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phospho c jun ser63 blocking peptide  (New England Biolabs)


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    New England Biolabs phospho c jun ser63 blocking peptide
    Galectin-1 (Gal-1)-induced phosphorylation of c-Jun N-terminal kinase 1 (JNK1) and JNK2 ( a ) and JNK activation with c-Jun(1-169)-GST ( b ), and c-Jun(1-89)-GST ( c ) as kinase substrates. Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with protein kinase C-θ (PKCθ) inhibitor and PKCδ inhibitor rottlerin for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, as well as with the ATP-competitive inhibitor for JNK SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) myricetin for 30 min as indicated. Control cells were incubated in medium alone. Cells were then stimulated with gal-1 without and in the presence of lactose or asialofetuin as indicated in panels a , b , and c . ( a ) For immunoblot analysis cell extract proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Blots were analyzed with a phospho-JNK (Thr183/Tyr185) monoclonal antibody (mAb). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. ( b ) After termination of the kinase reactions with 3 × SDS sample buffer, samples were electrophoretically separated and blotted on PVDF membranes. The [ 32 P]-labeled substrate c-Jun(1-169)-GST was recorded by autoradiography. To control loading, we separated 50 μ g cell extract protein/lane and blotted it on PVDF membranes. Membranes were probed with a JNK1 polyclonal antibody (pAb). ( c ) After termination of the kinase reactions, samples were separated and blotted on Hybond ECL membranes. Blots were analyzed for substrate phosphorylation with a phospho-c-Jun <t>(Ser63)</t> pAb. The bands were luminographically visualized on X-ray films using ECL Plus reagents. Shown are representative blots from three independent experiments
    Phospho C Jun Ser63 Blocking Peptide, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/phospho+c+jun+ser63+blocking+peptide/pmc03032336-103-24-54
    Average 86 stars, based on 1 article reviews
    phospho c jun ser63 blocking peptide - by Bioz Stars, 2026-10
    86/100 stars

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    1) Product Images from "Role of the JNK/c-Jun/AP-1 signaling pathway in galectin-1-induced T-cell death"

    Article Title: Role of the JNK/c-Jun/AP-1 signaling pathway in galectin-1-induced T-cell death

    Journal: Cell Death & Disease

    doi: 10.1038/cddis.2010.1

    Galectin-1 (Gal-1)-induced phosphorylation of c-Jun N-terminal kinase 1 (JNK1) and JNK2 ( a ) and JNK activation with c-Jun(1-169)-GST ( b ), and c-Jun(1-89)-GST ( c ) as kinase substrates. Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with protein kinase C-θ (PKCθ) inhibitor and PKCδ inhibitor rottlerin for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, as well as with the ATP-competitive inhibitor for JNK SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) myricetin for 30 min as indicated. Control cells were incubated in medium alone. Cells were then stimulated with gal-1 without and in the presence of lactose or asialofetuin as indicated in panels a , b , and c . ( a ) For immunoblot analysis cell extract proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Blots were analyzed with a phospho-JNK (Thr183/Tyr185) monoclonal antibody (mAb). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. ( b ) After termination of the kinase reactions with 3 × SDS sample buffer, samples were electrophoretically separated and blotted on PVDF membranes. The [ 32 P]-labeled substrate c-Jun(1-169)-GST was recorded by autoradiography. To control loading, we separated 50 μ g cell extract protein/lane and blotted it on PVDF membranes. Membranes were probed with a JNK1 polyclonal antibody (pAb). ( c ) After termination of the kinase reactions, samples were separated and blotted on Hybond ECL membranes. Blots were analyzed for substrate phosphorylation with a phospho-c-Jun (Ser63) pAb. The bands were luminographically visualized on X-ray films using ECL Plus reagents. Shown are representative blots from three independent experiments
    Figure Legend Snippet: Galectin-1 (Gal-1)-induced phosphorylation of c-Jun N-terminal kinase 1 (JNK1) and JNK2 ( a ) and JNK activation with c-Jun(1-169)-GST ( b ), and c-Jun(1-89)-GST ( c ) as kinase substrates. Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with protein kinase C-θ (PKCθ) inhibitor and PKCδ inhibitor rottlerin for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, as well as with the ATP-competitive inhibitor for JNK SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) myricetin for 30 min as indicated. Control cells were incubated in medium alone. Cells were then stimulated with gal-1 without and in the presence of lactose or asialofetuin as indicated in panels a , b , and c . ( a ) For immunoblot analysis cell extract proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Blots were analyzed with a phospho-JNK (Thr183/Tyr185) monoclonal antibody (mAb). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. ( b ) After termination of the kinase reactions with 3 × SDS sample buffer, samples were electrophoretically separated and blotted on PVDF membranes. The [ 32 P]-labeled substrate c-Jun(1-169)-GST was recorded by autoradiography. To control loading, we separated 50 μ g cell extract protein/lane and blotted it on PVDF membranes. Membranes were probed with a JNK1 polyclonal antibody (pAb). ( c ) After termination of the kinase reactions, samples were separated and blotted on Hybond ECL membranes. Blots were analyzed for substrate phosphorylation with a phospho-c-Jun (Ser63) pAb. The bands were luminographically visualized on X-ray films using ECL Plus reagents. Shown are representative blots from three independent experiments

