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cap1  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc cap1
    Cap1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/cap1/CAP1+Rabbit+mAb/pm41772738-96-28-30
    Average 94 stars, based on 5 article reviews
    cap1 - by Bioz Stars, 2026-10
    94/100 stars

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    Related Articles

    Migration:

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway.
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    In Vitro:

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway.
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    WST-1 Assay:

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway.
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Wound Healing Assay:

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway.
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Invasion Assay:

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway.
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Western Blot:

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway.
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Enzyme-linked Immunosorbent Assay:

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway.
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Two Tailed Test:

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway.
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Control:

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway.
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.

    Article Title: Ellagic acid is associated with reduced pancreatic carcinogenesis and modulation of the IL-6/STAT3 pathway
    Article Snippet: Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).Proteins separated on 10% or 12% acrylamide gels were transferred onto nitrocellulose blotting membranes (GE Healthcare UK Ltd., Buckinghamshire, UK).. The following antibodies were used: phospho-STAT3 (Tyr705) (1:1000, #9145, CST), STAT3 (1:1000, #8768, CST), phospho-NF-κB (Ser 536, 1:1000, #3033, CST), NF-κB (1:1000, #8242, CST), Cyclin D1(1:1000, #2922, CST), CAP1(1:1000, #47055, CST), SNAIL(1:1000, #3879, CST), IL-6 (1:1000, I2123, Merck), phospho-JAK2 (Tyr1007/1008) (1:1000, #3771, CST), JAK2 (1:1000, #3230, CST), Cleaved-Caspase 3 (Asp175) (1:1000, #9661, CST), Caspase 3 (1:1000, #9662, CST), β-Actin (1:5000, A5316, Merck).. Band intensity was quantified using Image J.Band intensity was quantified using Image J.



