src inhibitor pp1  (Millipore)


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    Structured Review

    Millipore src inhibitor pp1
    The <t>Src</t> inhibitor <t>PP1</t> enhances migration and attenuates ligand-dependent EGFR ubiquitylation. ( A ) Human telomerase-immortalized corneal epithelial cells were pretreated without or with 12 μM ( left ) or 0.01 μM ( right ) as indicated. Cells
    Src Inhibitor Pp1, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/src inhibitor pp1/product/Millipore
    Average 94 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    src inhibitor pp1 - by Bioz Stars, 2020-10
    94/100 stars

    Images

    1) Product Images from "Antagonizing c-Cbl Enhances EGFR-Dependent Corneal Epithelial Homeostasis"

    Article Title: Antagonizing c-Cbl Enhances EGFR-Dependent Corneal Epithelial Homeostasis

    Journal: Investigative Ophthalmology & Visual Science

    doi: 10.1167/iovs.14-14133

    The Src inhibitor PP1 enhances migration and attenuates ligand-dependent EGFR ubiquitylation. ( A ) Human telomerase-immortalized corneal epithelial cells were pretreated without or with 12 μM ( left ) or 0.01 μM ( right ) as indicated. Cells
    Figure Legend Snippet: The Src inhibitor PP1 enhances migration and attenuates ligand-dependent EGFR ubiquitylation. ( A ) Human telomerase-immortalized corneal epithelial cells were pretreated without or with 12 μM ( left ) or 0.01 μM ( right ) as indicated. Cells

    Techniques Used: Migration

    2) Product Images from "Adiponectin Regulates Vascular Endothelial Growth Factor-C Expression in Macrophages via Syk-ERK Pathway"

    Article Title: Adiponectin Regulates Vascular Endothelial Growth Factor-C Expression in Macrophages via Syk-ERK Pathway

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0056071

    Effects of Src inhibitor on adiponectin-induced changes in peripheral blood monocyte-derived macrophages (PBDMs). PBDMs were preincubated with 10 µM PP1 for 30 min and then incubated with adiponectin for 6 hours (A–D). The mRNA expression levels of COX-2 (A), TIMP-1 (B), IL-6 (C), and VEGF-C (D) were quantified by real-time PCR. Values are normalized to the level of GAPDH mRNA and expressed as mean ± SEM (n = 3). ***P
    Figure Legend Snippet: Effects of Src inhibitor on adiponectin-induced changes in peripheral blood monocyte-derived macrophages (PBDMs). PBDMs were preincubated with 10 µM PP1 for 30 min and then incubated with adiponectin for 6 hours (A–D). The mRNA expression levels of COX-2 (A), TIMP-1 (B), IL-6 (C), and VEGF-C (D) were quantified by real-time PCR. Values are normalized to the level of GAPDH mRNA and expressed as mean ± SEM (n = 3). ***P

    Techniques Used: Derivative Assay, Incubation, Expressing, Real-time Polymerase Chain Reaction

    3) Product Images from "β-Arrestin-1 Drives Endothelin-1–Mediated Podocyte Activation and Sustains Renal Injury"

    Article Title: β-Arrestin-1 Drives Endothelin-1–Mediated Podocyte Activation and Sustains Renal Injury

