phospho mek1 ser298  (Cell Signaling Technology Inc)

 
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    Name:
    Phospho MEK1 Ser298 Antibody
    Description:
    MEK1 and MEK2 also called MAPK or Erk kinases are dual specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation 1 3 Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221 located in the activation loop of subdomain VIII by Raf like molecules MEK1 2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx 1 4 Constitutively active forms of MEK1 2 are sufficient for the transformation of NIH 3T3 cells or the differentiation of PC 12 cells 4 MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII MEK1 is phosphorylated at Ser298 by PAK1 which facilitates signal transduction from Raf to MEK1 and Erk2 5 7 MEK1 is also phosphorylated by cdk5 at Thr286 in mitotic cells causing negative feedback of the p44 42 MAP kinase pathway 8
    Catalog Number:
    9128
    Price:
    None
    Applications:
    Western Blot
    Category:
    Primary Antibodies
    Source:
    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser298 of human MEK1. Antibodies are purified by protein A and peptide affinity chromatography.
    Reactivity:
    Human Mouse Rat Monkey
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    Structured Review

    Cell Signaling Technology Inc phospho mek1 ser298
    MEK1 and MEK2 also called MAPK or Erk kinases are dual specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation 1 3 Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221 located in the activation loop of subdomain VIII by Raf like molecules MEK1 2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx 1 4 Constitutively active forms of MEK1 2 are sufficient for the transformation of NIH 3T3 cells or the differentiation of PC 12 cells 4 MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII MEK1 is phosphorylated at Ser298 by PAK1 which facilitates signal transduction from Raf to MEK1 and Erk2 5 7 MEK1 is also phosphorylated by cdk5 at Thr286 in mitotic cells causing negative feedback of the p44 42 MAP kinase pathway 8
    https://www.bioz.com/result/phospho mek1 ser298/product/Cell Signaling Technology Inc
    Average 94 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    phospho mek1 ser298 - by Bioz Stars, 2020-09
    94/100 stars

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    Related Articles

    Incubation:

    Article Title: PAK1-mediated activation of ERK1/2 regulates lamellipodial dynamics
    Article Snippet: .. Membranes were then incubated at 4°C for 16 hours in 0.5% non-fat dried milk with rabbit polyclonal anti-PAK1, 2 and 3 (C19, Santa Cruz), anti-PAK1, anti-phospho-Thr423-PAK, anti-phospho-Ser473-Akt, anti-phospho-Thr202/Tyr204-ERK1/2, anti-ERK1/2, anti-phospho-Ser298-MEK1, anti-phospho-S217/221-MEK1, anti-phospho-Ser338-c-Raf (all from Cell Signalling Technology), anti-phospho-Thr180/Tyr182-p38 antibodies (New England Biolabs), anti-Rac1 (Upstate Biotechnology) or mouse monoclonal anti-β actin (Sigma). .. After washing, membranes were incubated with horseradish-peroxidase-conjugated anti-mouse or anti-rabbit antibodies (GE Healthcare) for 1 hr at room temperature.

    other:

    Article Title: Functional Analysis of Rare Variants Found in Schizophrenia Implicates a Critical Role for GIT1-PAK3 Signaling in Neuroplasticity
    Article Snippet: anti-phospho-AKT (Ser473) (Cell Signaling, #4058), anti-phosphop44/42 MAPK (ERK1/2) (Thr202/Tyr204) (Cell Signaling, #9101), anti-phospho-GRIA1 (Ser845) (Millipore, #04–1073), anti-phospho-MEK1 (MAPK2K1) (Ser298) (Cell Signaling, #9128), anti-phospho-PAK1 (Ser144)/PAK2 (Ser141)/PAK3 (Ser139) (Cell Signaling, #2606), anti-phospho-PAK1 (Ser199/204)/PAK2 (Ser192/197)/PAK3 (Ser200/205) (Cell Signaling, #2605), anti-phospho-PAK1 (Thr423)/PAK2 (Thr402)/PAK3 (Thr421) (Cell Signaling, #2601), anti-phospho-SRC Family (Tyr416) (Cell Signaling, #2101).).

