anti p bad ser112  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti p bad ser112
    Anti P Bad Ser112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti p bad ser112  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti p bad ser112
    Anti P Bad Ser112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho bad p bad  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho bad p bad
    Phospho Bad P Bad, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti phospho bad ser 112  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho bad ser 112
    Inhibition of Rsk induces a reduction of pBAD and pSRF levels in STHdh Q111/Q111 cells . Lysates from STHdh Q7/Q7 and STHdh Q111/Q111 cells treated with or without BI-D1870 (0.1 μM; BI) were subjected to western blot to analyze pBAD <t>(Ser-112)/Bad</t> (A) and pSRF (Ser-103)/SRF (B) and tubulin protein levels. Results are expressed as the ratio between phospho and total Bad (A) and SRF (B) levels. Data are the mean ± SEM of four independent experiments performed in duplicate. Representative immunoblots are presented. Results are expressed in percentage respect to STHdh Q7/Q7 cells. Data were analyzed using two-way ANOVA followed by Bonferroni's post hoc test. *p < 0.05 and **p < 0.01 as compared with control STHdh Q7/Q7 cells and +++ p < 0.001 as compared with control STHdh Q111/Q111 cells.
    Anti Phospho Bad Ser 112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Increased 90-kDa ribosomal S6 kinase (Rsk) activity is protective against mutant huntingtin toxicity"

    Article Title: Increased 90-kDa ribosomal S6 kinase (Rsk) activity is protective against mutant huntingtin toxicity

    Journal: Molecular Neurodegeneration

    doi: 10.1186/1750-1326-6-74

    Inhibition of Rsk induces a reduction of pBAD and pSRF levels in STHdh Q111/Q111 cells . Lysates from STHdh Q7/Q7 and STHdh Q111/Q111 cells treated with or without BI-D1870 (0.1 μM; BI) were subjected to western blot to analyze pBAD (Ser-112)/Bad (A) and pSRF (Ser-103)/SRF (B) and tubulin protein levels. Results are expressed as the ratio between phospho and total Bad (A) and SRF (B) levels. Data are the mean ± SEM of four independent experiments performed in duplicate. Representative immunoblots are presented. Results are expressed in percentage respect to STHdh Q7/Q7 cells. Data were analyzed using two-way ANOVA followed by Bonferroni's post hoc test. *p < 0.05 and **p < 0.01 as compared with control STHdh Q7/Q7 cells and +++ p < 0.001 as compared with control STHdh Q111/Q111 cells.
    Figure Legend Snippet: Inhibition of Rsk induces a reduction of pBAD and pSRF levels in STHdh Q111/Q111 cells . Lysates from STHdh Q7/Q7 and STHdh Q111/Q111 cells treated with or without BI-D1870 (0.1 μM; BI) were subjected to western blot to analyze pBAD (Ser-112)/Bad (A) and pSRF (Ser-103)/SRF (B) and tubulin protein levels. Results are expressed as the ratio between phospho and total Bad (A) and SRF (B) levels. Data are the mean ± SEM of four independent experiments performed in duplicate. Representative immunoblots are presented. Results are expressed in percentage respect to STHdh Q7/Q7 cells. Data were analyzed using two-way ANOVA followed by Bonferroni's post hoc test. *p < 0.05 and **p < 0.01 as compared with control STHdh Q7/Q7 cells and +++ p < 0.001 as compared with control STHdh Q111/Q111 cells.

    Techniques Used: Inhibition, Western Blot

    p bad  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p bad
    P Bad, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit anti phospho bad pbad  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti phospho bad pbad
    Effects of EA at acupoints on cytosolic expression of pMEK1/2, <t>pERK1/2,</t> <t>pp90RSK,</t> and <t>pBad.</t> (A) Representative western blot images showed the cytosolic expression of pMEK1/2, pERK1/2, pp90RSK, and pBad in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups after 3 d of reperfusion. Actin was used as an internal control. The relative cytosolic expression of (B) pMEK1/2, (C) pERK1/2, (D) pp90RSK, and (E) pBad (n = 4) was assessed in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups. Data are presented as mean ± SD. # P < 0.05 compared with the model group.
    Rabbit Anti Phospho Bad Pbad, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Electroacupuncture-like stimulation at Baihui and Dazhui acupoints exerts neuroprotective effects through activation of the brain-derived neurotrophic factor-mediated MEK1/2/ERK1/2/p90RSK/bad signaling pathway in mild transient focal cerebral ischemia in rats"