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2013040362

    ET A R and β -arrestin-1 form a molecular signaling complex with Src promoting EGFR transactivation in ET-1-treated podocytes. (A) The association of β -arrestin-1 ( β -arr1) with ET A R and Src was studied in cell lysates from control and ET-1–-treated podocytes by immunoprecipitation (IP) assays using irrelevant IgG (negative control) or an anti– β -arr1 antibody followed by immunoblotting (IB) with anti-ET A R, anti-Src, and anti– β -arr1 antibodies. (B) The role of ET A R in the formation of the molecular signaling complex was assessed by IPs using irrelevant IgG or an anti–arr1 antibody in lysates from podocytes exposed to control medium, ET-1 (100 nM, 15 minutes) alone or in the presence of BQ123 (1 μ M), followed by IB with anti– β -arr1 and anti-Src antibodies. (C) Cell lysates from podocytes incubated with control medium or ET-1 (100 nM) for 5, 15, or 30 minutes were immunoblotted with anti–phospho-Src (Y416), anti-Src, anti–phospho-EGFR (Y845), anti-EGFR, anti–phospho-AKT, anti-AKT, anti–phospho-p42/44 MAPK, anti-p42/44 MAPK, and anti-HSP70 antibodies. (D) IB analysis using anti–phospho-EGFR (Y845) and anti-EGFR antibodies in podocytes exposed to control medium or stimulated with ET-1 (100 nM, 15 minutes) in the presence or absence of PP1 (1 μ M). EGFR phosphorylation status was also assessed in ET-1–treated podocytes silenced for β -arrestin-1 (si- β -arr1) by specific siRNA or transfected with scrambled siRNA (SCR). For all panels, data are representative of at least three experiments. Molecular mass is indicated in kilodaltons.
    Figure Legend Snippet: ET A R and β -arrestin-1 form a molecular signaling complex with Src promoting EGFR transactivation in ET-1-treated podocytes. (A) The association of β -arrestin-1 ( β -arr1) with ET A R and Src was studied in cell lysates from control and ET-1–-treated podocytes by immunoprecipitation (IP) assays using irrelevant IgG (negative control) or an anti– β -arr1 antibody followed by immunoblotting (IB) with anti-ET A R, anti-Src, and anti– β -arr1 antibodies. (B) The role of ET A R in the formation of the molecular signaling complex was assessed by IPs using irrelevant IgG or an anti–arr1 antibody in lysates from podocytes exposed to control medium, ET-1 (100 nM, 15 minutes) alone or in the presence of BQ123 (1 μ M), followed by IB with anti– β -arr1 and anti-Src antibodies. (C) Cell lysates from podocytes incubated with control medium or ET-1 (100 nM) for 5, 15, or 30 minutes were immunoblotted with anti–phospho-Src (Y416), anti-Src, anti–phospho-EGFR (Y845), anti-EGFR, anti–phospho-AKT, anti-AKT, anti–phospho-p42/44 MAPK, anti-p42/44 MAPK, and anti-HSP70 antibodies. (D) IB analysis using anti–phospho-EGFR (Y845) and anti-EGFR antibodies in podocytes exposed to control medium or stimulated with ET-1 (100 nM, 15 minutes) in the presence or absence of PP1 (1 μ M). EGFR phosphorylation status was also assessed in ET-1–treated podocytes silenced for β -arrestin-1 (si- β -arr1) by specific siRNA or transfected with scrambled siRNA (SCR). For all panels, data are representative of at least three experiments. Molecular mass is indicated in kilodaltons.

