insulin injection. ** p < 0.01, *** p < 0.001 vs. control group receiving only NaCl, # p < 0.05 vs. group receiving only insulin.
    Figure Legend Snippet: Effect of insulin, Na 2 S, and Na 2 S 4 on phosphorylation of insulin receptor β-subunit ( a ), phosphorylation of IRS-1 ( b ), Akt1 phosphorylation at Ser 473 ( c ), and cAMP in the adipose tissue ( d ) in vivo. NaCl (control), Na 2 S (100 μmol/kg), or Na 2 S 4 (100 μmol/kg) were administered iv. 15 min before insulin (0.5 U/kg ip.). Samples of mesenteric adipose tissue were collected 30 min after insulin injection. ** p < 0.01, *** p < 0.001 vs. control group receiving only NaCl, # p < 0.05 vs. group receiving only insulin.

    Techniques Used: In Vivo, Injection

    Effect of insulin, Na 2 S, and Na 2 S 4 on glucose uptake ( a ), glycerol release ( b ), tyrosine phosphorylation of IRβ ( c ), tyrosine phosphorylation of IRS-1 ( d ), Akt1 phosphorylation ( e ), and cAMP concentration ( f ) in mesenteric adipose tissue isolated from lean (white) and obese (black) rats. * p < 0.05, ** p < 0.0, *** p < 0.001 vs. samples not treated with insulin, Na 2 S, and Na 2 S 4 collected from the respective group of rats (lean or obese), ^ p < 0.05, ^^ p < 0.01, ^^^ p < 0.001 vs. adipose tissue samples treated in the same manner collected from lean rats, # p < 0.05 vs. samples from the respective group (lean or obese) treated with insulin alone.
    Figure Legend Snippet: Effect of insulin, Na 2 S, and Na 2 S 4 on glucose uptake ( a ), glycerol release ( b ), tyrosine phosphorylation of IRβ ( c ), tyrosine phosphorylation of IRS-1 ( d ), Akt1 phosphorylation ( e ), and cAMP concentration ( f ) in mesenteric adipose tissue isolated from lean (white) and obese (black) rats. * p < 0.05, ** p < 0.0, *** p < 0.001 vs. samples not treated with insulin, Na 2 S, and Na 2 S 4 collected from the respective group of rats (lean or obese), ^ p < 0.05, ^^ p < 0.01, ^^^ p < 0.001 vs. adipose tissue samples treated in the same manner collected from lean rats, # p < 0.05 vs. samples from the respective group (lean or obese) treated with insulin alone.

    Techniques Used: Concentration Assay, Isolation

    pathscan total akt1 sandwich elisa kit  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pathscan total akt1 sandwich elisa kit
    Effect of insulin, Na 2 S, and Na 2 S 4 on phosphorylation of insulin receptor β-subunit ( a ), phosphorylation of IRS-1 ( b ), <t>Akt1</t> phosphorylation at Ser 473 ( c ), and cAMP in the adipose tissue ( d ) in vivo. NaCl (control), Na 2 S (100 μmol/kg), or Na 2 S 4 (100 μmol/kg) were administered iv. 15 min before insulin (0.5 U/kg ip.). Samples of mesenteric adipose tissue were collected 30 min after insulin injection. ** p < 0.01, *** p < 0.001 vs. control group receiving only NaCl, # p < 0.05 vs. group receiving only insulin.
    Pathscan Total Akt1 Sandwich Elisa Kit, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pathscan total akt1 sandwich elisa kit/product/Cell Signaling Technology Inc
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    pathscan total akt1 sandwich elisa kit - by Bioz Stars, 2023-01
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    Images

    1) Product Images from "Effect of Exogenous Hydrogen Sulfide and Polysulfide Donors on Insulin Sensitivity of the Adipose Tissue"

    Article Title: Effect of Exogenous Hydrogen Sulfide and Polysulfide Donors on Insulin Sensitivity of the Adipose Tissue

    Journal: Biomolecules

    doi: 10.3390/biom12050646

    Effect of insulin, Na 2 S, and Na 2 S 4 on phosphorylation of insulin receptor β-subunit ( a ), phosphorylation of IRS-1 ( b ), Akt1 phosphorylation at Ser 473 ( c ), and cAMP in the adipose tissue ( d ) in vivo. NaCl (control), Na 2 S (100 μmol/kg), or Na 2 S 4 (100 μmol/kg) were administered iv. 15 min before insulin (0.5 U/kg ip.). Samples of mesenteric adipose tissue were collected 30 min after insulin injection. ** p < 0.01, *** p < 0.001 vs. control group receiving only NaCl, # p < 0.05 vs. group receiving only insulin.
    Figure Legend Snippet: Effect of insulin, Na 2 S, and Na 2 S 4 on phosphorylation of insulin receptor β-subunit ( a ), phosphorylation of IRS-1 ( b ), Akt1 phosphorylation at Ser 473 ( c ), and cAMP in the adipose tissue ( d ) in vivo. NaCl (control), Na 2 S (100 μmol/kg), or Na 2 S 4 (100 μmol/kg) were administered iv. 15 min before insulin (0.5 U/kg ip.). Samples of mesenteric adipose tissue were collected 30 min after insulin injection. ** p < 0.01, *** p < 0.001 vs. control group receiving only NaCl, # p < 0.05 vs. group receiving only insulin.

    Techniques Used: In Vivo, Injection

    Effect of insulin, Na 2 S, and Na 2 S 4 on glucose uptake ( a ), glycerol release ( b ), tyrosine phosphorylation of IRβ ( c ), tyrosine phosphorylation of IRS-1 ( d ), Akt1 phosphorylation ( e ), and cAMP concentration ( f ) in mesenteric adipose tissue isolated from lean (white) and obese (black) rats. * p < 0.05, ** p < 0.0, *** p < 0.001 vs. samples not treated with insulin, Na 2 S, and Na 2 S 4 collected from the respective group of rats (lean or obese), ^ p < 0.05, ^^ p < 0.01, ^^^ p < 0.001 vs. adipose tissue samples treated in the same manner collected from lean rats, # p < 0.05 vs. samples from the respective group (lean or obese) treated with insulin alone.
    Figure Legend Snippet: Effect of insulin, Na 2 S, and Na 2 S 4 on glucose uptake ( a ), glycerol release ( b ), tyrosine phosphorylation of IRβ ( c ), tyrosine phosphorylation of IRS-1 ( d ), Akt1 phosphorylation ( e ), and cAMP concentration ( f ) in mesenteric adipose tissue isolated from lean (white) and obese (black) rats. * p < 0.05, ** p < 0.0, *** p < 0.001 vs. samples not treated with insulin, Na 2 S, and Na 2 S 4 collected from the respective group of rats (lean or obese), ^ p < 0.05, ^^ p < 0.01, ^^^ p < 0.001 vs. adipose tissue samples treated in the same manner collected from lean rats, # p < 0.05 vs. samples from the respective group (lean or obese) treated with insulin alone.