    Article Title: Electroacupuncture-like stimulation at Baihui and Dazhui acupoints exerts neuroprotective effects through activation of the brain-derived neurotrophic factor-mediated MEK1/2/ERK1/2/p90RSK/bad signaling pathway in mild transient focal cerebral ischemia in rats

    Journal: BMC Complementary and Alternative Medicine

    doi: 10.1186/1472-6882-14-92

    Effects of EA at acupoints on cytosolic expression of pMEK1/2, pERK1/2, pp90RSK, and pBad. (A) Representative western blot images showed the cytosolic expression of pMEK1/2, pERK1/2, pp90RSK, and pBad in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups after 3 d of reperfusion. Actin was used as an internal control. The relative cytosolic expression of (B) pMEK1/2, (C) pERK1/2, (D) pp90RSK, and (E) pBad (n = 4) was assessed in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups. Data are presented as mean ± SD. # P < 0.05 compared with the model group.
    Figure Legend Snippet: Effects of EA at acupoints on cytosolic expression of pMEK1/2, pERK1/2, pp90RSK, and pBad. (A) Representative western blot images showed the cytosolic expression of pMEK1/2, pERK1/2, pp90RSK, and pBad in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups after 3 d of reperfusion. Actin was used as an internal control. The relative cytosolic expression of (B) pMEK1/2, (C) pERK1/2, (D) pp90RSK, and (E) pBad (n = 4) was assessed in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups. Data are presented as mean ± SD. # P < 0.05 compared with the model group.

    Techniques Used: Expressing, Western Blot

    anti ser112  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ser112
    (A) Oocytes were microinjected with a mRNA encoding Bad-GFP and one hour later incubated in the presence or the absence of the JNK inhibitor, SP600125, or microinjected with p21 Cip1 protein (Cip). They were then stimulated with progesterone (time 0). Egg proteins were analysed at the indicated times by immunoblot using antibodies against Bad, Ser128 (pS128), <t>Ser112</t> (pS112) or Ser136 (pS136)-phosphorylated forms of Bad, and the active phosphorylated form of JNK (p-JNK). These data are representative experiments repeated on oocytes and eggs from at least three different females. (B) Regulation of apoptosis in unfertilized eggs. In the ovary, prophase oocytes are protected from apoptosis by an inhibited form of Bad phosphorylated at Ser112 and Ser136. At time of ovulation, the oocyte completes meiotic maturation. Bad becomes phosphorylated on Ser128 under the control of Cdk1 and JNK. During aging, the ovulated egg progressively accumulates increasing amounts of the Ser128 phosphorylated form of Bad that can ultimately trigger the death execution, unless fertilization occurs.
    Anti Ser112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti ser112/product/Cell Signaling Technology Inc
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    Images

    1) Product Images from "Unfertilized Xenopus Eggs Die by Bad-Dependent Apoptosis under the Control of Cdk1 and JNK"

    Article Title: Unfertilized Xenopus Eggs Die by Bad-Dependent Apoptosis under the Control of Cdk1 and JNK