    Techniques Used: Immunoprecipitation, Negative Control, Incubation, Transfection

    The complex ET A R/ β -arrestin-1/Src and the EGFR transactivation are required for β-catenin stability. (A) Cell lysates from control or ET-1–treated podocytes were immunoprecipitated with irrelevant IgG (negative control) or anti– β -arrestin-1 ( β -arr1) antibody and analyzed by immunoblotting (IB) using anti– β -catenin ( β -cat) and anti– β -arr1 antibodies. (B) Active β -cat was assessed in podocytes exposed to control medium, ET-1 (100 nM) alone or with BQ123 (1 μ M) by IB. Anti-HSP70 antibody was used to confirm equal protein loading. (C) Active β -cat in podocytes transfected with scrambled (SCR) or β -arrestin-1 (si- β -arr1) siRNA before exposure to ET-1 (100 nM) for 15 minutes. Anti-HSP70 antibody was used to confirm equal protein loading. (D) Lysates of podocytes treated with control medium, ET-1 (100 nM, 15 minutes) alone or in the presence of PP1 (1 μ M) were immunoprecipitated with irrelevant IgG or anti– β -cat antibody and analyzed by IB using an antiphosphorylated tyrosine (pTYR) and anti– β -cat antibodies. (E) Lysates of podocytes treated with control medium, ET-1 (100 nM, 15 minutes) alone or in the presence of AG1478 (1 μ M) were immunoprecipitated with irrelevant IgG or anti– β -cat antibody and analyzed by IB using anti-pTYR and anti– β -cat antibodies. (F) Accumulation of active β -cat was evaluated in podocytes exposed to control medium, ET-1 (100 nM) alone or supplemented with AG1478 (1 μ M). Cell lysates were analyzed by IB using anti-active β -cat and anti-HSP70 antibodies. For all panels, data are representative of at least two experiments. Molecular mass is indicated in kilodaltons.
    Figure Legend Snippet: The complex ET A R/ β -arrestin-1/Src and the EGFR transactivation are required for β-catenin stability. (A) Cell lysates from control or ET-1–treated podocytes were immunoprecipitated with irrelevant IgG (negative control) or anti– β -arrestin-1 ( β -arr1) antibody and analyzed by immunoblotting (IB) using anti– β -catenin ( β -cat) and anti– β -arr1 antibodies. (B) Active β -cat was assessed in podocytes exposed to control medium, ET-1 (100 nM) alone or with BQ123 (1 μ M) by IB. Anti-HSP70 antibody was used to confirm equal protein loading. (C) Active β -cat in podocytes transfected with scrambled (SCR) or β -arrestin-1 (si- β -arr1) siRNA before exposure to ET-1 (100 nM) for 15 minutes. Anti-HSP70 antibody was used to confirm equal protein loading. (D) Lysates of podocytes treated with control medium, ET-1 (100 nM, 15 minutes) alone or in the presence of PP1 (1 μ M) were immunoprecipitated with irrelevant IgG or anti– β -cat antibody and analyzed by IB using an antiphosphorylated tyrosine (pTYR) and anti– β -cat antibodies. (E) Lysates of podocytes treated with control medium, ET-1 (100 nM, 15 minutes) alone or in the presence of AG1478 (1 μ M) were immunoprecipitated with irrelevant IgG or anti– β -cat antibody and analyzed by IB using anti-pTYR and anti– β -cat antibodies. (F) Accumulation of active β -cat was evaluated in podocytes exposed to control medium, ET-1 (100 nM) alone or supplemented with AG1478 (1 μ M). Cell lysates were analyzed by IB using anti-active β -cat and anti-HSP70 antibodies. For all panels, data are representative of at least two experiments. Molecular mass is indicated in kilodaltons.

    Techniques Used: Immunoprecipitation, Negative Control, Transfection

    Related Articles

    Concentration Assay:

    Article Title: Antagonizing c-Cbl Enhances EGFR-Dependent Corneal Epithelial Homeostasis
    Article Snippet: .. The Src inhibitor PP1 (4-amino-5-[4-methylphenyl]-7-[t-butyl]pyrazolo-d-3,4-pyrimidine) (EMD Millipore, Billerica, MA, USA) was solubilized in DMSO at a concentration of 50 mM. .. For tissue culture experiments, cells were incubated for 2 hours at 37°C with the indicated concentrations of PP1 (0.025 % DMSO was used as a control) in serum-free media.

    Incubation:

    Article Title: Differential regulation of Cav2.2 channel exon 37 variants by alternatively spliced μ-opioid receptors
    Article Snippet: .. Cells expressing Cav2.2-37a and mMOR1C were incubated overnight with 500 ng/ml of PTX (Tocris 3097) or with 2 μM of Src inhibitor for 4 h (PP1, Millipore 567,809). ..

    other:

    Article Title: Adiponectin Regulates Vascular Endothelial Growth Factor-C Expression in Macrophages via Syk-ERK Pathway
    Article Snippet: Materials Syk inhibitor (BAY 61-3606), Src inhibitor (PP1) and MEK inhibitor (PD98059) were purchased from Calbiochem (Gibbstown, NJ).

    Article Title: Activation of the Ras/Mitogen-Activated Protein Kinase Pathway by Kinase-Defective Epidermal Growth Factor Receptors Results in Cell Survival but Not Proliferation
    Article Snippet: JAK kinase inhibitor AG490 ( ) and Src kinase inhibitor PP1 ( ) were gifts from Alexander Levitzki. ( ) was obtained from Sigma (St. Louis, Mo.).