    Techniques Used: Activation Assay, Incubation, Western Blot, Polyacrylamide Gel Electrophoresis, SDS Page, Expressing, Labeling, Autoradiography

    Galectin-1 (Gal-1)-induced phosphorylation kinetics of c-Jun and inhibition of c-Jun Ser63/73 phosphorylation with SP600125, protein kinase C-θ (PKCθ) inhibitor, and lactose ( A ) and with desipramine, imipramine, and myricetin ( B ). Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with PKCθ inhibitor for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, and with the ATP-competitive inhibitor for c-Jun N-terminal kinase (JNK) SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) with myricetin for 30 min as indicated. Control cells were incubated in medium alone. Non- and inhibitor-treated cells were then stimulated with gal-1 without and in the presence of lactose. Cell extract proteins were analyzed on blots with a phospho-c-Jun (Ser63) polyclonal antibody (pAb) and a phospho-c-Jun (Ser73) pAb without ( A , panel a; B ) and in the presence of c-Jun (Ser63) and c-Jun (Ser73) blocking peptides at 4 μ g/ml ( A , panel b). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. Shown are representative blots from three independent experiments
    Figure Legend Snippet: Galectin-1 (Gal-1)-induced phosphorylation kinetics of c-Jun and inhibition of c-Jun Ser63/73 phosphorylation with SP600125, protein kinase C-θ (PKCθ) inhibitor, and lactose ( A ) and with desipramine, imipramine, and myricetin ( B ). Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with PKCθ inhibitor for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, and with the ATP-competitive inhibitor for c-Jun N-terminal kinase (JNK) SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) with myricetin for 30 min as indicated. Control cells were incubated in medium alone. Non- and inhibitor-treated cells were then stimulated with gal-1 without and in the presence of lactose. Cell extract proteins were analyzed on blots with a phospho-c-Jun (Ser63) polyclonal antibody (pAb) and a phospho-c-Jun (Ser73) pAb without ( A , panel a; B ) and in the presence of c-Jun (Ser63) and c-Jun (Ser73) blocking peptides at 4 μ g/ml ( A , panel b). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. Shown are representative blots from three independent experiments

    Techniques Used: Inhibition, Incubation, Blocking Assay, Expressing

    Related Articles

    Blocking Assay:

    Article Title: Role of the JNK/c-Jun/AP-1 signaling pathway in galectin-1-induced T-cell death
    Article Snippet: The reporter gene constructs, pAP1(PMA)-TA-Luc and pTA-Luc, were from Clontech (Heidelberg, Germany) and actin (1-19) pAb, double-stranded AP-1 consensus (sc-2501), and the mutant (sc-2514) oligonucleotide were from Santa Cruz Biotechnology (Heidelberg, Germany). .. Bad pAb, Bcl-2 pAb, phospho-Bcl-2 (Ser70) monoclonal antibody (mAb), phospho-Bcl-2 (Thr56) pAb, cleaved caspase-9 (Asp315) pAb, cleaved caspase-3 (Asp175) rabbit mAb, phospho-c-Jun (Ser63) pAb, phospho-c-Jun (Ser63) blocking peptide, phospho-c-Jun (Ser73) pAb, phospho-c-Jun (Ser73) blocking peptide, phospho-MKK3/6 (Ser189/Thr207) mAb, phospho-MKK7 (Ser271/Thr275) pAb, phospho-JNK (Thr183/Tyr185) mAb, phospho-MKK4 (Ser257/Thr261) pAb, and the JNK assay kit were from New England Biolabs (Frankfurt, Germany). .. The Trans-AM AP-1 transcription factor assay kit was from Active Motif North America (Carlsbad, CA, USA).



