phosphor akt ser473  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt ser473
    Phosphor Akt Ser473, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phosphor akt ser473  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphor akt ser473
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    ser 473  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc ser 473
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    anti akt phospho ser473  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti akt phospho ser473
    Anti Akt Phospho Ser473, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pakt antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pakt antibody
    Protective effects of G-CSF on wound healing-related protein expression. ( A ) α-SMA, Collagen I, Bcl 2, Caspase 3, <t>pAKT,</t> <t>AKT,</t> β-actin expressions were evaluated by WB. ( B ) Each protein was normalized by β-actin and showed as fold change of Blank group. Each result was repeated at least for 3 times. Data were shown as mean ±SD. * P<0.05 versus Blank group, # P<0.05 versus Normal saline group.
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    Images

    1) Product Images from "Granulocyte-Colony Stimulating Factor (G-CSF) Accelerates Wound Healing in Hemorrhagic Shock Rats by Enhancing Angiogenesis and Attenuating Apoptosis"

    Article Title: Granulocyte-Colony Stimulating Factor (G-CSF) Accelerates Wound Healing in Hemorrhagic Shock Rats by Enhancing Angiogenesis and Attenuating Apoptosis

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

    doi: 10.12659/MSM.904988

    Protective effects of G-CSF on wound healing-related protein expression. ( A ) α-SMA, Collagen I, Bcl 2, Caspase 3, pAKT, AKT, β-actin expressions were evaluated by WB. ( B ) Each protein was normalized by β-actin and showed as fold change of Blank group. Each result was repeated at least for 3 times. Data were shown as mean ±SD. * P<0.05 versus Blank group, # P<0.05 versus Normal saline group.
    Figure Legend Snippet: Protective effects of G-CSF on wound healing-related protein expression. ( A ) α-SMA, Collagen I, Bcl 2, Caspase 3, pAKT, AKT, β-actin expressions were evaluated by WB. ( B ) Each protein was normalized by β-actin and showed as fold change of Blank group. Each result was repeated at least for 3 times. Data were shown as mean ±SD. * P<0.05 versus Blank group, # P<0.05 versus Normal saline group.

    Techniques Used: Expressing

    G-CSF promoted the angiogenic potential of HUVECs in vitro . ( A ) Representative images depicting the effect of the G-CSF treatment at 12 h on HUVEC migration at the indicated concentrations. ( B ) Statistically calculated relative migration rates; Scale bar=500 μm. ( C ) Typical images of the tube-like structures in the presence of G-CSF cultured on Matrigel for 12 h. ( D ) The amounts of capillary-like structures; Scale bar=200 μm. ( E ) Western blot of VEGF, Bcl 2, Caspase 3, phosphorylated AKT (pAKT) as well as the total AKT and β-actin expressions at different concentrations of G-CSF; the HUVECs were pre-incubated with G-CSF for 24 h then followed by H 2 O 2 stimulation (50 μmol/L) to determine the protein activities by Western blot. Each experiment was repeated 3 times and typical pictures are shown. Data are shown as mean ±SD. * P<0.05 versus HUVECs without G-CSF stimulation.
    Figure Legend Snippet: G-CSF promoted the angiogenic potential of HUVECs in vitro . ( A ) Representative images depicting the effect of the G-CSF treatment at 12 h on HUVEC migration at the indicated concentrations. ( B ) Statistically calculated relative migration rates; Scale bar=500 μm. ( C ) Typical images of the tube-like structures in the presence of G-CSF cultured on Matrigel for 12 h. ( D ) The amounts of capillary-like structures; Scale bar=200 μm. ( E ) Western blot of VEGF, Bcl 2, Caspase 3, phosphorylated AKT (pAKT) as well as the total AKT and β-actin expressions at different concentrations of G-CSF; the HUVECs were pre-incubated with G-CSF for 24 h then followed by H 2 O 2 stimulation (50 μmol/L) to determine the protein activities by Western blot. Each experiment was repeated 3 times and typical pictures are shown. Data are shown as mean ±SD. * P<0.05 versus HUVECs without G-CSF stimulation.

    Techniques Used: In Vitro, Migration, Cell Culture, Western Blot, Incubation

    ser473 pkb akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc ser473 pkb akt
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    anti akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti akt
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    anti akt1  (Cell Signaling Technology Inc)


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    antibody phospho akt ser 473  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc antibody phospho akt ser 473
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    ser473  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc ser473
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    pakt ser473  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pakt ser473
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    Protective effects of G-CSF on wound healing-related protein expression. ( A ) α-SMA, Collagen I, Bcl 2, Caspase 3, <t>pAKT,</t> <t>AKT,</t> β-actin expressions were evaluated by WB. ( B ) Each protein was normalized by β-actin and showed as fold change of Blank group. Each result was repeated at least for 3 times. Data were shown as mean ±SD. * P<0.05 versus Blank group, # P<0.05 versus Normal saline group.
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    Protective effects of G-CSF on wound healing-related protein expression. ( A ) α-SMA, Collagen I, Bcl 2, Caspase 3, <t>pAKT,</t> <t>AKT,</t> β-actin expressions were evaluated by WB. ( B ) Each protein was normalized by β-actin and showed as fold change of Blank group. Each result was repeated at least for 3 times. Data were shown as mean ±SD. * P<0.05 versus Blank group, # P<0.05 versus Normal saline group.
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    Image Search Results