    Expressing:

    Article Title: Differential regulation of Cav2.2 channel exon 37 variants by alternatively spliced μ-opioid receptors
    Article Snippet: .. Cells expressing Cav2.2-37a and mMOR1C were incubated overnight with 500 ng/ml of PTX (Tocris 3097) or with 2 μM of Src inhibitor for 4 h (PP1, Millipore 567,809). ..

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    Millipore src inhibitor pp1
    The <t>Src</t> inhibitor <t>PP1</t> enhances migration and attenuates ligand-dependent EGFR ubiquitylation. ( A ) Human telomerase-immortalized corneal epithelial cells were pretreated without or with 12 μM ( left ) or 0.01 μM ( right ) as indicated. Cells
    Src Inhibitor Pp1, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/src inhibitor pp1/product/Millipore
    Average 94 stars, based on 30 article reviews
    Price from $9.99 to $1999.99
    src inhibitor pp1 - by Bioz Stars, 2020-10
    94/100 stars
      Buy from Supplier

    Image Search Results


    The Src inhibitor PP1 enhances migration and attenuates ligand-dependent EGFR ubiquitylation. ( A ) Human telomerase-immortalized corneal epithelial cells were pretreated without or with 12 μM ( left ) or 0.01 μM ( right ) as indicated. Cells

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: Antagonizing c-Cbl Enhances EGFR-Dependent Corneal Epithelial Homeostasis

    doi: 10.1167/iovs.14-14133

    Figure Lengend Snippet: The Src inhibitor PP1 enhances migration and attenuates ligand-dependent EGFR ubiquitylation. ( A ) Human telomerase-immortalized corneal epithelial cells were pretreated without or with 12 μM ( left ) or 0.01 μM ( right ) as indicated. Cells

    Article Snippet: The Src inhibitor PP1 (4-amino-5-[4-methylphenyl]-7-[t-butyl]pyrazolo-d-3,4-pyrimidine) (EMD Millipore, Billerica, MA, USA) was solubilized in DMSO at a concentration of 50 mM.

    Techniques: Migration

    Regulation of ERα/PI3K and ERα/Src interactions in MCF-7 cells detected by PLA MCF-7 cells transfected with control siRNA duplexes or with specific PRMT1 siRNA duplexes were controlled for PRMT1 expression by Western blot. We analysed by PLA ERα/PI3K (panels a,b) and ERα/Src dimers (panels c,d). Quantification of the number of signals was performed as described. The mean ± SEM of four experiments is shown. p -value was determined by Student's t -test. MCF-7 cells, treated or not with PP1 (5 µM) or LY294002 (20 µM) 15 min before E 2 treatment, were incubated with the vehicle or with E 2 for 5 min. Cell lysates were immunoprecipitated with anti-Src and blotted with indicated antibodies. ERα/PI3K (panels a–c) and ERα/Src (panels d–f) interactions were analysed by PLA in cells treated as described above. Quantification of the number of signals was performed for each couple as described. The mean ± SEM of four experiments is shown. p -value was determined by Student's t -test. MCF-7 cells were incubated with 1 nM of a peptide mimicking hERα 536–541 containing Y537 (Y-pep) or the corresponding phosphorylated peptide (pY-pep) 30 min before E 2 treatment. Then, cell lysates were immunoprecipitated with anti-Src and blotted with indicated antibodies. From the same experiment, ERα/PI3K (panels a,b) and ERα/Src interactions (panels c,d) were analysed by PLA. Quantification of the number of signals was performed as described. The mean ± SEM of four experiments is shown. p -value was determined by Student's t -test.