    Techniques Used: Concentration Assay, Isolation

    total akt1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc total akt1
    Total Akt1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pathscan total akt1 sandwich elisa kit  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pathscan total akt1 sandwich elisa kit
    Pathscan Total Akt1 Sandwich Elisa Kit, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pathscan total akt1 sandwich elisa kit/product/Cell Signaling Technology Inc
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    pathscan total akt1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pathscan total akt1
    (A-E) Overexpression of activated AKT2 and AKT3 promotes metastasis in human A375p cells. Pan-AKT expression was analyzed by Western blot of A375p cells transfected with <t>myr-AKT1,</t> myr-AKT2 or myr-AKT3 (A). A375p cell transfected with the constructs described in (A) were analyzed by ELISA to determine phosphorylation of AKT1 (B), AKT2 (C) and AKT3 (D), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (E). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 2.1, 1.7 and 1.9 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 2.9, 1.9 and 1.8 fold respectively. (F-J) Overexpression of activated AKT2 and AKT3 promotes metastasis in mouse B16F1 cells. Pan-AKT expression was analyzed by western blot of B16 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 (F). B16 cells transfected with the constructs described in (F) were analyzed by ELISA to determine the phosphorylation of AKT1 (G), AKT2 (H) and AKT3 (I), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (J). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 1.9, 2.5 and 2 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 1.6, 2 and 1.7 fold respectively. (K, L) Knockdown of AKT2 and AKT3 inhibits metastasis in human A375sm cells. A375sm cell transfected with shRNA for AKT1, AKT2 and AKT3 were analyzed by western blot with Akt isoform-specific anti-Akt1, Akt2 and Akt3 antibodies (K); gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection in NSG mice (L). shc, vector control; sh1 and sh2, different shRNAs of AKT1, AKT2 or AKT3. β-actin as an internal control. (M) A375sm cell cotransfected with CRISPR/cas9 and HDR plasmid for specifically knockout of AKT1, AKT2, and AKT3 were analyzed by western blot with Akt isoform-specific anti-AKT1, AKT2 and AKT3 antibodies. β-tubulin as an internal control. (N) Gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection of knockout of AKT1 (Akt1KO), AKT2 (Akt2KO) and AKT3 (Akt3KO) cells in NSG mice.
    Pathscan Total Akt1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94/100 stars

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    1) Product Images from "PHLPP1 mediates melanoma metastasis suppression through repressing AKT2 activation"

    Article Title: PHLPP1 mediates melanoma metastasis suppression through repressing AKT2 activation

    Journal: Oncogene

    doi: 10.1038/s41388-017-0061-7

    (A-E) Overexpression of activated AKT2 and AKT3 promotes metastasis in human A375p cells. Pan-AKT expression was analyzed by Western blot of A375p cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 (A). A375p cell transfected with the constructs described in (A) were analyzed by ELISA to determine phosphorylation of AKT1 (B), AKT2 (C) and AKT3 (D), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (E). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 2.1, 1.7 and 1.9 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 2.9, 1.9 and 1.8 fold respectively. (F-J) Overexpression of activated AKT2 and AKT3 promotes metastasis in mouse B16F1 cells. Pan-AKT expression was analyzed by western blot of B16 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 (F). B16 cells transfected with the constructs described in (F) were analyzed by ELISA to determine the phosphorylation of AKT1 (G), AKT2 (H) and AKT3 (I), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (J). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 1.9, 2.5 and 2 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 1.6, 2 and 1.7 fold respectively. (K, L) Knockdown of AKT2 and AKT3 inhibits metastasis in human A375sm cells. A375sm cell transfected with shRNA for AKT1, AKT2 and AKT3 were analyzed by western blot with Akt isoform-specific anti-Akt1, Akt2 and Akt3 antibodies (K); gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection in NSG mice (L). shc, vector control; sh1 and sh2, different shRNAs of AKT1, AKT2 or AKT3. β-actin as an internal control. (M) A375sm cell cotransfected with CRISPR/cas9 and HDR plasmid for specifically knockout of AKT1, AKT2, and AKT3 were analyzed by western blot with Akt isoform-specific anti-AKT1, AKT2 and AKT3 antibodies. β-tubulin as an internal control. (N) Gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection of knockout of AKT1 (Akt1KO), AKT2 (Akt2KO) and AKT3 (Akt3KO) cells in NSG mice.
    Figure Legend Snippet: (A-E) Overexpression of activated AKT2 and AKT3 promotes metastasis in human A375p cells. Pan-AKT expression was analyzed by Western blot of A375p cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 (A). A375p cell transfected with the constructs described in (A) were analyzed by ELISA to determine phosphorylation of AKT1 (B), AKT2 (C) and AKT3 (D), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (E). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 2.1, 1.7 and 1.9 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 2.9, 1.9 and 1.8 fold respectively. (F-J) Overexpression of activated AKT2 and AKT3 promotes metastasis in mouse B16F1 cells. Pan-AKT expression was analyzed by western blot of B16 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 (F). B16 cells transfected with the constructs described in (F) were analyzed by ELISA to determine the phosphorylation of AKT1 (G), AKT2 (H) and AKT3 (I), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (J). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 1.9, 2.5 and 2 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 1.6, 2 and 1.7 fold respectively. (K, L) Knockdown of AKT2 and AKT3 inhibits metastasis in human A375sm cells. A375sm cell transfected with shRNA for AKT1, AKT2 and AKT3 were analyzed by western blot with Akt isoform-specific anti-Akt1, Akt2 and Akt3 antibodies (K); gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection in NSG mice (L). shc, vector control; sh1 and sh2, different shRNAs of AKT1, AKT2 or AKT3. β-actin as an internal control. (M) A375sm cell cotransfected with CRISPR/cas9 and HDR plasmid for specifically knockout of AKT1, AKT2, and AKT3 were analyzed by western blot with Akt isoform-specific anti-AKT1, AKT2 and AKT3 antibodies. β-tubulin as an internal control. (N) Gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection of knockout of AKT1 (Akt1KO), AKT2 (Akt2KO) and AKT3 (Akt3KO) cells in NSG mice.