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0023672

    (A) Oocytes were microinjected with a mRNA encoding Bad-GFP and one hour later incubated in the presence or the absence of the JNK inhibitor, SP600125, or microinjected with p21 Cip1 protein (Cip). They were then stimulated with progesterone (time 0). Egg proteins were analysed at the indicated times by immunoblot using antibodies against Bad, Ser128 (pS128), Ser112 (pS112) or Ser136 (pS136)-phosphorylated forms of Bad, and the active phosphorylated form of JNK (p-JNK). These data are representative experiments repeated on oocytes and eggs from at least three different females. (B) Regulation of apoptosis in unfertilized eggs. In the ovary, prophase oocytes are protected from apoptosis by an inhibited form of Bad phosphorylated at Ser112 and Ser136. At time of ovulation, the oocyte completes meiotic maturation. Bad becomes phosphorylated on Ser128 under the control of Cdk1 and JNK. During aging, the ovulated egg progressively accumulates increasing amounts of the Ser128 phosphorylated form of Bad that can ultimately trigger the death execution, unless fertilization occurs.
    Figure Legend Snippet: (A) Oocytes were microinjected with a mRNA encoding Bad-GFP and one hour later incubated in the presence or the absence of the JNK inhibitor, SP600125, or microinjected with p21 Cip1 protein (Cip). They were then stimulated with progesterone (time 0). Egg proteins were analysed at the indicated times by immunoblot using antibodies against Bad, Ser128 (pS128), Ser112 (pS112) or Ser136 (pS136)-phosphorylated forms of Bad, and the active phosphorylated form of JNK (p-JNK). These data are representative experiments repeated on oocytes and eggs from at least three different females. (B) Regulation of apoptosis in unfertilized eggs. In the ovary, prophase oocytes are protected from apoptosis by an inhibited form of Bad phosphorylated at Ser112 and Ser136. At time of ovulation, the oocyte completes meiotic maturation. Bad becomes phosphorylated on Ser128 under the control of Cdk1 and JNK. During aging, the ovulated egg progressively accumulates increasing amounts of the Ser128 phosphorylated form of Bad that can ultimately trigger the death execution, unless fertilization occurs.

    Techniques Used: Incubation, Western Blot

    ser112  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc ser112
    Ser112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pbad s112  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pbad s112
    Pbad S112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p bad  (Cell Signaling Technology Inc)


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


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    Cell Signaling Technology Inc phospho bad
    Analysis of <t>PAK,</t> <t>AKT</t> and <t>BAD-phosphorylation</t> in EGF-stimulated 22Rv1 prostate cancer cells following AZA1 treatment. Representative Western blot images and quantification of immunoblots stained with phospho-PAK1/2 (pPAK), phospho-AKT (pAKT) and phospho-BAD (pBAD) antibodies before and after treatment with 2, 5 and 10 µM AZA1 for 24 h. Rac1/Cdc42 blockade reduces phosphorylation of PAK1, AKT and BAD in 22Rv1 prostate cancer cells compared to controls (means of 3 independent experiments). *, significantly different from unstimulated and untreated controls; + , significantly different from EGF-stimulated control; ‡ , significantly different from unstimulated, untreated control and EGF-stimulated control. SP, specific protein; LC, loading control.
    Phospho Bad, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "A Rac1/Cdc42 GTPase-Specific Small Molecule Inhibitor Suppresses Growth of Primary Human Prostate Cancer Xenografts and Prolongs Survival in Mice"

    Article Title: A Rac1/Cdc42 GTPase-Specific Small Molecule Inhibitor Suppresses Growth of Primary Human Prostate Cancer Xenografts and Prolongs Survival in Mice

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0074924

    Analysis of PAK, AKT and BAD-phosphorylation in EGF-stimulated 22Rv1 prostate cancer cells following AZA1 treatment. Representative Western blot images and quantification of immunoblots stained with phospho-PAK1/2 (pPAK), phospho-AKT (pAKT) and phospho-BAD (pBAD) antibodies before and after treatment with 2, 5 and 10 µM AZA1 for 24 h. Rac1/Cdc42 blockade reduces phosphorylation of PAK1, AKT and BAD in 22Rv1 prostate cancer cells compared to controls (means of 3 independent experiments). *, significantly different from unstimulated and untreated controls; + , significantly different from EGF-stimulated control; ‡ , significantly different from unstimulated, untreated control and EGF-stimulated control. SP, specific protein; LC, loading control.
    Figure Legend Snippet: Analysis of PAK, AKT and BAD-phosphorylation in EGF-stimulated 22Rv1 prostate cancer cells following AZA1 treatment. Representative Western blot images and quantification of immunoblots stained with phospho-PAK1/2 (pPAK), phospho-AKT (pAKT) and phospho-BAD (pBAD) antibodies before and after treatment with 2, 5 and 10 µM AZA1 for 24 h. Rac1/Cdc42 blockade reduces phosphorylation of PAK1, AKT and BAD in 22Rv1 prostate cancer cells compared to controls (means of 3 independent experiments). *, significantly different from unstimulated and untreated controls; + , significantly different from EGF-stimulated control; ‡ , significantly different from unstimulated, untreated control and EGF-stimulated control. SP, specific protein; LC, loading control.