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    phospho c jun ser63 blocking peptide  (New England Biolabs)
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    New England Biolabs phospho c jun ser63 blocking peptide
    Galectin-1 (Gal-1)-induced phosphorylation of c-Jun N-terminal kinase 1 (JNK1) and JNK2 ( a ) and JNK activation with c-Jun(1-169)-GST ( b ), and c-Jun(1-89)-GST ( c ) as kinase substrates. Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with protein kinase C-θ (PKCθ) inhibitor and PKCδ inhibitor rottlerin for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, as well as with the ATP-competitive inhibitor for JNK SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) myricetin for 30 min as indicated. Control cells were incubated in medium alone. Cells were then stimulated with gal-1 without and in the presence of lactose or asialofetuin as indicated in panels a , b , and c . ( a ) For immunoblot analysis cell extract proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Blots were analyzed with a phospho-JNK (Thr183/Tyr185) monoclonal antibody (mAb). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. ( b ) After termination of the kinase reactions with 3 × SDS sample buffer, samples were electrophoretically separated and blotted on PVDF membranes. The [ 32 P]-labeled substrate c-Jun(1-169)-GST was recorded by autoradiography. To control loading, we separated 50 μ g cell extract protein/lane and blotted it on PVDF membranes. Membranes were probed with a JNK1 polyclonal antibody (pAb). ( c ) After termination of the kinase reactions, samples were separated and blotted on Hybond ECL membranes. Blots were analyzed for substrate phosphorylation with a phospho-c-Jun <t>(Ser63)</t> pAb. The bands were luminographically visualized on X-ray films using ECL Plus reagents. Shown are representative blots from three independent experiments
    Phospho C Jun Ser63 Blocking Peptide, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/phospho+c+jun+ser63+blocking+peptide/pmc03032336-103-24-54
    Average 86 stars, based on 1 article reviews
    phospho c jun ser63 blocking peptide - by Bioz Stars, 2026-10
    86/100 stars
    		  Buy from Supplier

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    Galectin-1 (Gal-1)-induced phosphorylation of c-Jun N-terminal kinase 1 (JNK1) and JNK2 ( a ) and JNK activation with c-Jun(1-169)-GST ( b ), and c-Jun(1-89)-GST ( c ) as kinase substrates. Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with protein kinase C-θ (PKCθ) inhibitor and PKCδ inhibitor rottlerin for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, as well as with the ATP-competitive inhibitor for JNK SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) myricetin for 30 min as indicated. Control cells were incubated in medium alone. Cells were then stimulated with gal-1 without and in the presence of lactose or asialofetuin as indicated in panels a , b , and c . ( a ) For immunoblot analysis cell extract proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Blots were analyzed with a phospho-JNK (Thr183/Tyr185) monoclonal antibody (mAb). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. ( b ) After termination of the kinase reactions with 3 × SDS sample buffer, samples were electrophoretically separated and blotted on PVDF membranes. The [ 32 P]-labeled substrate c-Jun(1-169)-GST was recorded by autoradiography. To control loading, we separated 50 μ g cell extract protein/lane and blotted it on PVDF membranes. Membranes were probed with a JNK1 polyclonal antibody (pAb). ( c ) After termination of the kinase reactions, samples were separated and blotted on Hybond ECL membranes. Blots were analyzed for substrate phosphorylation with a phospho-c-Jun (Ser63) pAb. The bands were luminographically visualized on X-ray films using ECL Plus reagents. Shown are representative blots from three independent experiments

    Journal: Cell Death & Disease

    Article Title: Role of the JNK/c-Jun/AP-1 signaling pathway in galectin-1-induced T-cell death

    doi: 10.1038/cddis.2010.1

    Figure Lengend Snippet: Galectin-1 (Gal-1)-induced phosphorylation of c-Jun N-terminal kinase 1 (JNK1) and JNK2 ( a ) and JNK activation with c-Jun(1-169)-GST ( b ), and c-Jun(1-89)-GST ( c ) as kinase substrates. Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with protein kinase C-θ (PKCθ) inhibitor and PKCδ inhibitor rottlerin for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, as well as with the ATP-competitive inhibitor for JNK SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) myricetin for 30 min as indicated. Control cells were incubated in medium alone. Cells were then stimulated with gal-1 without and in the presence of lactose or asialofetuin as indicated in panels a , b , and c . ( a ) For immunoblot analysis cell extract proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Blots were analyzed with a phospho-JNK (Thr183/Tyr185) monoclonal antibody (mAb). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. ( b ) After termination of the kinase reactions with 3 × SDS sample buffer, samples were electrophoretically separated and blotted on PVDF membranes. The [ 32 P]-labeled substrate c-Jun(1-169)-GST was recorded by autoradiography. To control loading, we separated 50 μ g cell extract protein/lane and blotted it on PVDF membranes. Membranes were probed with a JNK1 polyclonal antibody (pAb). ( c ) After termination of the kinase reactions, samples were separated and blotted on Hybond ECL membranes. Blots were analyzed for substrate phosphorylation with a phospho-c-Jun (Ser63) pAb. The bands were luminographically visualized on X-ray films using ECL Plus reagents. Shown are representative blots from three independent experiments