    Techniques Used: Over Expression, Expressing, Western Blot, Transfection, Construct, Enzyme-linked Immunosorbent Assay, Injection, Plasmid Preparation, shRNA, CRISPR, Knock-Out

    (A-I) ELISA analysis of stable A375sm expressing PHLPP1, PHLPP1ΔC and PHLPP2 cells transfected with myr-Akt1, myr-AKT2 or myr-AKT3 plasmids was performed to determine protein levels of total Akt1 (A), total Akt2 (B) and total Akt3 (C), phosphorylated Akt1 (D), phosphorylated Akt2 (E), phosphorylated Akt3 (F), phosphorylated Akt-Thr-308 (G), phosphorylated Erk1/2 (H), total Erk1/2 (I); c, empty vector control; #, no statistical difference; *, p < 0.05; **, p < 0.01; ***, p < 0.001. (J) Gross pulmonary metastases of A375sm cells stably expressing PHLPP1, PHLPP1ΔC or PHLPP2 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 constructs were determined using tail vein injection in SCID mice. c, empty vector control. (K) Representative histopathology with H&E staining of lung sections with metastases from mice inoculated with stable A375sm expressing PHLPP1, PHLPP1ΔC or PHLPP2 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 constructs. c, empty vector control.
    Figure Legend Snippet: (A-I) ELISA analysis of stable A375sm expressing PHLPP1, PHLPP1ΔC and PHLPP2 cells transfected with myr-Akt1, myr-AKT2 or myr-AKT3 plasmids was performed to determine protein levels of total Akt1 (A), total Akt2 (B) and total Akt3 (C), phosphorylated Akt1 (D), phosphorylated Akt2 (E), phosphorylated Akt3 (F), phosphorylated Akt-Thr-308 (G), phosphorylated Erk1/2 (H), total Erk1/2 (I); c, empty vector control; #, no statistical difference; *, p < 0.05; **, p < 0.01; ***, p < 0.001. (J) Gross pulmonary metastases of A375sm cells stably expressing PHLPP1, PHLPP1ΔC or PHLPP2 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 constructs were determined using tail vein injection in SCID mice. c, empty vector control. (K) Representative histopathology with H&E staining of lung sections with metastases from mice inoculated with stable A375sm expressing PHLPP1, PHLPP1ΔC or PHLPP2 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 constructs. c, empty vector control.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Expressing, Transfection, Plasmid Preparation, Stable Transfection, Construct, Injection, Histopathology, Staining

    (A) Whole cell lysates from A375sm cells and stable A375p-myr-AKT2 (A375p Akt2) cells treated with various doses of MK2206 were analyzed by western blot. (B-E) ELISA analysis of A375sm and stable A375p myr-AKT2 cells treated with different doses of MK2206 was performed to determine protein levels of phosphorylated AKT1 (B), phosphorylated AKT2 (C), phosphorylated AKT3 (D), and phosphorylated AKT-Thr-308 (E). #, no statistical difference; *, p < 0.05; **, p < 0.01; ***, p < 0.001. (F) Gross pulmonary metastases from mice treated with MK2206 or from pretreated cultured A375p Akt2 cells with either 12 nM or 65 nM MK2206 for 36 hours in cell culture (green color). Mice harboring A375p cells stably transfected with the myr-AKT2 expression vector (A375p Akt2) were treated with two different doses of MK2206 immediately (black color) or 7 days after cells injection (red color). After pretreatment with MK2206 for 36 hours, A375p Akt2 cells were injected into NSG mice by tail vein. c, mock control. (G-H) Tumor growth curve (G) and tumor weight (H) of A375sm cells in xenograft NSG mice with/without treatment of MK2206. (I) Representative histopathology (H&E staining) or immunohistochemical staining in metastases derived from mice bearing A375sm cells treated with MK2206. H&E, hematoxylin and eosin staining; t-Akt, immunohistochemical staining with the anti-AKT antibody; p-Akt, immunohistochemical staining with anti-p-AKT antibody 20X. (J) Immunoreactivity score of total AKT (T-Akt) and phosphorylated AKT (p-Akt) expression in metastases from mice treated with MK2206. Quantitative scores analyzed using ImageScope V10.0 software from Aperio Technologies, presenting the percentage of cells in strongly positive, positive, weakly positive and negative for immunohistochemical staining with an anti-AKT or phosphorylated AKT antibody. (K-L) Whole tissue lysates from tumors in mice treated with MK2206 were analyzed by ELISA to determine protein levels of phosphorylated AKT1 (p-Akt1), phosphorylated AKT2 (p-Akt2), phosphorylated AKT3 (p-Akt3), phosphorylated AKT-Thr-308 (p-AktThr308), and phosphorylated Erk1/2 (p-Erk1/2), total Erk1/2 (T-Erk1/2), total AKT (T-Akt1), total AKT2 (T-Akt2) and total AKT3 (T-Akt3).
    Figure Legend Snippet: (A) Whole cell lysates from A375sm cells and stable A375p-myr-AKT2 (A375p Akt2) cells treated with various doses of MK2206 were analyzed by western blot. (B-E) ELISA analysis of A375sm and stable A375p myr-AKT2 cells treated with different doses of MK2206 was performed to determine protein levels of phosphorylated AKT1 (B), phosphorylated AKT2 (C), phosphorylated AKT3 (D), and phosphorylated AKT-Thr-308 (E). #, no statistical difference; *, p < 0.05; **, p < 0.01; ***, p < 0.001. (F) Gross pulmonary metastases from mice treated with MK2206 or from pretreated cultured A375p Akt2 cells with either 12 nM or 65 nM MK2206 for 36 hours in cell culture (green color). Mice harboring A375p cells stably transfected with the myr-AKT2 expression vector (A375p Akt2) were treated with two different doses of MK2206 immediately (black color) or 7 days after cells injection (red color). After pretreatment with MK2206 for 36 hours, A375p Akt2 cells were injected into NSG mice by tail vein. c, mock control. (G-H) Tumor growth curve (G) and tumor weight (H) of A375sm cells in xenograft NSG mice with/without treatment of MK2206. (I) Representative histopathology (H&E staining) or immunohistochemical staining in metastases derived from mice bearing A375sm cells treated with MK2206. H&E, hematoxylin and eosin staining; t-Akt, immunohistochemical staining with the anti-AKT antibody; p-Akt, immunohistochemical staining with anti-p-AKT antibody 20X. (J) Immunoreactivity score of total AKT (T-Akt) and phosphorylated AKT (p-Akt) expression in metastases from mice treated with MK2206. Quantitative scores analyzed using ImageScope V10.0 software from Aperio Technologies, presenting the percentage of cells in strongly positive, positive, weakly positive and negative for immunohistochemical staining with an anti-AKT or phosphorylated AKT antibody. (K-L) Whole tissue lysates from tumors in mice treated with MK2206 were analyzed by ELISA to determine protein levels of phosphorylated AKT1 (p-Akt1), phosphorylated AKT2 (p-Akt2), phosphorylated AKT3 (p-Akt3), phosphorylated AKT-Thr-308 (p-AktThr308), and phosphorylated Erk1/2 (p-Erk1/2), total Erk1/2 (T-Erk1/2), total AKT (T-Akt1), total AKT2 (T-Akt2) and total AKT3 (T-Akt3).