    Journal: EMBO Molecular Medicine

    Article Title: Activation of rapid oestrogen signalling in aggressive human breast cancers

    doi: 10.1002/emmm.201201615

    Figure Lengend Snippet: Regulation of ERα/PI3K and ERα/Src interactions in MCF-7 cells detected by PLA MCF-7 cells transfected with control siRNA duplexes or with specific PRMT1 siRNA duplexes were controlled for PRMT1 expression by Western blot. We analysed by PLA ERα/PI3K (panels a,b) and ERα/Src dimers (panels c,d). Quantification of the number of signals was performed as described. The mean ± SEM of four experiments is shown. p -value was determined by Student's t -test. MCF-7 cells, treated or not with PP1 (5 µM) or LY294002 (20 µM) 15 min before E 2 treatment, were incubated with the vehicle or with E 2 for 5 min. Cell lysates were immunoprecipitated with anti-Src and blotted with indicated antibodies. ERα/PI3K (panels a–c) and ERα/Src (panels d–f) interactions were analysed by PLA in cells treated as described above. Quantification of the number of signals was performed for each couple as described. The mean ± SEM of four experiments is shown. p -value was determined by Student's t -test. MCF-7 cells were incubated with 1 nM of a peptide mimicking hERα 536–541 containing Y537 (Y-pep) or the corresponding phosphorylated peptide (pY-pep) 30 min before E 2 treatment. Then, cell lysates were immunoprecipitated with anti-Src and blotted with indicated antibodies. From the same experiment, ERα/PI3K (panels a,b) and ERα/Src interactions (panels c,d) were analysed by PLA. Quantification of the number of signals was performed as described. The mean ± SEM of four experiments is shown. p -value was determined by Student's t -test.

    Article Snippet: When stated, MCF-7 cells were treated with Src inhibitors PP1 or with PI3K inhibitor LY 294002 (Calbiochem).

    Techniques: Proximity Ligation Assay, Transfection, Expressing, Western Blot, Incubation, Immunoprecipitation

    Schematic illustration of stimulation of ERK phosphorylation by β -adrenergic receptors in astrocytes. Isoproterenol (ISO) binds to β -adrenergic receptors. At high concentrations ( > 1 μ M), the activation of the receptors induces β 1 -adrenergic (red arrows), PKA-dependent “G s /G i switching,” which in turn induces an enhancement of intracellular Ca 2+ concentration by Ca 2+ release from intracellular stores. The latter activates Zn-dependent metalloproteinases (MMPs) and leads to shedding of growth factor(s). The released epidermal growth factor (EGF) receptor ligand stimulates phosphorylation of the EGF receptor in the same and adjacent cells. The downstream target of the EGF receptor, extracellular regulated kinase (ERK), shown in blue, is phosphorylated via the Ras/Raf/MEK pathway. As shown in yellow ovals the ERK phosphorylation by isoproterenol at high concentration can be inhibited by H-89, an inhibitor of protein-kinase A (PKA); by PTX, an inhibitor of G i protein; by BAPTA/AM, an intracellular Ca 2+ chelator; by GM6001, an inhibitor of Zn-dependent metalloproteinases; by AG1478, an inhibitor of the receptor-tyrosine kinase of the EGF receptor; by siRNA against β -arrestin 1 and less completely by siRNA against β -arrestin 2; and by U0126, an inhibitor of MEK, which directly phosphorylates ERK. In contrast, at low concentration (100 nM) β 2 -adrenergic (green arrows) activation of the receptors activates Src via recruitment of β -arrestin 2. Src in turn stimulates ERK phosphorylation and phosphorylates EGF receptors at different sites than β 1 -adrenergic stimulation, without involvement of the receptor-tyrosine kinase. Its ERK 1/2 phosphorylation is secondary to MEK activation, which may be induced by direct activation of Raf or Ras by Src. The ERK phosphorylation by isoproterenol at low concentration can be inhibited by siRNA against β -arrestin 2; by PP1, a Src inhibitor; and by the MEK inhibitor U0126. The effect of most of these inhibitors on MCAO-induced edema was investigated and tabulated in Table 3 .

