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polyclonal anti p jnk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc polyclonal anti p jnk
    Polyclonal Anti P Jnk, 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/polyclonal anti p jnk/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    polyclonal anti p jnk - by Bioz Stars, 2024-12
    95/100 stars

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    As denoted in , IMR-90 cells were synchronized with 2 mM double thymidine arrest, incubated with 5 μM cytochalasin D or the solvent DMSO as a control at 5.5–6 h after the second release, and collected at each indicated time point after the second release. Cell lysates were resolved by 8% SDS-PAGE and blotted. Blots were probed with (A) p-ERK1/2 and p-RSK1 (Ser 380) and re-probed with anti-ERK1/2 and anti-RSK1 to observe the total amount of each protein, (B) p-ERK1/2 and <t>p-Cdc25C</t> (Ser 216), and re-probed with anti-ERK1/2 and anti-Cdc25C. (A, B) Cell cycle progression at G2/M was monitored by detecting p-Cdc2 (Tyr 15) followed by re-probing with anti-Cdc2 to detect the total amount of Cdc2. (C) The same samples from (A) and (B) were blotted with p-Wee1 (Ser 642) and re-probed with anti-Wee1. Each blot was re-probed with anti-actin as a loading control.
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    As denoted in , IMR-90 cells were synchronized with 2 mM double thymidine arrest, incubated with 5 μM cytochalasin D or the solvent DMSO as a control at 5.5–6 h after the second release, and collected at each indicated time point after the second release. Cell lysates were resolved by 8% SDS-PAGE and blotted. Blots were probed with (A) p-ERK1/2 and p-RSK1 (Ser 380) and re-probed with anti-ERK1/2 and anti-RSK1 to observe the total amount of each protein, (B) p-ERK1/2 and <t>p-Cdc25C</t> (Ser 216), and re-probed with anti-ERK1/2 and anti-Cdc25C. (A, B) Cell cycle progression at G2/M was monitored by detecting p-Cdc2 (Tyr 15) followed by re-probing with anti-Cdc2 to detect the total amount of Cdc2. (C) The same samples from (A) and (B) were blotted with p-Wee1 (Ser 642) and re-probed with anti-Wee1. Each blot was re-probed with anti-actin as a loading control.
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    ALKBH5 induces posttranscriptional activation of PER1 to inhibit PC progression in an m6A-YTHDF2-dependent manner. ALKBH5 loss that abrogates mRNA demethylation leads to an upregulation of PER1 m6A levels in PC cells. Then, degradation of PER1 mRNA occurs on the basis of the m6A-YTHDF2 interaction. PER1 downregulation results in the inhibition of ATM phosphorylation and inactivation of the ATM-CHK2-P53/CDC25C pathways. G2/M arrest in PC cells was suppressed as a result. The PER1-related P53 downregulation and P53-dependent transcriptional inactivation of ALKBH5 indicates a feedback loop underlying the progression of PC

    Journal: Molecular Cancer

    Article Title: RNA demethylase ALKBH5 prevents pancreatic cancer progression by posttranscriptional activation of PER1 in an m6A-YTHDF2-dependent manner

    doi: 10.1186/s12943-020-01158-w

    Figure Lengend Snippet: ALKBH5 induces posttranscriptional activation of PER1 to inhibit PC progression in an m6A-YTHDF2-dependent manner. ALKBH5 loss that abrogates mRNA demethylation leads to an upregulation of PER1 m6A levels in PC cells. Then, degradation of PER1 mRNA occurs on the basis of the m6A-YTHDF2 interaction. PER1 downregulation results in the inhibition of ATM phosphorylation and inactivation of the ATM-CHK2-P53/CDC25C pathways. G2/M arrest in PC cells was suppressed as a result. The PER1-related P53 downregulation and P53-dependent transcriptional inactivation of ALKBH5 indicates a feedback loop underlying the progression of PC

    Article Snippet: The primary antibodies were rabbit monoclonal anti-ALKBH5 (ab195377, Abcam), mouse monoclonal anti-PER1 (sc-398,890, Santa Cruz), mouse monoclonal anti-p-ATM (Ser-1981; sc-47,739, Santa Cruz), rabbit monoclonal anti-p-CHK2 (Thr-68; ab32148, Abcam), rabbit polyclonal anti-p-CDC25C (Ser216; ab47322, Abcam), rabbit monoclonal anti-p-P53 (Ser-15; ab1431, Abcam), mouse monoclonal anti-P21 (sc-71,811, Santa Cruz), mouse monoclonal anti-CYCLIN B1 (ab72, Abcam), rabbit polyclonal anti-p-CDK1 (Tyr15; ab47594), mouse monoclonal anti-CDK1 (A17, Abcam) and rabbit polyclonal anti-β-ACTIN (ab8227, Abcam).

    Techniques: Activation Assay, Inhibition

    As denoted in , IMR-90 cells were synchronized with 2 mM double thymidine arrest, incubated with 5 μM cytochalasin D or the solvent DMSO as a control at 5.5–6 h after the second release, and collected at each indicated time point after the second release. Cell lysates were resolved by 8% SDS-PAGE and blotted. Blots were probed with (A) p-ERK1/2 and p-RSK1 (Ser 380) and re-probed with anti-ERK1/2 and anti-RSK1 to observe the total amount of each protein, (B) p-ERK1/2 and p-Cdc25C (Ser 216), and re-probed with anti-ERK1/2 and anti-Cdc25C. (A, B) Cell cycle progression at G2/M was monitored by detecting p-Cdc2 (Tyr 15) followed by re-probing with anti-Cdc2 to detect the total amount of Cdc2. (C) The same samples from (A) and (B) were blotted with p-Wee1 (Ser 642) and re-probed with anti-Wee1. Each blot was re-probed with anti-actin as a loading control.