    Techniques Used: Western Blot, Enzyme-linked Immunosorbent Assay, Cell Culture, Stable Transfection, Transfection, Expressing, Plasmid Preparation, Injection, Histopathology, Staining, Immunohistochemical staining, Derivative Assay, Software

    human pathscan elisa kits  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc human pathscan elisa kits
    Effects of BEV + RES on Notch signaling. Bar graph depicts the relative mRNA expression levels of notch 4 and dll 4 in with respect to mRNA levels of gapdh in untreated ARPE-19 cells and those treated with BEV, RES and BEV + RES ( A ). Graphical representation of quantified mean fluorescent intensity of immunofluorescent images for NOTCH 4 and DLL 4 are shown ( B ). Representative immunofluorscent images showing positivity for NOTCH 4 and DLL4 in untreated and BEV, RES, BEV + RES treated ARPE-19 cells ( C ). Representative western blots of NOTCH 4, DLL4 and the downstream target HES 1 in untreated and treated ARPE-19 cells ( D ). Graphical representation of the densitometric analysis of western blot results with respect to the levels of GAPDH is shown ( E ). Graphical representation of <t>PathScan</t> ® <t>ELISA</t> results of untreated and cells treated with BEV, RES and BEV + RES ( F ). Representative Western blot showing phosphorylated and total MEK1/2 (i) and p44/42 MAPK (ii) ( G ). Statistical analysis was performed using student’s t-test (*P < 0.05,**P < 0.01, ***P < 0.005) (n ≥ 3). Scale bar = 5 µm.
    Human Pathscan Elisa Kits, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human pathscan elisa kits/product/Cell Signaling Technology Inc
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    1) Product Images from "Resveratrol reverses the adverse effects of bevacizumab on cultured ARPE-19 cells"

    Article Title: Resveratrol reverses the adverse effects of bevacizumab on cultured ARPE-19 cells

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-12496-z

    Effects of BEV + RES on Notch signaling. Bar graph depicts the relative mRNA expression levels of notch 4 and dll 4 in with respect to mRNA levels of gapdh in untreated ARPE-19 cells and those treated with BEV, RES and BEV + RES ( A ). Graphical representation of quantified mean fluorescent intensity of immunofluorescent images for NOTCH 4 and DLL 4 are shown ( B ). Representative immunofluorscent images showing positivity for NOTCH 4 and DLL4 in untreated and BEV, RES, BEV + RES treated ARPE-19 cells ( C ). Representative western blots of NOTCH 4, DLL4 and the downstream target HES 1 in untreated and treated ARPE-19 cells ( D ). Graphical representation of the densitometric analysis of western blot results with respect to the levels of GAPDH is shown ( E ). Graphical representation of PathScan ® ELISA results of untreated and cells treated with BEV, RES and BEV + RES ( F ). Representative Western blot showing phosphorylated and total MEK1/2 (i) and p44/42 MAPK (ii) ( G ). Statistical analysis was performed using student’s t-test (*P < 0.05,**P < 0.01, ***P < 0.005) (n ≥ 3). Scale bar = 5 µm.
    Figure Legend Snippet: Effects of BEV + RES on Notch signaling. Bar graph depicts the relative mRNA expression levels of notch 4 and dll 4 in with respect to mRNA levels of gapdh in untreated ARPE-19 cells and those treated with BEV, RES and BEV + RES ( A ). Graphical representation of quantified mean fluorescent intensity of immunofluorescent images for NOTCH 4 and DLL 4 are shown ( B ). Representative immunofluorscent images showing positivity for NOTCH 4 and DLL4 in untreated and BEV, RES, BEV + RES treated ARPE-19 cells ( C ). Representative western blots of NOTCH 4, DLL4 and the downstream target HES 1 in untreated and treated ARPE-19 cells ( D ). Graphical representation of the densitometric analysis of western blot results with respect to the levels of GAPDH is shown ( E ). Graphical representation of PathScan ® ELISA results of untreated and cells treated with BEV, RES and BEV + RES ( F ). Representative Western blot showing phosphorylated and total MEK1/2 (i) and p44/42 MAPK (ii) ( G ). Statistical analysis was performed using student’s t-test (*P < 0.05,**P < 0.01, ***P < 0.005) (n ≥ 3). Scale bar = 5 µm.