    Journal: BioMed Research International

    Article Title: Inhibition of Brain Swelling after Ischemia-Reperfusion by β-Adrenergic Antagonists: Correlation with Increased K+ and Decreased Ca2+ Concentrations in Extracellular Fluid

    doi: 10.1155/2014/873590

    Figure Lengend Snippet: Schematic illustration of stimulation of ERK phosphorylation by β -adrenergic receptors in astrocytes. Isoproterenol (ISO) binds to β -adrenergic receptors. At high concentrations ( > 1 μ M), the activation of the receptors induces β 1 -adrenergic (red arrows), PKA-dependent “G s /G i switching,” which in turn induces an enhancement of intracellular Ca 2+ concentration by Ca 2+ release from intracellular stores. The latter activates Zn-dependent metalloproteinases (MMPs) and leads to shedding of growth factor(s). The released epidermal growth factor (EGF) receptor ligand stimulates phosphorylation of the EGF receptor in the same and adjacent cells. The downstream target of the EGF receptor, extracellular regulated kinase (ERK), shown in blue, is phosphorylated via the Ras/Raf/MEK pathway. As shown in yellow ovals the ERK phosphorylation by isoproterenol at high concentration can be inhibited by H-89, an inhibitor of protein-kinase A (PKA); by PTX, an inhibitor of G i protein; by BAPTA/AM, an intracellular Ca 2+ chelator; by GM6001, an inhibitor of Zn-dependent metalloproteinases; by AG1478, an inhibitor of the receptor-tyrosine kinase of the EGF receptor; by siRNA against β -arrestin 1 and less completely by siRNA against β -arrestin 2; and by U0126, an inhibitor of MEK, which directly phosphorylates ERK. In contrast, at low concentration (100 nM) β 2 -adrenergic (green arrows) activation of the receptors activates Src via recruitment of β -arrestin 2. Src in turn stimulates ERK phosphorylation and phosphorylates EGF receptors at different sites than β 1 -adrenergic stimulation, without involvement of the receptor-tyrosine kinase. Its ERK 1/2 phosphorylation is secondary to MEK activation, which may be induced by direct activation of Raf or Ras by Src. The ERK phosphorylation by isoproterenol at low concentration can be inhibited by siRNA against β -arrestin 2; by PP1, a Src inhibitor; and by the MEK inhibitor U0126. The effect of most of these inhibitors on MCAO-induced edema was investigated and tabulated in Table 3 .

    Article Snippet: The EGFR tyrosine kinase inhibitor, Tyrphostin AG 1478 (N-[(2R)-2-(hydroxamidocarbonymethyl)-4-methylpentanoyl]-L-tryptophan methylamide); the metalloproteinase inhibitor, GM 6001 (1,4-diamino-2,3-dicyano-1,4-bis[2-aminophenylthio]butadiene); the MEK inhibitor, U0126, (1,4-diamino-2,3-dicyano-1,4-bis[2-aminophenylthio]butadiene); and the Src inhibitor, PP1 (4-amino-5-(4-methylphenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine) were obtained from Calbiochem (La Jolla, CA, USA).

    Techniques: Activation Assay, Concentration Assay

    Effects of Src inhibitor on adiponectin-induced changes in peripheral blood monocyte-derived macrophages (PBDMs). PBDMs were preincubated with 10 µM PP1 for 30 min and then incubated with adiponectin for 6 hours (A–D). The mRNA expression levels of COX-2 (A), TIMP-1 (B), IL-6 (C), and VEGF-C (D) were quantified by real-time PCR. Values are normalized to the level of GAPDH mRNA and expressed as mean ± SEM (n = 3). ***P

    Journal: PLoS ONE

    Article Title: Adiponectin Regulates Vascular Endothelial Growth Factor-C Expression in Macrophages via Syk-ERK Pathway

    doi: 10.1371/journal.pone.0056071

    Figure Lengend Snippet: Effects of Src inhibitor on adiponectin-induced changes in peripheral blood monocyte-derived macrophages (PBDMs). PBDMs were preincubated with 10 µM PP1 for 30 min and then incubated with adiponectin for 6 hours (A–D). The mRNA expression levels of COX-2 (A), TIMP-1 (B), IL-6 (C), and VEGF-C (D) were quantified by real-time PCR. Values are normalized to the level of GAPDH mRNA and expressed as mean ± SEM (n = 3). ***P

    Article Snippet: Materials Syk inhibitor (BAY 61-3606), Src inhibitor (PP1) and MEK inhibitor (PD98059) were purchased from Calbiochem (Gibbstown, NJ).

    Techniques: Derivative Assay, Incubation, Expressing, Real-time Polymerase Chain Reaction