    Techniques Used: Western Blot, Staining

    AZA1 inhibits activation of Rac1 and Cdc42 GTPases, shifting the balance towards cell growth inhibition and apoptosis. These effects are exerted by different mechanisms. AZA1 inhibits the PAK pathway via the cell cycle regulator Cyclin D1 and suppresses PAK and AKT activation leading to reduced BAD phosphorylation to induce pro-apoptotic activity. In addition, suppression of Rac1 and Cdc42 suppresses cancer cell migration and invasion by affecting actin polymerization and subsequent inhibition of lamellipodia and filopodia formation.
    Figure Legend Snippet: AZA1 inhibits activation of Rac1 and Cdc42 GTPases, shifting the balance towards cell growth inhibition and apoptosis. These effects are exerted by different mechanisms. AZA1 inhibits the PAK pathway via the cell cycle regulator Cyclin D1 and suppresses PAK and AKT activation leading to reduced BAD phosphorylation to induce pro-apoptotic activity. In addition, suppression of Rac1 and Cdc42 suppresses cancer cell migration and invasion by affecting actin polymerization and subsequent inhibition of lamellipodia and filopodia formation.

    Techniques Used: Activation Assay, Inhibition, Activity Assay, Migration

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    Cell Signaling Technology Inc anti p bad ser112
    Anti P Bad Ser112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Inhibition of Rsk induces a reduction of pBAD and pSRF levels in STHdh Q111/Q111 cells . Lysates from STHdh Q7/Q7 and STHdh Q111/Q111 cells treated with or without BI-D1870 (0.1 μM; BI) were subjected to western blot to analyze pBAD <t>(Ser-112)/Bad</t> (A) and pSRF (Ser-103)/SRF (B) and tubulin protein levels. Results are expressed as the ratio between phospho and total Bad (A) and SRF (B) levels. Data are the mean ± SEM of four independent experiments performed in duplicate. Representative immunoblots are presented. Results are expressed in percentage respect to STHdh Q7/Q7 cells. Data were analyzed using two-way ANOVA followed by Bonferroni's post hoc test. *p < 0.05 and **p < 0.01 as compared with control STHdh Q7/Q7 cells and +++ p < 0.001 as compared with control STHdh Q111/Q111 cells.
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    Inhibition of Rsk induces a reduction of pBAD and pSRF levels in STHdh Q111/Q111 cells . Lysates from STHdh Q7/Q7 and STHdh Q111/Q111 cells treated with or without BI-D1870 (0.1 μM; BI) were subjected to western blot to analyze pBAD <t>(Ser-112)/Bad</t> (A) and pSRF (Ser-103)/SRF (B) and tubulin protein levels. Results are expressed as the ratio between phospho and total Bad (A) and SRF (B) levels. Data are the mean ± SEM of four independent experiments performed in duplicate. Representative immunoblots are presented. Results are expressed in percentage respect to STHdh Q7/Q7 cells. Data were analyzed using two-way ANOVA followed by Bonferroni's post hoc test. *p < 0.05 and **p < 0.01 as compared with control STHdh Q7/Q7 cells and +++ p < 0.001 as compared with control STHdh Q111/Q111 cells.
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    Cell Signaling Technology Inc rabbit anti phospho bad pbad
    Effects of EA at acupoints on cytosolic expression of pMEK1/2, <t>pERK1/2,</t> <t>pp90RSK,</t> and <t>pBad.</t> (A) Representative western blot images showed the cytosolic expression of pMEK1/2, pERK1/2, pp90RSK, and pBad in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups after 3 d of reperfusion. Actin was used as an internal control. The relative cytosolic expression of (B) pMEK1/2, (C) pERK1/2, (D) pp90RSK, and (E) pBad (n = 4) was assessed in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups. Data are presented as mean ± SD. # P < 0.05 compared with the model group.
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    (A) Oocytes were microinjected with a mRNA encoding Bad-GFP and one hour later incubated in the presence or the absence of the JNK inhibitor, SP600125, or microinjected with p21 Cip1 protein (Cip). They were then stimulated with progesterone (time 0). Egg proteins were analysed at the indicated times by immunoblot using antibodies against Bad, Ser128 (pS128), <t>Ser112</t> (pS112) or Ser136 (pS136)-phosphorylated forms of Bad, and the active phosphorylated form of JNK (p-JNK). These data are representative experiments repeated on oocytes and eggs from at least three different females. (B) Regulation of apoptosis in unfertilized eggs. In the ovary, prophase oocytes are protected from apoptosis by an inhibited form of Bad phosphorylated at Ser112 and Ser136. At time of ovulation, the oocyte completes meiotic maturation. Bad becomes phosphorylated on Ser128 under the control of Cdk1 and JNK. During aging, the ovulated egg progressively accumulates increasing amounts of the Ser128 phosphorylated form of Bad that can ultimately trigger the death execution, unless fertilization occurs.