    Techniques Used: Expressing, Western Blot, Enzyme-linked Immunosorbent Assay

    horseradish peroxidase conjugated goat anti rabbit secondary antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pathscan total akt1 sandwich elisa kit
    Effect of insulin, Na 2 S, and Na 2 S 4 on phosphorylation of insulin receptor β-subunit ( a ), phosphorylation of IRS-1 ( b ), <t>Akt1</t> phosphorylation at Ser 473 ( c ), and cAMP in the adipose tissue ( d ) in vivo. NaCl (control), Na 2 S (100 μmol/kg), or Na 2 S 4 (100 μmol/kg) were administered iv. 15 min before insulin (0.5 U/kg ip.). Samples of mesenteric adipose tissue were collected 30 min after insulin injection. ** p < 0.01, *** p < 0.001 vs. control group receiving only NaCl, # p < 0.05 vs. group receiving only insulin.
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    Effect of insulin, Na 2 S, and Na 2 S 4 on phosphorylation of insulin receptor β-subunit ( a ), phosphorylation of IRS-1 ( b ), <t>Akt1</t> phosphorylation at Ser 473 ( c ), and cAMP in the adipose tissue ( d ) in vivo. NaCl (control), Na 2 S (100 μmol/kg), or Na 2 S 4 (100 μmol/kg) were administered iv. 15 min before insulin (0.5 U/kg ip.). Samples of mesenteric adipose tissue were collected 30 min after insulin injection. ** p < 0.01, *** p < 0.001 vs. control group receiving only NaCl, # p < 0.05 vs. group receiving only insulin.
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    (A-E) Overexpression of activated AKT2 and AKT3 promotes metastasis in human A375p cells. Pan-AKT expression was analyzed by Western blot of A375p cells transfected with <t>myr-AKT1,</t> myr-AKT2 or myr-AKT3 (A). A375p cell transfected with the constructs described in (A) were analyzed by ELISA to determine phosphorylation of AKT1 (B), AKT2 (C) and AKT3 (D), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (E). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 2.1, 1.7 and 1.9 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 2.9, 1.9 and 1.8 fold respectively. (F-J) Overexpression of activated AKT2 and AKT3 promotes metastasis in mouse B16F1 cells. Pan-AKT expression was analyzed by western blot of B16 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 (F). B16 cells transfected with the constructs described in (F) were analyzed by ELISA to determine the phosphorylation of AKT1 (G), AKT2 (H) and AKT3 (I), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (J). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 1.9, 2.5 and 2 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 1.6, 2 and 1.7 fold respectively. (K, L) Knockdown of AKT2 and AKT3 inhibits metastasis in human A375sm cells. A375sm cell transfected with shRNA for AKT1, AKT2 and AKT3 were analyzed by western blot with Akt isoform-specific anti-Akt1, Akt2 and Akt3 antibodies (K); gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection in NSG mice (L). shc, vector control; sh1 and sh2, different shRNAs of AKT1, AKT2 or AKT3. β-actin as an internal control. (M) A375sm cell cotransfected with CRISPR/cas9 and HDR plasmid for specifically knockout of AKT1, AKT2, and AKT3 were analyzed by western blot with Akt isoform-specific anti-AKT1, AKT2 and AKT3 antibodies. β-tubulin as an internal control. (N) Gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection of knockout of AKT1 (Akt1KO), AKT2 (Akt2KO) and AKT3 (Akt3KO) cells in NSG mice.
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    Effects of BEV + RES on Notch signaling. Bar graph depicts the relative mRNA expression levels of notch 4 and dll 4 in with respect to mRNA levels of gapdh in untreated ARPE-19 cells and those treated with BEV, RES and BEV + RES ( A ). Graphical representation of quantified mean fluorescent intensity of immunofluorescent images for NOTCH 4 and DLL 4 are shown ( B ). Representative immunofluorscent images showing positivity for NOTCH 4 and DLL4 in untreated and BEV, RES, BEV + RES treated ARPE-19 cells ( C ). Representative western blots of NOTCH 4, DLL4 and the downstream target HES 1 in untreated and treated ARPE-19 cells ( D ). Graphical representation of the densitometric analysis of western blot results with respect to the levels of GAPDH is shown ( E ). Graphical representation of <t>PathScan</t> ® <t>ELISA</t> results of untreated and cells treated with BEV, RES and BEV + RES ( F ). Representative Western blot showing phosphorylated and total MEK1/2 (i) and p44/42 MAPK (ii) ( G ). Statistical analysis was performed using student’s t-test (*P < 0.05,**P < 0.01, ***P < 0.005) (n ≥ 3). Scale bar = 5 µm.
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    Effects of BEV + RES on Notch signaling. Bar graph depicts the relative mRNA expression levels of notch 4 and dll 4 in with respect to mRNA levels of gapdh in untreated ARPE-19 cells and those treated with BEV, RES and BEV + RES ( A ). Graphical representation of quantified mean fluorescent intensity of immunofluorescent images for NOTCH 4 and DLL 4 are shown ( B ). Representative immunofluorscent images showing positivity for NOTCH 4 and DLL4 in untreated and BEV, RES, BEV + RES treated ARPE-19 cells ( C ). Representative western blots of NOTCH 4, DLL4 and the downstream target HES 1 in untreated and treated ARPE-19 cells ( D ). Graphical representation of the densitometric analysis of western blot results with respect to the levels of GAPDH is shown ( E ). Graphical representation of <t>PathScan</t> ® <t>ELISA</t> results of untreated and cells treated with BEV, RES and BEV + RES ( F ). Representative Western blot showing phosphorylated and total MEK1/2 (i) and p44/42 MAPK (ii) ( G ). Statistical analysis was performed using student’s t-test (*P < 0.05,**P < 0.01, ***P < 0.005) (n ≥ 3). Scale bar = 5 µm.
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    Effects of BEV + RES on Notch signaling. Bar graph depicts the relative mRNA expression levels of notch 4 and dll 4 in with respect to mRNA levels of gapdh in untreated ARPE-19 cells and those treated with BEV, RES and BEV + RES ( A ). Graphical representation of quantified mean fluorescent intensity of immunofluorescent images for NOTCH 4 and DLL 4 are shown ( B ). Representative immunofluorscent images showing positivity for NOTCH 4 and DLL4 in untreated and BEV, RES, BEV + RES treated ARPE-19 cells ( C ). Representative western blots of NOTCH 4, DLL4 and the downstream target HES 1 in untreated and treated ARPE-19 cells ( D ). Graphical representation of the densitometric analysis of western blot results with respect to the levels of GAPDH is shown ( E ). Graphical representation of <t>PathScan</t> ® <t>ELISA</t> results of untreated and cells treated with BEV, RES and BEV + RES ( F ). Representative Western blot showing phosphorylated and total MEK1/2 (i) and p44/42 MAPK (ii) ( G ). Statistical analysis was performed using student’s t-test (*P < 0.05,**P < 0.01, ***P < 0.005) (n ≥ 3). Scale bar = 5 µm.
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    Effects of BEV + RES on Notch signaling. Bar graph depicts the relative mRNA expression levels of notch 4 and dll 4 in with respect to mRNA levels of gapdh in untreated ARPE-19 cells and those treated with BEV, RES and BEV + RES ( A ). Graphical representation of quantified mean fluorescent intensity of immunofluorescent images for NOTCH 4 and DLL 4 are shown ( B ). Representative immunofluorscent images showing positivity for NOTCH 4 and DLL4 in untreated and BEV, RES, BEV + RES treated ARPE-19 cells ( C ). Representative western blots of NOTCH 4, DLL4 and the downstream target HES 1 in untreated and treated ARPE-19 cells ( D ). Graphical representation of the densitometric analysis of western blot results with respect to the levels of GAPDH is shown ( E ). Graphical representation of <t>PathScan</t> ® <t>ELISA</t> results of untreated and cells treated with BEV, RES and BEV + RES ( F ). Representative Western blot showing phosphorylated and total MEK1/2 (i) and p44/42 MAPK (ii) ( G ). Statistical analysis was performed using student’s t-test (*P < 0.05,**P < 0.01, ***P < 0.005) (n ≥ 3). Scale bar = 5 µm.
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    Effects of BEV + RES on Notch signaling. Bar graph depicts the relative mRNA expression levels of notch 4 and dll 4 in with respect to mRNA levels of gapdh in untreated ARPE-19 cells and those treated with BEV, RES and BEV + RES ( A ). Graphical representation of quantified mean fluorescent intensity of immunofluorescent images for NOTCH 4 and DLL 4 are shown ( B ). Representative immunofluorscent images showing positivity for NOTCH 4 and DLL4 in untreated and BEV, RES, BEV + RES treated ARPE-19 cells ( C ). Representative western blots of NOTCH 4, DLL4 and the downstream target HES 1 in untreated and treated ARPE-19 cells ( D ). Graphical representation of the densitometric analysis of western blot results with respect to the levels of GAPDH is shown ( E ). Graphical representation of <t>PathScan</t> ® <t>ELISA</t> results of untreated and cells treated with BEV, RES and BEV + RES ( F ). Representative Western blot showing phosphorylated and total MEK1/2 (i) and p44/42 MAPK (ii) ( G ). Statistical analysis was performed using student’s t-test (*P < 0.05,**P < 0.01, ***P < 0.005) (n ≥ 3). Scale bar = 5 µm.
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    Image Search Results


    Effect of insulin, Na 2 S, and Na 2 S 4 on phosphorylation of insulin receptor β-subunit ( a ), phosphorylation of IRS-1 ( b ), Akt1 phosphorylation at Ser 473 ( c ), and cAMP in the adipose tissue ( d ) in vivo. NaCl (control), Na 2 S (100 μmol/kg), or Na 2 S 4 (100 μmol/kg) were administered iv. 15 min before insulin (0.5 U/kg ip.). Samples of mesenteric adipose tissue were collected 30 min after insulin injection. ** p < 0.01, *** p < 0.001 vs. control group receiving only NaCl, # p < 0.05 vs. group receiving only insulin.