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    Addgene inc cap1
    (A) Interaction between OST1 and <t>CAP1</t> validated by BiFC assays. The images are the representative of three independent experiments ( n = 3). OST1 K50R indicates the kinase-dead form of OST1. NLS-mCherry indicates nuclear localization. We repeated the experiment four times with similar results and at least 8 leaves were observed per time. Scale bars = 50 μm. (B) Co-IP assay was performed to test the interaction of CAP1 with OST1 and OST1 K50R , detected with anti-Flag and anti-MYC antibodies. GFP-2Flag was set as a negative control. The images are the representative of two independent experiments ( n = 2) with the same results. (C) In vitro kinase assay showing the phosphorylation of CAP1 by OST1. The phosphorylation <t>of</t> <t>His-CAP1</t> was examined using an anti-thiophosphate ester (thioP). The loading amounts of His-CAP1 and GST-OST1 were detected using Coomassie Brilliant Blue (CBB) staining. (D) OST1 phosphorylates CAP1 in vitro . CAP1 from OE- CAP1 and ost1 :OE- CAP1 seedlings was immunoprecipitated and separated by a Pho-tag-PAGE gel, then analyzed with anti-Flag antibody. The IP input was analyzed by regular SDS-PAGE gel with anti-Flag antibody. (E) The phospho-sites of CAP1 identified from mass spectrometry analysis. (F) Phosphorylation levels of mutation of phosphosites (serine to alanine, S to A) by OST1, detected with anti-phosphoserine antibody. The loading amounts of His-CAP1 and GST-OST1 were detected by CBB staining. Values indicate mean ± SD ( n = 3 biological repeats). CAP1 (3 μM), ADF4 (3 μM), RCAR12 (1 μM), ABA (1 μM), F-actin (3 μM).
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    Cyagen Biosciences conditional knockdown cap1 mice 83 nphs2 cre
    (A) Interaction between OST1 and <t>CAP1</t> validated by BiFC assays. The images are the representative of three independent experiments ( n = 3). OST1 K50R indicates the kinase-dead form of OST1. NLS-mCherry indicates nuclear localization. We repeated the experiment four times with similar results and at least 8 leaves were observed per time. Scale bars = 50 μm. (B) Co-IP assay was performed to test the interaction of CAP1 with OST1 and OST1 K50R , detected with anti-Flag and anti-MYC antibodies. GFP-2Flag was set as a negative control. The images are the representative of two independent experiments ( n = 2) with the same results. (C) In vitro kinase assay showing the phosphorylation of CAP1 by OST1. The phosphorylation <t>of</t> <t>His-CAP1</t> was examined using an anti-thiophosphate ester (thioP). The loading amounts of His-CAP1 and GST-OST1 were detected using Coomassie Brilliant Blue (CBB) staining. (D) OST1 phosphorylates CAP1 in vitro . CAP1 from OE- CAP1 and ost1 :OE- CAP1 seedlings was immunoprecipitated and separated by a Pho-tag-PAGE gel, then analyzed with anti-Flag antibody. The IP input was analyzed by regular SDS-PAGE gel with anti-Flag antibody. (E) The phospho-sites of CAP1 identified from mass spectrometry analysis. (F) Phosphorylation levels of mutation of phosphosites (serine to alanine, S to A) by OST1, detected with anti-phosphoserine antibody. The loading amounts of His-CAP1 and GST-OST1 were detected by CBB staining. Values indicate mean ± SD ( n = 3 biological repeats). CAP1 (3 μM), ADF4 (3 μM), RCAR12 (1 μM), ABA (1 μM), F-actin (3 μM).
    Conditional Knockdown Cap1 Mice 83 Nphs2 Cre, supplied by Cyagen Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology sirna
    (A) Interaction between OST1 and <t>CAP1</t> validated by BiFC assays. The images are the representative of three independent experiments ( n = 3). OST1 K50R indicates the kinase-dead form of OST1. NLS-mCherry indicates nuclear localization. We repeated the experiment four times with similar results and at least 8 leaves were observed per time. Scale bars = 50 μm. (B) Co-IP assay was performed to test the interaction of CAP1 with OST1 and OST1 K50R , detected with anti-Flag and anti-MYC antibodies. GFP-2Flag was set as a negative control. The images are the representative of two independent experiments ( n = 2) with the same results. (C) In vitro kinase assay showing the phosphorylation of CAP1 by OST1. The phosphorylation <t>of</t> <t>His-CAP1</t> was examined using an anti-thiophosphate ester (thioP). The loading amounts of His-CAP1 and GST-OST1 were detected using Coomassie Brilliant Blue (CBB) staining. (D) OST1 phosphorylates CAP1 in vitro . CAP1 from OE- CAP1 and ost1 :OE- CAP1 seedlings was immunoprecipitated and separated by a Pho-tag-PAGE gel, then analyzed with anti-Flag antibody. The IP input was analyzed by regular SDS-PAGE gel with anti-Flag antibody. (E) The phospho-sites of CAP1 identified from mass spectrometry analysis. (F) Phosphorylation levels of mutation of phosphosites (serine to alanine, S to A) by OST1, detected with anti-phosphoserine antibody. The loading amounts of His-CAP1 and GST-OST1 were detected by CBB staining. Values indicate mean ± SD ( n = 3 biological repeats). CAP1 (3 μM), ADF4 (3 μM), RCAR12 (1 μM), ABA (1 μM), F-actin (3 μM).
    Sirna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology plasmid 122 cap1 sirna
    (A) Interaction between OST1 and <t>CAP1</t> validated by BiFC assays. The images are the representative of three independent experiments ( n = 3). OST1 K50R indicates the kinase-dead form of OST1. NLS-mCherry indicates nuclear localization. We repeated the experiment four times with similar results and at least 8 leaves were observed per time. Scale bars = 50 μm. (B) Co-IP assay was performed to test the interaction of CAP1 with OST1 and OST1 K50R , detected with anti-Flag and anti-MYC antibodies. GFP-2Flag was set as a negative control. The images are the representative of two independent experiments ( n = 2) with the same results. (C) In vitro kinase assay showing the phosphorylation of CAP1 by OST1. The phosphorylation <t>of</t> <t>His-CAP1</t> was examined using an anti-thiophosphate ester (thioP). The loading amounts of His-CAP1 and GST-OST1 were detected using Coomassie Brilliant Blue (CBB) staining. (D) OST1 phosphorylates CAP1 in vitro . CAP1 from OE- CAP1 and ost1 :OE- CAP1 seedlings was immunoprecipitated and separated by a Pho-tag-PAGE gel, then analyzed with anti-Flag antibody. The IP input was analyzed by regular SDS-PAGE gel with anti-Flag antibody. (E) The phospho-sites of CAP1 identified from mass spectrometry analysis. (F) Phosphorylation levels of mutation of phosphosites (serine to alanine, S to A) by OST1, detected with anti-phosphoserine antibody. The loading amounts of His-CAP1 and GST-OST1 were detected by CBB staining. Values indicate mean ± SD ( n = 3 biological repeats). CAP1 (3 μM), ADF4 (3 μM), RCAR12 (1 μM), ABA (1 μM), F-actin (3 μM).
    Plasmid 122 Cap1 Sirna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc cap1
    (A) Interaction between OST1 and <t>CAP1</t> validated by BiFC assays. The images are the representative of three independent experiments ( n = 3). OST1 K50R indicates the kinase-dead form of OST1. NLS-mCherry indicates nuclear localization. We repeated the experiment four times with similar results and at least 8 leaves were observed per time. Scale bars = 50 μm. (B) Co-IP assay was performed to test the interaction of CAP1 with OST1 and OST1 K50R , detected with anti-Flag and anti-MYC antibodies. GFP-2Flag was set as a negative control. The images are the representative of two independent experiments ( n = 2) with the same results. (C) In vitro kinase assay showing the phosphorylation of CAP1 by OST1. The phosphorylation <t>of</t> <t>His-CAP1</t> was examined using an anti-thiophosphate ester (thioP). The loading amounts of His-CAP1 and GST-OST1 were detected using Coomassie Brilliant Blue (CBB) staining. (D) OST1 phosphorylates CAP1 in vitro . CAP1 from OE- CAP1 and ost1 :OE- CAP1 seedlings was immunoprecipitated and separated by a Pho-tag-PAGE gel, then analyzed with anti-Flag antibody. The IP input was analyzed by regular SDS-PAGE gel with anti-Flag antibody. (E) The phospho-sites of CAP1 identified from mass spectrometry analysis. (F) Phosphorylation levels of mutation of phosphosites (serine to alanine, S to A) by OST1, detected with anti-phosphoserine antibody. The loading amounts of His-CAP1 and GST-OST1 were detected by CBB staining. Values indicate mean ± SD ( n = 3 biological repeats). CAP1 (3 μM), ADF4 (3 μM), RCAR12 (1 μM), ABA (1 μM), F-actin (3 μM).
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    Image Search Results