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  • 93
    Cell Signaling Technology Inc anti phospho ser298 mek1
    PAK1 regulates CSF-1-induced MAPK activation but not macrophage differentiation or chemotaxis. A, lysates from Wt and PAK1 −/− BMMs were immunoblotted for PAK1 and PAK2 using a group 1 specific polyclonal antibody (C19) or a PAK1-specific polyclonal antibody. β-actin was used as a loading control. B, Flow cytometry analysis of Wt and PAK1 −/− BMMs surface F4/80 expression levels, detected using a FITC-F4/80 antibody. Background fluorescence levels were established with a FITC-IgG2b negative control antibody. C, Wt BMMs were stimulated with 33 ng/ml CSF-1, and lysates were immunoblotted for phospho-Thr423-PAK1 and β-actin as a loading control. D, Wt and PAK1 −/− BMMs were stimulated with 33 ng/ml CSF-1 and lysates were immunoblotted for phospho-Ser473-Akt, phospho-Thr202/Tyr204-ERK1/2, phospho-Thr180/Tyr182-p38 and <t>phospho-Ser298-MEK1/2</t> levels. β-actin was used as a loading control. Western blots are representative of three separate experiments. E, To investigate chemotaxis, 1×10 5 Wt or PAK1 −/− BMMs were placed into the upper chamber of a Transwell with 33 ng/ml CSF-1 in the lower chamber. After 24 hours, cell migration was evaluated by determining the cell number in ten randomly selected fields. Results are the mean +/− s.e.m. of 3 experiments performed in triplicate.
    Anti Phospho Ser298 Mek1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho ser298 mek1/product/Cell Signaling Technology Inc
    Average 93 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    anti phospho ser298 mek1 - by Bioz Stars, 2020-09
    93/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc phospho mek1
    PAK1 regulates CSF-1-induced MAPK activation but not macrophage differentiation or chemotaxis. A, lysates from Wt and PAK1 −/− BMMs were immunoblotted for PAK1 and PAK2 using a group 1 specific polyclonal antibody (C19) or a PAK1-specific polyclonal antibody. β-actin was used as a loading control. B, Flow cytometry analysis of Wt and PAK1 −/− BMMs surface F4/80 expression levels, detected using a FITC-F4/80 antibody. Background fluorescence levels were established with a FITC-IgG2b negative control antibody. C, Wt BMMs were stimulated with 33 ng/ml CSF-1, and lysates were immunoblotted for phospho-Thr423-PAK1 and β-actin as a loading control. D, Wt and PAK1 −/− BMMs were stimulated with 33 ng/ml CSF-1 and lysates were immunoblotted for phospho-Ser473-Akt, phospho-Thr202/Tyr204-ERK1/2, phospho-Thr180/Tyr182-p38 and <t>phospho-Ser298-MEK1/2</t> levels. β-actin was used as a loading control. Western blots are representative of three separate experiments. E, To investigate chemotaxis, 1×10 5 Wt or PAK1 −/− BMMs were placed into the upper chamber of a Transwell with 33 ng/ml CSF-1 in the lower chamber. After 24 hours, cell migration was evaluated by determining the cell number in ten randomly selected fields. Results are the mean +/− s.e.m. of 3 experiments performed in triplicate.
    Phospho Mek1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho mek1/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phospho mek1 - by Bioz Stars, 2020-09
    93/100 stars
      Buy from Supplier