    Journal: Biomolecules

    Article Title: Effect of Exogenous Hydrogen Sulfide and Polysulfide Donors on Insulin Sensitivity of the Adipose Tissue

    doi: 10.3390/biom12050646

    Figure Lengend Snippet: Effect of insulin, Na 2 S, and Na 2 S 4 on phosphorylation of insulin receptor β-subunit ( a ), phosphorylation of IRS-1 ( b ), Akt1 phosphorylation at Ser 473 ( c ), and cAMP in the adipose tissue ( d ) in vivo. NaCl (control), Na 2 S (100 μmol/kg), or Na 2 S 4 (100 μmol/kg) were administered iv. 15 min before insulin (0.5 U/kg ip.). Samples of mesenteric adipose tissue were collected 30 min after insulin injection. ** p < 0.01, *** p < 0.001 vs. control group receiving only NaCl, # p < 0.05 vs. group receiving only insulin.

    Article Snippet: We measured total Akt and Akt phosphorylated at Ser 473 using Cell Signaling Technology PathScan Total Akt1 Sandwich ELISA Kit (Kit #7170) and PathScan Phospho-Akt1 (Ser473) Sandwich ELISA Kit (#7160), respectively.

    Techniques: In Vivo, Injection

    Effect of insulin, Na 2 S, and Na 2 S 4 on glucose uptake ( a ), glycerol release ( b ), tyrosine phosphorylation of IRβ ( c ), tyrosine phosphorylation of IRS-1 ( d ), Akt1 phosphorylation ( e ), and cAMP concentration ( f ) in mesenteric adipose tissue isolated from lean (white) and obese (black) rats. * p < 0.05, ** p < 0.0, *** p < 0.001 vs. samples not treated with insulin, Na 2 S, and Na 2 S 4 collected from the respective group of rats (lean or obese), ^ p < 0.05, ^^ p < 0.01, ^^^ p < 0.001 vs. adipose tissue samples treated in the same manner collected from lean rats, # p < 0.05 vs. samples from the respective group (lean or obese) treated with insulin alone.

    Journal: Biomolecules

    Article Title: Effect of Exogenous Hydrogen Sulfide and Polysulfide Donors on Insulin Sensitivity of the Adipose Tissue

    doi: 10.3390/biom12050646

    Figure Lengend Snippet: Effect of insulin, Na 2 S, and Na 2 S 4 on glucose uptake ( a ), glycerol release ( b ), tyrosine phosphorylation of IRβ ( c ), tyrosine phosphorylation of IRS-1 ( d ), Akt1 phosphorylation ( e ), and cAMP concentration ( f ) in mesenteric adipose tissue isolated from lean (white) and obese (black) rats. * p < 0.05, ** p < 0.0, *** p < 0.001 vs. samples not treated with insulin, Na 2 S, and Na 2 S 4 collected from the respective group of rats (lean or obese), ^ p < 0.05, ^^ p < 0.01, ^^^ p < 0.001 vs. adipose tissue samples treated in the same manner collected from lean rats, # p < 0.05 vs. samples from the respective group (lean or obese) treated with insulin alone.

    Article Snippet: We measured total Akt and Akt phosphorylated at Ser 473 using Cell Signaling Technology PathScan Total Akt1 Sandwich ELISA Kit (Kit #7170) and PathScan Phospho-Akt1 (Ser473) Sandwich ELISA Kit (#7160), respectively.

    Techniques: Concentration Assay, Isolation

    (A-E) Overexpression of activated AKT2 and AKT3 promotes metastasis in human A375p cells. Pan-AKT expression was analyzed by Western blot of A375p cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 (A). A375p cell transfected with the constructs described in (A) were analyzed by ELISA to determine phosphorylation of AKT1 (B), AKT2 (C) and AKT3 (D), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (E). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 2.1, 1.7 and 1.9 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 2.9, 1.9 and 1.8 fold respectively. (F-J) Overexpression of activated AKT2 and AKT3 promotes metastasis in mouse B16F1 cells. Pan-AKT expression was analyzed by western blot of B16 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 (F). B16 cells transfected with the constructs described in (F) were analyzed by ELISA to determine the phosphorylation of AKT1 (G), AKT2 (H) and AKT3 (I), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (J). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 1.9, 2.5 and 2 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 1.6, 2 and 1.7 fold respectively. (K, L) Knockdown of AKT2 and AKT3 inhibits metastasis in human A375sm cells. A375sm cell transfected with shRNA for AKT1, AKT2 and AKT3 were analyzed by western blot with Akt isoform-specific anti-Akt1, Akt2 and Akt3 antibodies (K); gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection in NSG mice (L). shc, vector control; sh1 and sh2, different shRNAs of AKT1, AKT2 or AKT3. β-actin as an internal control. (M) A375sm cell cotransfected with CRISPR/cas9 and HDR plasmid for specifically knockout of AKT1, AKT2, and AKT3 were analyzed by western blot with Akt isoform-specific anti-AKT1, AKT2 and AKT3 antibodies. β-tubulin as an internal control. (N) Gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection of knockout of AKT1 (Akt1KO), AKT2 (Akt2KO) and AKT3 (Akt3KO) cells in NSG mice.

    Journal: Oncogene

    Article Title: PHLPP1 mediates melanoma metastasis suppression through repressing AKT2 activation

    doi: 10.1038/s41388-017-0061-7

    Figure Lengend Snippet: (A-E) Overexpression of activated AKT2 and AKT3 promotes metastasis in human A375p cells. Pan-AKT expression was analyzed by Western blot of A375p cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 (A). A375p cell transfected with the constructs described in (A) were analyzed by ELISA to determine phosphorylation of AKT1 (B), AKT2 (C) and AKT3 (D), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (E). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 2.1, 1.7 and 1.9 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 2.9, 1.9 and 1.8 fold respectively. (F-J) Overexpression of activated AKT2 and AKT3 promotes metastasis in mouse B16F1 cells. Pan-AKT expression was analyzed by western blot of B16 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 (F). B16 cells transfected with the constructs described in (F) were analyzed by ELISA to determine the phosphorylation of AKT1 (G), AKT2 (H) and AKT3 (I), and by experimental metastasis assay using tail vein injection to determine the gross pulmonary metastasis (J). c, empty vector control. Compared to vector control, total of Akt1, Akt2 and Akt3 were increased by 1.9, 2.5 and 2 fold respectively; phosphorylated Akt1, Akt2 and Akt3 were significantly enhanced by 1.6, 2 and 1.7 fold respectively. (K, L) Knockdown of AKT2 and AKT3 inhibits metastasis in human A375sm cells. A375sm cell transfected with shRNA for AKT1, AKT2 and AKT3 were analyzed by western blot with Akt isoform-specific anti-Akt1, Akt2 and Akt3 antibodies (K); gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection in NSG mice (L). shc, vector control; sh1 and sh2, different shRNAs of AKT1, AKT2 or AKT3. β-actin as an internal control. (M) A375sm cell cotransfected with CRISPR/cas9 and HDR plasmid for specifically knockout of AKT1, AKT2, and AKT3 were analyzed by western blot with Akt isoform-specific anti-AKT1, AKT2 and AKT3 antibodies. β-tubulin as an internal control. (N) Gross pulmonary metastasis was determined by experimental metastasis assay using tail vein injection of knockout of AKT1 (Akt1KO), AKT2 (Akt2KO) and AKT3 (Akt3KO) cells in NSG mice.