    (A) Interaction between OST1 and CAP1 validated by BiFC assays. The images are the representative of three independent experiments ( n = 3). OST1 K50R indicates the kinase-dead form of OST1. NLS-mCherry indicates nuclear localization. We repeated the experiment four times with similar results and at least 8 leaves were observed per time. Scale bars = 50 μm. (B) Co-IP assay was performed to test the interaction of CAP1 with OST1 and OST1 K50R , detected with anti-Flag and anti-MYC antibodies. GFP-2Flag was set as a negative control. The images are the representative of two independent experiments ( n = 2) with the same results. (C) In vitro kinase assay showing the phosphorylation of CAP1 by OST1. The phosphorylation of His-CAP1 was examined using an anti-thiophosphate ester (thioP). The loading amounts of His-CAP1 and GST-OST1 were detected using Coomassie Brilliant Blue (CBB) staining. (D) OST1 phosphorylates CAP1 in vitro . CAP1 from OE- CAP1 and ost1 :OE- CAP1 seedlings was immunoprecipitated and separated by a Pho-tag-PAGE gel, then analyzed with anti-Flag antibody. The IP input was analyzed by regular SDS-PAGE gel with anti-Flag antibody. (E) The phospho-sites of CAP1 identified from mass spectrometry analysis. (F) Phosphorylation levels of mutation of phosphosites (serine to alanine, S to A) by OST1, detected with anti-phosphoserine antibody. The loading amounts of His-CAP1 and GST-OST1 were detected by CBB staining. Values indicate mean ± SD ( n = 3 biological repeats). CAP1 (3 μM), ADF4 (3 μM), RCAR12 (1 μM), ABA (1 μM), F-actin (3 μM).

    Journal: PLOS Genetics

    Article Title: The RCAR12-CAP1-OST1 module controls ABA-mediated stomatal closure in Arabidopsis