    Anti Ser112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Cell Signaling Technology Inc ser112
    (A) Oocytes were microinjected with a mRNA encoding Bad-GFP and one hour later incubated in the presence or the absence of the JNK inhibitor, SP600125, or microinjected with p21 Cip1 protein (Cip). They were then stimulated with progesterone (time 0). Egg proteins were analysed at the indicated times by immunoblot using antibodies against Bad, Ser128 (pS128), <t>Ser112</t> (pS112) or Ser136 (pS136)-phosphorylated forms of Bad, and the active phosphorylated form of JNK (p-JNK). These data are representative experiments repeated on oocytes and eggs from at least three different females. (B) Regulation of apoptosis in unfertilized eggs. In the ovary, prophase oocytes are protected from apoptosis by an inhibited form of Bad phosphorylated at Ser112 and Ser136. At time of ovulation, the oocyte completes meiotic maturation. Bad becomes phosphorylated on Ser128 under the control of Cdk1 and JNK. During aging, the ovulated egg progressively accumulates increasing amounts of the Ser128 phosphorylated form of Bad that can ultimately trigger the death execution, unless fertilization occurs.
    Ser112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Cell Signaling Technology Inc pbad s112
    (A) Oocytes were microinjected with a mRNA encoding Bad-GFP and one hour later incubated in the presence or the absence of the JNK inhibitor, SP600125, or microinjected with p21 Cip1 protein (Cip). They were then stimulated with progesterone (time 0). Egg proteins were analysed at the indicated times by immunoblot using antibodies against Bad, Ser128 (pS128), <t>Ser112</t> (pS112) or Ser136 (pS136)-phosphorylated forms of Bad, and the active phosphorylated form of JNK (p-JNK). These data are representative experiments repeated on oocytes and eggs from at least three different females. (B) Regulation of apoptosis in unfertilized eggs. In the ovary, prophase oocytes are protected from apoptosis by an inhibited form of Bad phosphorylated at Ser112 and Ser136. At time of ovulation, the oocyte completes meiotic maturation. Bad becomes phosphorylated on Ser128 under the control of Cdk1 and JNK. During aging, the ovulated egg progressively accumulates increasing amounts of the Ser128 phosphorylated form of Bad that can ultimately trigger the death execution, unless fertilization occurs.
    Pbad S112, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pbad s112/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Cell Signaling Technology Inc phospho bad
    Analysis of <t>PAK,</t> <t>AKT</t> and <t>BAD-phosphorylation</t> in EGF-stimulated 22Rv1 prostate cancer cells following AZA1 treatment. Representative Western blot images and quantification of immunoblots stained with phospho-PAK1/2 (pPAK), phospho-AKT (pAKT) and phospho-BAD (pBAD) antibodies before and after treatment with 2, 5 and 10 µM AZA1 for 24 h. Rac1/Cdc42 blockade reduces phosphorylation of PAK1, AKT and BAD in 22Rv1 prostate cancer cells compared to controls (means of 3 independent experiments). *, significantly different from unstimulated and untreated controls; + , significantly different from EGF-stimulated control; ‡ , significantly different from unstimulated, untreated control and EGF-stimulated control. SP, specific protein; LC, loading control.
    Phospho Bad, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Inhibition of Rsk induces a reduction of pBAD and pSRF levels in STHdh Q111/Q111 cells . Lysates from STHdh Q7/Q7 and STHdh Q111/Q111 cells treated with or without BI-D1870 (0.1 μM; BI) were subjected to western blot to analyze pBAD (Ser-112)/Bad (A) and pSRF (Ser-103)/SRF (B) and tubulin protein levels. Results are expressed as the ratio between phospho and total Bad (A) and SRF (B) levels. Data are the mean ± SEM of four independent experiments performed in duplicate. Representative immunoblots are presented. Results are expressed in percentage respect to STHdh Q7/Q7 cells. Data were analyzed using two-way ANOVA followed by Bonferroni's post hoc test. *p < 0.05 and **p < 0.01 as compared with control STHdh Q7/Q7 cells and +++ p < 0.001 as compared with control STHdh Q111/Q111 cells.