    Article Snippet: Protein level of phospho-AKT 1 (Ser473), phospho-AKT 2(Ser474), phospho-AKT 3(Ser472), phospho-AKT (Thr308), total-AKT1, total-AKT2, total-AKT3, phospho-ERK 1/2 (Thr202/Tyr204) and total-ERK1/2 were measured by ELISA assays using PathScan® Phospho-AKT1 (Ser473), PathScan® Phospho -Akt2 (Ser474), PathScan® Phospho –Akt3 (Ser472), PathScan® Phospho -Akt (Thr308), PathScan® Total Akt1, PathScan® Total Akt2, PathScan® Total Akt3, PathScan® Phospho –Erk1/2 (Thr202/Tyr204) and PathScan® Total Erk1/2 Sandwich ELISA Kits purchased from Cell Signaling (Danvers, MA, USA).

    Techniques: Over Expression, Expressing, Western Blot, Transfection, Construct, Enzyme-linked Immunosorbent Assay, Injection, Plasmid Preparation, shRNA, CRISPR, Knock-Out

    (A-I) ELISA analysis of stable A375sm expressing PHLPP1, PHLPP1ΔC and PHLPP2 cells transfected with myr-Akt1, myr-AKT2 or myr-AKT3 plasmids was performed to determine protein levels of total Akt1 (A), total Akt2 (B) and total Akt3 (C), phosphorylated Akt1 (D), phosphorylated Akt2 (E), phosphorylated Akt3 (F), phosphorylated Akt-Thr-308 (G), phosphorylated Erk1/2 (H), total Erk1/2 (I); c, empty vector control; #, no statistical difference; *, p < 0.05; **, p < 0.01; ***, p < 0.001. (J) Gross pulmonary metastases of A375sm cells stably expressing PHLPP1, PHLPP1ΔC or PHLPP2 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 constructs were determined using tail vein injection in SCID mice. c, empty vector control. (K) Representative histopathology with H&E staining of lung sections with metastases from mice inoculated with stable A375sm expressing PHLPP1, PHLPP1ΔC or PHLPP2 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 constructs. c, empty vector control.

    Journal: Oncogene

    Article Title: PHLPP1 mediates melanoma metastasis suppression through repressing AKT2 activation

    doi: 10.1038/s41388-017-0061-7

    Figure Lengend Snippet: (A-I) ELISA analysis of stable A375sm expressing PHLPP1, PHLPP1ΔC and PHLPP2 cells transfected with myr-Akt1, myr-AKT2 or myr-AKT3 plasmids was performed to determine protein levels of total Akt1 (A), total Akt2 (B) and total Akt3 (C), phosphorylated Akt1 (D), phosphorylated Akt2 (E), phosphorylated Akt3 (F), phosphorylated Akt-Thr-308 (G), phosphorylated Erk1/2 (H), total Erk1/2 (I); c, empty vector control; #, no statistical difference; *, p < 0.05; **, p < 0.01; ***, p < 0.001. (J) Gross pulmonary metastases of A375sm cells stably expressing PHLPP1, PHLPP1ΔC or PHLPP2 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 constructs were determined using tail vein injection in SCID mice. c, empty vector control. (K) Representative histopathology with H&E staining of lung sections with metastases from mice inoculated with stable A375sm expressing PHLPP1, PHLPP1ΔC or PHLPP2 cells transfected with myr-AKT1, myr-AKT2 or myr-AKT3 constructs. c, empty vector control.

    Article Snippet: Protein level of phospho-AKT 1 (Ser473), phospho-AKT 2(Ser474), phospho-AKT 3(Ser472), phospho-AKT (Thr308), total-AKT1, total-AKT2, total-AKT3, phospho-ERK 1/2 (Thr202/Tyr204) and total-ERK1/2 were measured by ELISA assays using PathScan® Phospho-AKT1 (Ser473), PathScan® Phospho -Akt2 (Ser474), PathScan® Phospho –Akt3 (Ser472), PathScan® Phospho -Akt (Thr308), PathScan® Total Akt1, PathScan® Total Akt2, PathScan® Total Akt3, PathScan® Phospho –Erk1/2 (Thr202/Tyr204) and PathScan® Total Erk1/2 Sandwich ELISA Kits purchased from Cell Signaling (Danvers, MA, USA).

    Techniques: Enzyme-linked Immunosorbent Assay, Expressing, Transfection, Plasmid Preparation, Stable Transfection, Construct, Injection, Histopathology, Staining

    (A) Whole cell lysates from A375sm cells and stable A375p-myr-AKT2 (A375p Akt2) cells treated with various doses of MK2206 were analyzed by western blot. (B-E) ELISA analysis of A375sm and stable A375p myr-AKT2 cells treated with different doses of MK2206 was performed to determine protein levels of phosphorylated AKT1 (B), phosphorylated AKT2 (C), phosphorylated AKT3 (D), and phosphorylated AKT-Thr-308 (E). #, no statistical difference; *, p < 0.05; **, p < 0.01; ***, p < 0.001. (F) Gross pulmonary metastases from mice treated with MK2206 or from pretreated cultured A375p Akt2 cells with either 12 nM or 65 nM MK2206 for 36 hours in cell culture (green color). Mice harboring A375p cells stably transfected with the myr-AKT2 expression vector (A375p Akt2) were treated with two different doses of MK2206 immediately (black color) or 7 days after cells injection (red color). After pretreatment with MK2206 for 36 hours, A375p Akt2 cells were injected into NSG mice by tail vein. c, mock control. (G-H) Tumor growth curve (G) and tumor weight (H) of A375sm cells in xenograft NSG mice with/without treatment of MK2206. (I) Representative histopathology (H&E staining) or immunohistochemical staining in metastases derived from mice bearing A375sm cells treated with MK2206. H&E, hematoxylin and eosin staining; t-Akt, immunohistochemical staining with the anti-AKT antibody; p-Akt, immunohistochemical staining with anti-p-AKT antibody 20X. (J) Immunoreactivity score of total AKT (T-Akt) and phosphorylated AKT (p-Akt) expression in metastases from mice treated with MK2206. Quantitative scores analyzed using ImageScope V10.0 software from Aperio Technologies, presenting the percentage of cells in strongly positive, positive, weakly positive and negative for immunohistochemical staining with an anti-AKT or phosphorylated AKT antibody. (K-L) Whole tissue lysates from tumors in mice treated with MK2206 were analyzed by ELISA to determine protein levels of phosphorylated AKT1 (p-Akt1), phosphorylated AKT2 (p-Akt2), phosphorylated AKT3 (p-Akt3), phosphorylated AKT-Thr-308 (p-AktThr308), and phosphorylated Erk1/2 (p-Erk1/2), total Erk1/2 (T-Erk1/2), total AKT (T-Akt1), total AKT2 (T-Akt2) and total AKT3 (T-Akt3).