    Protective effects of G-CSF on wound healing-related protein expression. ( A ) α-SMA, Collagen I, Bcl 2, Caspase 3, pAKT, AKT, β-actin expressions were evaluated by WB. ( B ) Each protein was normalized by β-actin and showed as fold change of Blank group. Each result was repeated at least for 3 times. Data were shown as mean ±SD. * P<0.05 versus Blank group, # P<0.05 versus Normal saline group.

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

    Article Title: Granulocyte-Colony Stimulating Factor (G-CSF) Accelerates Wound Healing in Hemorrhagic Shock Rats by Enhancing Angiogenesis and Attenuating Apoptosis

    doi: 10.12659/MSM.904988

    Figure Lengend Snippet: Protective effects of G-CSF on wound healing-related protein expression. ( A ) α-SMA, Collagen I, Bcl 2, Caspase 3, pAKT, AKT, β-actin expressions were evaluated by WB. ( B ) Each protein was normalized by β-actin and showed as fold change of Blank group. Each result was repeated at least for 3 times. Data were shown as mean ±SD. * P<0.05 versus Blank group, # P<0.05 versus Normal saline group.

    Article Snippet: The blots were blocked for 1 h in 5% nonfat dry milk, and the first antibodies were added at the following proper dilutions and kept overnight at 4°C: pAKT antibody (1: 1500, CST technology, USA), AKT antibody (1: 1500, CST technology), VEGF (1: 1000, Abcam, USA), α-SMA (1: 500, BOSTER, China), collagen I (1: 500, BOSTER), Bcl 2 (1: 1000, CST technology), caspase 3 (1: 1500, CST technology), and mouse monoclonal β-actin antibody (1: 4000, Santa Cruz, USA).

    Techniques: Expressing

    G-CSF promoted the angiogenic potential of HUVECs in vitro . ( A ) Representative images depicting the effect of the G-CSF treatment at 12 h on HUVEC migration at the indicated concentrations. ( B ) Statistically calculated relative migration rates; Scale bar=500 μm. ( C ) Typical images of the tube-like structures in the presence of G-CSF cultured on Matrigel for 12 h. ( D ) The amounts of capillary-like structures; Scale bar=200 μm. ( E ) Western blot of VEGF, Bcl 2, Caspase 3, phosphorylated AKT (pAKT) as well as the total AKT and β-actin expressions at different concentrations of G-CSF; the HUVECs were pre-incubated with G-CSF for 24 h then followed by H 2 O 2 stimulation (50 μmol/L) to determine the protein activities by Western blot. Each experiment was repeated 3 times and typical pictures are shown. Data are shown as mean ±SD. * P<0.05 versus HUVECs without G-CSF stimulation.

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

    Article Title: Granulocyte-Colony Stimulating Factor (G-CSF) Accelerates Wound Healing in Hemorrhagic Shock Rats by Enhancing Angiogenesis and Attenuating Apoptosis

    doi: 10.12659/MSM.904988

    Figure Lengend Snippet: G-CSF promoted the angiogenic potential of HUVECs in vitro . ( A ) Representative images depicting the effect of the G-CSF treatment at 12 h on HUVEC migration at the indicated concentrations. ( B ) Statistically calculated relative migration rates; Scale bar=500 μm. ( C ) Typical images of the tube-like structures in the presence of G-CSF cultured on Matrigel for 12 h. ( D ) The amounts of capillary-like structures; Scale bar=200 μm. ( E ) Western blot of VEGF, Bcl 2, Caspase 3, phosphorylated AKT (pAKT) as well as the total AKT and β-actin expressions at different concentrations of G-CSF; the HUVECs were pre-incubated with G-CSF for 24 h then followed by H 2 O 2 stimulation (50 μmol/L) to determine the protein activities by Western blot. Each experiment was repeated 3 times and typical pictures are shown. Data are shown as mean ±SD. * P<0.05 versus HUVECs without G-CSF stimulation.

    Article Snippet: The blots were blocked for 1 h in 5% nonfat dry milk, and the first antibodies were added at the following proper dilutions and kept overnight at 4°C: pAKT antibody (1: 1500, CST technology, USA), AKT antibody (1: 1500, CST technology), VEGF (1: 1000, Abcam, USA), α-SMA (1: 500, BOSTER, China), collagen I (1: 500, BOSTER), Bcl 2 (1: 1000, CST technology), caspase 3 (1: 1500, CST technology), and mouse monoclonal β-actin antibody (1: 4000, Santa Cruz, USA).

    Techniques: In Vitro, Migration, Cell Culture, Western Blot, Incubation