    Image Search Results


    PAK1 regulates CSF-1-induced MAPK activation but not macrophage differentiation or chemotaxis. A, lysates from Wt and PAK1 −/− BMMs were immunoblotted for PAK1 and PAK2 using a group 1 specific polyclonal antibody (C19) or a PAK1-specific polyclonal antibody. β-actin was used as a loading control. B, Flow cytometry analysis of Wt and PAK1 −/− BMMs surface F4/80 expression levels, detected using a FITC-F4/80 antibody. Background fluorescence levels were established with a FITC-IgG2b negative control antibody. C, Wt BMMs were stimulated with 33 ng/ml CSF-1, and lysates were immunoblotted for phospho-Thr423-PAK1 and β-actin as a loading control. D, Wt and PAK1 −/− BMMs were stimulated with 33 ng/ml CSF-1 and lysates were immunoblotted for phospho-Ser473-Akt, phospho-Thr202/Tyr204-ERK1/2, phospho-Thr180/Tyr182-p38 and phospho-Ser298-MEK1/2 levels. β-actin was used as a loading control. Western blots are representative of three separate experiments. E, To investigate chemotaxis, 1×10 5 Wt or PAK1 −/− BMMs were placed into the upper chamber of a Transwell with 33 ng/ml CSF-1 in the lower chamber. After 24 hours, cell migration was evaluated by determining the cell number in ten randomly selected fields. Results are the mean +/− s.e.m. of 3 experiments performed in triplicate.

    Journal: Journal of cell science

    Article Title: PAK1-mediated activation of ERK1/2 regulates lamellipodial dynamics

    doi: 10.1242/jcs.027680

    Figure Lengend Snippet: PAK1 regulates CSF-1-induced MAPK activation but not macrophage differentiation or chemotaxis. A, lysates from Wt and PAK1 −/− BMMs were immunoblotted for PAK1 and PAK2 using a group 1 specific polyclonal antibody (C19) or a PAK1-specific polyclonal antibody. β-actin was used as a loading control. B, Flow cytometry analysis of Wt and PAK1 −/− BMMs surface F4/80 expression levels, detected using a FITC-F4/80 antibody. Background fluorescence levels were established with a FITC-IgG2b negative control antibody. C, Wt BMMs were stimulated with 33 ng/ml CSF-1, and lysates were immunoblotted for phospho-Thr423-PAK1 and β-actin as a loading control. D, Wt and PAK1 −/− BMMs were stimulated with 33 ng/ml CSF-1 and lysates were immunoblotted for phospho-Ser473-Akt, phospho-Thr202/Tyr204-ERK1/2, phospho-Thr180/Tyr182-p38 and phospho-Ser298-MEK1/2 levels. β-actin was used as a loading control. Western blots are representative of three separate experiments. E, To investigate chemotaxis, 1×10 5 Wt or PAK1 −/− BMMs were placed into the upper chamber of a Transwell with 33 ng/ml CSF-1 in the lower chamber. After 24 hours, cell migration was evaluated by determining the cell number in ten randomly selected fields. Results are the mean +/− s.e.m. of 3 experiments performed in triplicate.

    Article Snippet: Membranes were then incubated at 4°C for 16 hours in 0.5% non-fat dried milk with rabbit polyclonal anti-PAK1, 2 and 3 (C19, Santa Cruz), anti-PAK1, anti-phospho-Thr423-PAK, anti-phospho-Ser473-Akt, anti-phospho-Thr202/Tyr204-ERK1/2, anti-ERK1/2, anti-phospho-Ser298-MEK1, anti-phospho-S217/221-MEK1, anti-phospho-Ser338-c-Raf (all from Cell Signalling Technology), anti-phospho-Thr180/Tyr182-p38 antibodies (New England Biolabs), anti-Rac1 (Upstate Biotechnology) or mouse monoclonal anti-β actin (Sigma).

    Techniques: Activation Assay, Chemotaxis Assay, Flow Cytometry, Cytometry, Expressing, Fluorescence, Negative Control, Western Blot, Migration