    Journal: Oncogene

    Article Title: PHLPP1 mediates melanoma metastasis suppression through repressing AKT2 activation

    doi: 10.1038/s41388-017-0061-7

    Figure Lengend Snippet: (A) Whole cell lysates from A375sm cells and stable A375p-myr-AKT2 (A375p Akt2) cells treated with various doses of MK2206 were analyzed by western blot. (B-E) ELISA analysis of A375sm and stable A375p myr-AKT2 cells treated with different doses of MK2206 was performed to determine protein levels of phosphorylated AKT1 (B), phosphorylated AKT2 (C), phosphorylated AKT3 (D), and phosphorylated AKT-Thr-308 (E). #, no statistical difference; *, p < 0.05; **, p < 0.01; ***, p < 0.001. (F) Gross pulmonary metastases from mice treated with MK2206 or from pretreated cultured A375p Akt2 cells with either 12 nM or 65 nM MK2206 for 36 hours in cell culture (green color). Mice harboring A375p cells stably transfected with the myr-AKT2 expression vector (A375p Akt2) were treated with two different doses of MK2206 immediately (black color) or 7 days after cells injection (red color). After pretreatment with MK2206 for 36 hours, A375p Akt2 cells were injected into NSG mice by tail vein. c, mock control. (G-H) Tumor growth curve (G) and tumor weight (H) of A375sm cells in xenograft NSG mice with/without treatment of MK2206. (I) Representative histopathology (H&E staining) or immunohistochemical staining in metastases derived from mice bearing A375sm cells treated with MK2206. H&E, hematoxylin and eosin staining; t-Akt, immunohistochemical staining with the anti-AKT antibody; p-Akt, immunohistochemical staining with anti-p-AKT antibody 20X. (J) Immunoreactivity score of total AKT (T-Akt) and phosphorylated AKT (p-Akt) expression in metastases from mice treated with MK2206. Quantitative scores analyzed using ImageScope V10.0 software from Aperio Technologies, presenting the percentage of cells in strongly positive, positive, weakly positive and negative for immunohistochemical staining with an anti-AKT or phosphorylated AKT antibody. (K-L) Whole tissue lysates from tumors in mice treated with MK2206 were analyzed by ELISA to determine protein levels of phosphorylated AKT1 (p-Akt1), phosphorylated AKT2 (p-Akt2), phosphorylated AKT3 (p-Akt3), phosphorylated AKT-Thr-308 (p-AktThr308), and phosphorylated Erk1/2 (p-Erk1/2), total Erk1/2 (T-Erk1/2), total AKT (T-Akt1), total AKT2 (T-Akt2) and total AKT3 (T-Akt3).

    Article Snippet: Protein level of phospho-AKT 1 (Ser473), phospho-AKT 2(Ser474), phospho-AKT 3(Ser472), phospho-AKT (Thr308), total-AKT1, total-AKT2, total-AKT3, phospho-ERK 1/2 (Thr202/Tyr204) and total-ERK1/2 were measured by ELISA assays using PathScan® Phospho-AKT1 (Ser473), PathScan® Phospho -Akt2 (Ser474), PathScan® Phospho –Akt3 (Ser472), PathScan® Phospho -Akt (Thr308), PathScan® Total Akt1, PathScan® Total Akt2, PathScan® Total Akt3, PathScan® Phospho –Erk1/2 (Thr202/Tyr204) and PathScan® Total Erk1/2 Sandwich ELISA Kits purchased from Cell Signaling (Danvers, MA, USA).

    Techniques: Western Blot, Enzyme-linked Immunosorbent Assay, Cell Culture, Stable Transfection, Transfection, Expressing, Plasmid Preparation, Injection, Histopathology, Staining, Immunohistochemical staining, Derivative Assay, Software

    Effects of BEV + RES on Notch signaling. Bar graph depicts the relative mRNA expression levels of notch 4 and dll 4 in with respect to mRNA levels of gapdh in untreated ARPE-19 cells and those treated with BEV, RES and BEV + RES ( A ). Graphical representation of quantified mean fluorescent intensity of immunofluorescent images for NOTCH 4 and DLL 4 are shown ( B ). Representative immunofluorscent images showing positivity for NOTCH 4 and DLL4 in untreated and BEV, RES, BEV + RES treated ARPE-19 cells ( C ). Representative western blots of NOTCH 4, DLL4 and the downstream target HES 1 in untreated and treated ARPE-19 cells ( D ). Graphical representation of the densitometric analysis of western blot results with respect to the levels of GAPDH is shown ( E ). Graphical representation of PathScan ® ELISA results of untreated and cells treated with BEV, RES and BEV + RES ( F ). Representative Western blot showing phosphorylated and total MEK1/2 (i) and p44/42 MAPK (ii) ( G ). Statistical analysis was performed using student’s t-test (*P < 0.05,**P < 0.01, ***P < 0.005) (n ≥ 3). Scale bar = 5 µm.

    Journal: Scientific Reports

    Article Title: Resveratrol reverses the adverse effects of bevacizumab on cultured ARPE-19 cells

    doi: 10.1038/s41598-017-12496-z

    Figure Lengend Snippet: Effects of BEV + RES on Notch signaling. Bar graph depicts the relative mRNA expression levels of notch 4 and dll 4 in with respect to mRNA levels of gapdh in untreated ARPE-19 cells and those treated with BEV, RES and BEV + RES ( A ). Graphical representation of quantified mean fluorescent intensity of immunofluorescent images for NOTCH 4 and DLL 4 are shown ( B ). Representative immunofluorscent images showing positivity for NOTCH 4 and DLL4 in untreated and BEV, RES, BEV + RES treated ARPE-19 cells ( C ). Representative western blots of NOTCH 4, DLL4 and the downstream target HES 1 in untreated and treated ARPE-19 cells ( D ). Graphical representation of the densitometric analysis of western blot results with respect to the levels of GAPDH is shown ( E ). Graphical representation of PathScan ® ELISA results of untreated and cells treated with BEV, RES and BEV + RES ( F ). Representative Western blot showing phosphorylated and total MEK1/2 (i) and p44/42 MAPK (ii) ( G ). Statistical analysis was performed using student’s t-test (*P < 0.05,**P < 0.01, ***P < 0.005) (n ≥ 3). Scale bar = 5 µm.

    Article Snippet: The quantity of phosporylated p-MEK1/2 (Ser217/221), p44/42MAPK(Thr202/Tyr204),p-SAPK/JNK(Thr183/Tyr185),p-Akt1(Ser473) and p-Akt1(Thr 308) were measured from cell lysates using human PathScan ® ELISA kits (Cell Signaling technology,Beverly,MA,USA).

    Techniques: Expressing, Western Blot, Enzyme-linked Immunosorbent Assay