    Journal: Molecular Neurodegeneration

    Article Title: Increased 90-kDa ribosomal S6 kinase (Rsk) activity is protective against mutant huntingtin toxicity

    doi: 10.1186/1750-1326-6-74

    Figure Lengend Snippet: Inhibition of Rsk induces a reduction of pBAD and pSRF levels in STHdh Q111/Q111 cells . Lysates from STHdh Q7/Q7 and STHdh Q111/Q111 cells treated with or without BI-D1870 (0.1 μM; BI) were subjected to western blot to analyze pBAD (Ser-112)/Bad (A) and pSRF (Ser-103)/SRF (B) and tubulin protein levels. Results are expressed as the ratio between phospho and total Bad (A) and SRF (B) levels. Data are the mean ± SEM of four independent experiments performed in duplicate. Representative immunoblots are presented. Results are expressed in percentage respect to STHdh Q7/Q7 cells. Data were analyzed using two-way ANOVA followed by Bonferroni's post hoc test. *p < 0.05 and **p < 0.01 as compared with control STHdh Q7/Q7 cells and +++ p < 0.001 as compared with control STHdh Q111/Q111 cells.

    Article Snippet: The following primary antibodies were used: anti-Rsk1, anti-Rsk2, anti-phospho-Rsk (Ser-221) and anti-phospho-Rsk (Ser-380) (all 1:500; Santa Cruz Biotechnology, Santa Cruz, CA), anti-htt monoclonal 2166 (1:1000; Millipore Bioscience Research reagents, Temecula, CA), anti-phospho-SRF (Ser-103), anti-SRF, anti-phospho-Bad (Ser-112) and anti-Bad (all 1:1000; Cell Signaling Technology, Beverly, MA), and anti-HA (1:1000; Sigma-Aldrich, Saint Louis, MO).

    Techniques: Inhibition, Western Blot

    Effects of EA at acupoints on cytosolic expression of pMEK1/2, pERK1/2, pp90RSK, and pBad. (A) Representative western blot images showed the cytosolic expression of pMEK1/2, pERK1/2, pp90RSK, and pBad in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups after 3 d of reperfusion. Actin was used as an internal control. The relative cytosolic expression of (B) pMEK1/2, (C) pERK1/2, (D) pp90RSK, and (E) pBad (n = 4) was assessed in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups. Data are presented as mean ± SD. # P < 0.05 compared with the model group.

    Journal: BMC Complementary and Alternative Medicine

    Article Title: Electroacupuncture-like stimulation at Baihui and Dazhui acupoints exerts neuroprotective effects through activation of the brain-derived neurotrophic factor-mediated MEK1/2/ERK1/2/p90RSK/bad signaling pathway in mild transient focal cerebral ischemia in rats

    doi: 10.1186/1472-6882-14-92

    Figure Lengend Snippet: Effects of EA at acupoints on cytosolic expression of pMEK1/2, pERK1/2, pp90RSK, and pBad. (A) Representative western blot images showed the cytosolic expression of pMEK1/2, pERK1/2, pp90RSK, and pBad in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups after 3 d of reperfusion. Actin was used as an internal control. The relative cytosolic expression of (B) pMEK1/2, (C) pERK1/2, (D) pp90RSK, and (E) pBad (n = 4) was assessed in the ischemic cortex in the sham, model, EA, non-acup, and U0126 + EA groups. Data are presented as mean ± SD. # P < 0.05 compared with the model group.