    Article Snippet: Bad pAb, Bcl-2 pAb, phospho-Bcl-2 (Ser70) monoclonal antibody (mAb), phospho-Bcl-2 (Thr56) pAb, cleaved caspase-9 (Asp315) pAb, cleaved caspase-3 (Asp175) rabbit mAb, phospho-c-Jun (Ser63) pAb, phospho-c-Jun (Ser63) blocking peptide, phospho-c-Jun (Ser73) pAb, phospho-c-Jun (Ser73) blocking peptide, phospho-MKK3/6 (Ser189/Thr207) mAb, phospho-MKK7 (Ser271/Thr275) pAb, phospho-JNK (Thr183/Tyr185) mAb, phospho-MKK4 (Ser257/Thr261) pAb, and the JNK assay kit were from New England Biolabs (Frankfurt, Germany).

    Techniques: Activation Assay, Incubation, Western Blot, Polyacrylamide Gel Electrophoresis, SDS Page, Expressing, Labeling, Autoradiography

    Galectin-1 (Gal-1)-induced phosphorylation kinetics of c-Jun and inhibition of c-Jun Ser63/73 phosphorylation with SP600125, protein kinase C-θ (PKCθ) inhibitor, and lactose ( A ) and with desipramine, imipramine, and myricetin ( B ). Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with PKCθ inhibitor for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, and with the ATP-competitive inhibitor for c-Jun N-terminal kinase (JNK) SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) with myricetin for 30 min as indicated. Control cells were incubated in medium alone. Non- and inhibitor-treated cells were then stimulated with gal-1 without and in the presence of lactose. Cell extract proteins were analyzed on blots with a phospho-c-Jun (Ser63) polyclonal antibody (pAb) and a phospho-c-Jun (Ser73) pAb without ( A , panel a; B ) and in the presence of c-Jun (Ser63) and c-Jun (Ser73) blocking peptides at 4 μ g/ml ( A , panel b). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. Shown are representative blots from three independent experiments

    Journal: Cell Death & Disease

    Article Title: Role of the JNK/c-Jun/AP-1 signaling pathway in galectin-1-induced T-cell death

    doi: 10.1038/cddis.2010.1

    Figure Lengend Snippet: Galectin-1 (Gal-1)-induced phosphorylation kinetics of c-Jun and inhibition of c-Jun Ser63/73 phosphorylation with SP600125, protein kinase C-θ (PKCθ) inhibitor, and lactose ( A ) and with desipramine, imipramine, and myricetin ( B ). Jurkat E6.1 cells (2 × 10 6 per ml RPMI 1640 medium) were incubated with PKCθ inhibitor for 1 h, with the sphingomyelinase inhibitors desipramine and imipramine for 2 h, and with the ATP-competitive inhibitor for c-Jun N-terminal kinase (JNK) SP600125 and for mitogen-activated protein kinase kinase 4 (MKK4) with myricetin for 30 min as indicated. Control cells were incubated in medium alone. Non- and inhibitor-treated cells were then stimulated with gal-1 without and in the presence of lactose. Cell extract proteins were analyzed on blots with a phospho-c-Jun (Ser63) polyclonal antibody (pAb) and a phospho-c-Jun (Ser73) pAb without ( A , panel a; B ) and in the presence of c-Jun (Ser63) and c-Jun (Ser73) blocking peptides at 4 μ g/ml ( A , panel b). The bands were luminographically visualized on X-ray films using ECL Plus reagents. Equal loading of gel lanes was verified by reprobing the blots for expression of β -actin. Shown are representative blots from three independent experiments

    Article Snippet: Bad pAb, Bcl-2 pAb, phospho-Bcl-2 (Ser70) monoclonal antibody (mAb), phospho-Bcl-2 (Thr56) pAb, cleaved caspase-9 (Asp315) pAb, cleaved caspase-3 (Asp175) rabbit mAb, phospho-c-Jun (Ser63) pAb, phospho-c-Jun (Ser63) blocking peptide, phospho-c-Jun (Ser73) pAb, phospho-c-Jun (Ser73) blocking peptide, phospho-MKK3/6 (Ser189/Thr207) mAb, phospho-MKK7 (Ser271/Thr275) pAb, phospho-JNK (Thr183/Tyr185) mAb, phospho-MKK4 (Ser257/Thr261) pAb, and the JNK assay kit were from New England Biolabs (Frankfurt, Germany).

    Techniques: Inhibition, Incubation, Blocking Assay, Expressing