    Journal: Molecules and Cells

    Article Title: Actin Dysfunction Induces Cell Cycle Delay at G2/M with Sustained ERK and RSK Activation in IMR-90 Normal Human Fibroblasts

    doi: 10.14348/molcells.2018.2266

    Figure Lengend Snippet: As denoted in , IMR-90 cells were synchronized with 2 mM double thymidine arrest, incubated with 5 μM cytochalasin D or the solvent DMSO as a control at 5.5–6 h after the second release, and collected at each indicated time point after the second release. Cell lysates were resolved by 8% SDS-PAGE and blotted. Blots were probed with (A) p-ERK1/2 and p-RSK1 (Ser 380) and re-probed with anti-ERK1/2 and anti-RSK1 to observe the total amount of each protein, (B) p-ERK1/2 and p-Cdc25C (Ser 216), and re-probed with anti-ERK1/2 and anti-Cdc25C. (A, B) Cell cycle progression at G2/M was monitored by detecting p-Cdc2 (Tyr 15) followed by re-probing with anti-Cdc2 to detect the total amount of Cdc2. (C) The same samples from (A) and (B) were blotted with p-Wee1 (Ser 642) and re-probed with anti-Wee1. Each blot was re-probed with anti-actin as a loading control.

    Article Snippet: Rabbit polyclonal p-Cdc2 (Tyr 15) (ab47594, Abcam, USA), mouse monoclonal anti-cyclin A (4656, Cell Signaling Technology, USA), rabbit polyclonal p-Cdc25C (Ser 216) (9528, Cell Signaling Technology), rabbit monoclonal anti-Cdc25C (ab32444, Abcam), rabbit polyclonal anti-β-actin (4967, Cell Signaling Technology), rabbit monoclonal p-Wee1 (Ser 642) (4910, Cell Signaling Technology), rabbit polyclonal anti-Wee1 (4936, Cell Signaling Technology), rabbit monoclonal anti-FLAG (F7425, Sigma), rabbit polyclonal p-ERK1/2 (Thr 202/Tyr 204) (9101, Cell Signaling), rabbit polyclonal anti-ERK1/2 (9102, Cell Signaling), rabbit monoclonal p-RSK1 (Ser 380) (ab32203, Abcam), rabbit polyclonal anti-RSK1 (9333, Cell Signaling), rabbit monoclonal histone H3 (4499, Cell Signaling Technology), and mouse monoclonal p-H3 (Ser 10) (9706, Cell Signaling Technology) were used in this study.

    Techniques: Incubation, SDS Page

    (A) The layout shows how the experiment was performed. IMR-90 cells were synchronized with 2 mM thymidine and transfected with DN-RSK or empty vector as described in the Materials and Methods. Cells were treated with 5 μM CD or only DMSO as a control at 5.5–6 h after the second release and collected at each indicated time point after the second release. Each cell lysate was resolved by 8% SDS-PAGE and blotted with (B) anti-FLAG and anti-actin, (C) p-ERK1/2 and p-Cdc2 (Tyr 15), (D) p-Cdc25C (Ser 216), and p-Wee1 (Ser 642). Each membrane was reprobed with anti-actin as a loading control.

    Journal: Molecules and Cells

    Article Title: Actin Dysfunction Induces Cell Cycle Delay at G2/M with Sustained ERK and RSK Activation in IMR-90 Normal Human Fibroblasts

    doi: 10.14348/molcells.2018.2266

    Figure Lengend Snippet: (A) The layout shows how the experiment was performed. IMR-90 cells were synchronized with 2 mM thymidine and transfected with DN-RSK or empty vector as described in the Materials and Methods. Cells were treated with 5 μM CD or only DMSO as a control at 5.5–6 h after the second release and collected at each indicated time point after the second release. Each cell lysate was resolved by 8% SDS-PAGE and blotted with (B) anti-FLAG and anti-actin, (C) p-ERK1/2 and p-Cdc2 (Tyr 15), (D) p-Cdc25C (Ser 216), and p-Wee1 (Ser 642). Each membrane was reprobed with anti-actin as a loading control.

    Article Snippet: Rabbit polyclonal p-Cdc2 (Tyr 15) (ab47594, Abcam, USA), mouse monoclonal anti-cyclin A (4656, Cell Signaling Technology, USA), rabbit polyclonal p-Cdc25C (Ser 216) (9528, Cell Signaling Technology), rabbit monoclonal anti-Cdc25C (ab32444, Abcam), rabbit polyclonal anti-β-actin (4967, Cell Signaling Technology), rabbit monoclonal p-Wee1 (Ser 642) (4910, Cell Signaling Technology), rabbit polyclonal anti-Wee1 (4936, Cell Signaling Technology), rabbit monoclonal anti-FLAG (F7425, Sigma), rabbit polyclonal p-ERK1/2 (Thr 202/Tyr 204) (9101, Cell Signaling), rabbit polyclonal anti-ERK1/2 (9102, Cell Signaling), rabbit monoclonal p-RSK1 (Ser 380) (ab32203, Abcam), rabbit polyclonal anti-RSK1 (9333, Cell Signaling), rabbit monoclonal histone H3 (4499, Cell Signaling Technology), and mouse monoclonal p-H3 (Ser 10) (9706, Cell Signaling Technology) were used in this study.

    Techniques: Transfection, Plasmid Preparation, SDS Page