    Article Snippet: They were then incubated with a rabbit anti-pMEK1/2 (1:1000 dilution, #2338 Cell Signaling Technology), rabbit anti-pERK1/2 (1:1000 dilution, #4376 Cell Signaling Technology), rabbit anti-pp90RSK (1:1000 dilution, #9344 Cell Signaling Technology), or rabbit anti-phospho-Bad (pBad) (1:1000 dilution, #9291 Cell Signaling Technology) antibody overnight at 4°C.

    Techniques: Expressing, Western Blot

    (A) Oocytes were microinjected with a mRNA encoding Bad-GFP and one hour later incubated in the presence or the absence of the JNK inhibitor, SP600125, or microinjected with p21 Cip1 protein (Cip). They were then stimulated with progesterone (time 0). Egg proteins were analysed at the indicated times by immunoblot using antibodies against Bad, Ser128 (pS128), Ser112 (pS112) or Ser136 (pS136)-phosphorylated forms of Bad, and the active phosphorylated form of JNK (p-JNK). These data are representative experiments repeated on oocytes and eggs from at least three different females. (B) Regulation of apoptosis in unfertilized eggs. In the ovary, prophase oocytes are protected from apoptosis by an inhibited form of Bad phosphorylated at Ser112 and Ser136. At time of ovulation, the oocyte completes meiotic maturation. Bad becomes phosphorylated on Ser128 under the control of Cdk1 and JNK. During aging, the ovulated egg progressively accumulates increasing amounts of the Ser128 phosphorylated form of Bad that can ultimately trigger the death execution, unless fertilization occurs.

    Journal: PLoS ONE

    Article Title: Unfertilized Xenopus Eggs Die by Bad-Dependent Apoptosis under the Control of Cdk1 and JNK

    doi: 10.1371/journal.pone.0023672

    Figure Lengend Snippet: (A) Oocytes were microinjected with a mRNA encoding Bad-GFP and one hour later incubated in the presence or the absence of the JNK inhibitor, SP600125, or microinjected with p21 Cip1 protein (Cip). They were then stimulated with progesterone (time 0). Egg proteins were analysed at the indicated times by immunoblot using antibodies against Bad, Ser128 (pS128), Ser112 (pS112) or Ser136 (pS136)-phosphorylated forms of Bad, and the active phosphorylated form of JNK (p-JNK). These data are representative experiments repeated on oocytes and eggs from at least three different females. (B) Regulation of apoptosis in unfertilized eggs. In the ovary, prophase oocytes are protected from apoptosis by an inhibited form of Bad phosphorylated at Ser112 and Ser136. At time of ovulation, the oocyte completes meiotic maturation. Bad becomes phosphorylated on Ser128 under the control of Cdk1 and JNK. During aging, the ovulated egg progressively accumulates increasing amounts of the Ser128 phosphorylated form of Bad that can ultimately trigger the death execution, unless fertilization occurs.

    Article Snippet: Samples of 50 µg of proteins (equivalent to 0.25 to 2 oocytes or eggs) in Laemmli buffer were electrophoresed on 10% or 15% SDS-PAGE (Amresco Inc., USA), transferred to nitrocellulose filters (Schleicher and Schuell) using a semi-dry blotting system (Millipore) and immunoblotted using the following antibodies: anti- Xenopus cyclin B2 , anti-phosphorylated ERK 1/2 (New England Biolabs), anti-ERK1 and anti- Xenopus Mos (Santa Cruz Biotechnologies), anti-caspase 9 , anti-Cyt c, anti-Bax, anti-p150Glued (BD Bioscience, USA), anti-phosphorylated histone H2B (Upstate Biotechnology Inc., USA), anti-Ser128 phosphorylated Bad (Abcam, France), anti-caspase 3, anti-Ser10 phosphorylated histone H3, anti-phosphorylated JNK, anti-Bad, anti-Ser112 phosphorylated Bad and anti-Ser136 phosphorylated Bad (Cell Signaling, Danvers, USA).