    PAK1 promotes ERK1/2 activation at the cell periphery. A, Wt and PAK1 −/− BMMs were adhered onto tissue culture plastic for 10 minutes in growth medium. Lysates were immunoblotted for phospho-Thr202/Tyr204-ERK1/2, phospho-Thr180/Tyr182-p38, phospho-Ser298-MEK1/2 and total ERK1/2. Densitometry quantification of phosphorylated ERK1/2 and p38 levels equalised to total ERK1/2 protein levels are shown (a.u., arbitrary units). Data show the mean +/− s.d. of two separate experiments. B, Wt and PAK1 −/− BMMs were plated onto glass coverslips for 10 minutes in growth medium and were stained using an ERK1/2 antibody and TRITC-phalloidin to visualise F-actin. Cells were imaged by confocal microscopy. ERK1/2 localisation was quantified by determining the number of cells with ERK1/2 staining at the periphery. The mean +/− s.d. is shown for two separate experiments, n = 60 (Wt) and 45 (PAK1 −/− ). C, BMMs were stained with a phospho-Thr202/Tyr204-ERK1/2 antibody (P-ERK1/2) and TRITC-phalloidin (F-actin). Localisation of phospho-ERK1/2 was quantified by determining the number of cells with staining at the cell periphery. The mean +/− s.d. is shown for two separate experiments, n = 39 (Wt) and 62 (PAK1 −/− ). D, Wt and PAK1−/− BMMs were kept in suspension or adhered onto tissue culture plastic for 10 minutes in growth medium. Lysates were immunoblotted for phospho-Ser217/221-MEK1/2, and total ERK1/2 as a loading control. Densitometry quantification of phosphorylated MEK1/2 equalised to total ERK1/2 protein levels is shown (a.u., arbitrary units). Data show the mean +/− s.d. of two separate experiments.

    Journal: Journal of cell science

    Article Title: PAK1-mediated activation of ERK1/2 regulates lamellipodial dynamics

    doi: 10.1242/jcs.027680

    Figure Lengend Snippet: PAK1 promotes ERK1/2 activation at the cell periphery. A, Wt and PAK1 −/− BMMs were adhered onto tissue culture plastic for 10 minutes in growth medium. Lysates were immunoblotted for phospho-Thr202/Tyr204-ERK1/2, phospho-Thr180/Tyr182-p38, phospho-Ser298-MEK1/2 and total ERK1/2. Densitometry quantification of phosphorylated ERK1/2 and p38 levels equalised to total ERK1/2 protein levels are shown (a.u., arbitrary units). Data show the mean +/− s.d. of two separate experiments. B, Wt and PAK1 −/− BMMs were plated onto glass coverslips for 10 minutes in growth medium and were stained using an ERK1/2 antibody and TRITC-phalloidin to visualise F-actin. Cells were imaged by confocal microscopy. ERK1/2 localisation was quantified by determining the number of cells with ERK1/2 staining at the periphery. The mean +/− s.d. is shown for two separate experiments, n = 60 (Wt) and 45 (PAK1 −/− ). C, BMMs were stained with a phospho-Thr202/Tyr204-ERK1/2 antibody (P-ERK1/2) and TRITC-phalloidin (F-actin). Localisation of phospho-ERK1/2 was quantified by determining the number of cells with staining at the cell periphery. The mean +/− s.d. is shown for two separate experiments, n = 39 (Wt) and 62 (PAK1 −/− ). D, Wt and PAK1−/− BMMs were kept in suspension or adhered onto tissue culture plastic for 10 minutes in growth medium. Lysates were immunoblotted for phospho-Ser217/221-MEK1/2, and total ERK1/2 as a loading control. Densitometry quantification of phosphorylated MEK1/2 equalised to total ERK1/2 protein levels is shown (a.u., arbitrary units). Data show the mean +/− s.d. of two separate experiments.

    Article Snippet: Membranes were then incubated at 4°C for 16 hours in 0.5% non-fat dried milk with rabbit polyclonal anti-PAK1, 2 and 3 (C19, Santa Cruz), anti-PAK1, anti-phospho-Thr423-PAK, anti-phospho-Ser473-Akt, anti-phospho-Thr202/Tyr204-ERK1/2, anti-ERK1/2, anti-phospho-Ser298-MEK1, anti-phospho-S217/221-MEK1, anti-phospho-Ser338-c-Raf (all from Cell Signalling Technology), anti-phospho-Thr180/Tyr182-p38 antibodies (New England Biolabs), anti-Rac1 (Upstate Biotechnology) or mouse monoclonal anti-β actin (Sigma).

    Techniques: Activation Assay, Staining, Confocal Microscopy