    Techniques: Incubation, Western Blot

    Analysis of PAK, AKT and BAD-phosphorylation in EGF-stimulated 22Rv1 prostate cancer cells following AZA1 treatment. Representative Western blot images and quantification of immunoblots stained with phospho-PAK1/2 (pPAK), phospho-AKT (pAKT) and phospho-BAD (pBAD) antibodies before and after treatment with 2, 5 and 10 µM AZA1 for 24 h. Rac1/Cdc42 blockade reduces phosphorylation of PAK1, AKT and BAD in 22Rv1 prostate cancer cells compared to controls (means of 3 independent experiments). *, significantly different from unstimulated and untreated controls; + , significantly different from EGF-stimulated control; ‡ , significantly different from unstimulated, untreated control and EGF-stimulated control. SP, specific protein; LC, loading control.

    Journal: PLoS ONE

    Article Title: A Rac1/Cdc42 GTPase-Specific Small Molecule Inhibitor Suppresses Growth of Primary Human Prostate Cancer Xenografts and Prolongs Survival in Mice

    doi: 10.1371/journal.pone.0074924

    Figure Lengend Snippet: Analysis of PAK, AKT and BAD-phosphorylation in EGF-stimulated 22Rv1 prostate cancer cells following AZA1 treatment. Representative Western blot images and quantification of immunoblots stained with phospho-PAK1/2 (pPAK), phospho-AKT (pAKT) and phospho-BAD (pBAD) antibodies before and after treatment with 2, 5 and 10 µM AZA1 for 24 h. Rac1/Cdc42 blockade reduces phosphorylation of PAK1, AKT and BAD in 22Rv1 prostate cancer cells compared to controls (means of 3 independent experiments). *, significantly different from unstimulated and untreated controls; + , significantly different from EGF-stimulated control; ‡ , significantly different from unstimulated, untreated control and EGF-stimulated control. SP, specific protein; LC, loading control.

    Article Snippet: The blots were probed with antibodies against phospho-PAK1 (pS144)/PAK2 (pS141) (Cell Signaling Technology, Danvers, MA), phospho-AKT (anti-phospho-AKT pT308 from BD Biosciences) and phospho-BAD (anti-phospho-BAD Ser112 from Cell Signaling Technology) before incubation with horseradish peroxidase–conjugated secondary antibodies (Amersham Pharmacia Biotech).

    Techniques: Western Blot, Staining

    AZA1 inhibits activation of Rac1 and Cdc42 GTPases, shifting the balance towards cell growth inhibition and apoptosis. These effects are exerted by different mechanisms. AZA1 inhibits the PAK pathway via the cell cycle regulator Cyclin D1 and suppresses PAK and AKT activation leading to reduced BAD phosphorylation to induce pro-apoptotic activity. In addition, suppression of Rac1 and Cdc42 suppresses cancer cell migration and invasion by affecting actin polymerization and subsequent inhibition of lamellipodia and filopodia formation.

    Journal: PLoS ONE

    Article Title: A Rac1/Cdc42 GTPase-Specific Small Molecule Inhibitor Suppresses Growth of Primary Human Prostate Cancer Xenografts and Prolongs Survival in Mice

    doi: 10.1371/journal.pone.0074924

    Figure Lengend Snippet: AZA1 inhibits activation of Rac1 and Cdc42 GTPases, shifting the balance towards cell growth inhibition and apoptosis. These effects are exerted by different mechanisms. AZA1 inhibits the PAK pathway via the cell cycle regulator Cyclin D1 and suppresses PAK and AKT activation leading to reduced BAD phosphorylation to induce pro-apoptotic activity. In addition, suppression of Rac1 and Cdc42 suppresses cancer cell migration and invasion by affecting actin polymerization and subsequent inhibition of lamellipodia and filopodia formation.

    Article Snippet: The blots were probed with antibodies against phospho-PAK1 (pS144)/PAK2 (pS141) (Cell Signaling Technology, Danvers, MA), phospho-AKT (anti-phospho-AKT pT308 from BD Biosciences) and phospho-BAD (anti-phospho-BAD Ser112 from Cell Signaling Technology) before incubation with horseradish peroxidase–conjugated secondary antibodies (Amersham Pharmacia Biotech).

    Techniques: Activation Assay, Inhibition, Activity Assay, Migration