    doi: 10.1371/journal.pgen.1012092

    Figure Lengend Snippet: (A) Interaction between OST1 and CAP1 validated by BiFC assays. The images are the representative of three independent experiments ( n = 3). OST1 K50R indicates the kinase-dead form of OST1. NLS-mCherry indicates nuclear localization. We repeated the experiment four times with similar results and at least 8 leaves were observed per time. Scale bars = 50 μm. (B) Co-IP assay was performed to test the interaction of CAP1 with OST1 and OST1 K50R , detected with anti-Flag and anti-MYC antibodies. GFP-2Flag was set as a negative control. The images are the representative of two independent experiments ( n = 2) with the same results. (C) In vitro kinase assay showing the phosphorylation of CAP1 by OST1. The phosphorylation of His-CAP1 was examined using an anti-thiophosphate ester (thioP). The loading amounts of His-CAP1 and GST-OST1 were detected using Coomassie Brilliant Blue (CBB) staining. (D) OST1 phosphorylates CAP1 in vitro . CAP1 from OE- CAP1 and ost1 :OE- CAP1 seedlings was immunoprecipitated and separated by a Pho-tag-PAGE gel, then analyzed with anti-Flag antibody. The IP input was analyzed by regular SDS-PAGE gel with anti-Flag antibody. (E) The phospho-sites of CAP1 identified from mass spectrometry analysis. (F) Phosphorylation levels of mutation of phosphosites (serine to alanine, S to A) by OST1, detected with anti-phosphoserine antibody. The loading amounts of His-CAP1 and GST-OST1 were detected by CBB staining. Values indicate mean ± SD ( n = 3 biological repeats). CAP1 (3 μM), ADF4 (3 μM), RCAR12 (1 μM), ABA (1 μM), F-actin (3 μM).

    Article Snippet: GST-RCAR12 or GST (5 μg) were incubated with His-CAP1 (5 μg) and 25 μL glutathione S-Sepharose 4B (GS4B, GE Healthcare, PA, USA) resin in 500 μL binding buffer containing 25 mM Tris, pH 7.5, 150 mM NaCl, 1% Triton X-100 and ABA.

    Techniques: Co-Immunoprecipitation Assay, Negative Control, In Vitro, Kinase Assay, Phospho-proteomics, Staining, Immunoprecipitation, SDS Page, Mass Spectrometry, Mutagenesis

    (A(A) GST pull-down assay was performed for the interaction of ADF4 with CAP1. In vitro phosphorylation assay was performed, followed by GST pull-down. OST1 K50R indicates the kinase-dead form of OST1. λ-PPase, Lambda Protein Phosphatase. The loading amounts of His-CAP1, GST-ADF4 and GST were detected by CBB staining.(B) Relative protein levels of His-CAP1 in (A). The intensity of His-band was measured using ImageJ software. Three independent experiments were provided for the data statistics. Values are means ± SD ( n = 3). Different letters indicate statistically significant differences by one-way ANOVA with Tukey’s test ( P < 0.05). (C) Analysis of the interaction of CAP1 using Co-IP assay before and after 50 μΜ ABA treatment for 3 h. CAP1-6Flag was immunoprecipitated using anti-Flag-M2 agrose, and immunoblotting assays were performed using anti-Flag and anti-MYC antibodies. (D) Relative protein levels of ADF4 in (C). The intensity was measured using ImageJ software. Four independent experiments were provided for the data statistics. Values are means ± SD (n = 4). Asterisk indicates statistically significant differences (*P < 0.05, Student’s t- test, two-sided). (E) The interactions of the phosphomimic variant of CAP1 S246/249/250/253-256D and CAP1 with ADF4 were analyzed using in vitro GST pull-down assay. The loading was detected by CBB staining. (F) The interactions of the phosphomimic variant of CAP1 S246/249/250/253-256D and CAP1 with ADF4 were analyzed using LCI (Luciferase Complementation Imaging) assay. The indicated constructs were transiently expressed in N. benthamiana leaves. Leaves were photographed 3-day after infiltration. (G) Representative confocal images of F-actin. F-actin was incubated with indicated proteins for 30 min before staining with Alexa488-Phalloidin. Scale bar = 5 μm. (H) Quantification of the length of F-actin in (G) by ImageJ. More than 100 filaments were measured for each treatment. Values are mean ± SEM. * P < 0.05, as determined by one-way ANOVA with Tukey’s test. (I) Depolymerization of F-actin (10% pyrene labeled). F-actin disassembly was monitored by tracking the decrease in pyrene fluorescence per minute. a.u., arbitrary units. Values indicate mean ± SD ( n = 3 biological repeats). CAP1 (3 μM), ADF4 (3 μM), OST1 (1 μM), F-actin (3 μM).

    Journal: PLOS Genetics

    Article Title: The RCAR12-CAP1-OST1 module controls ABA-mediated stomatal closure in Arabidopsis

    doi: 10.1371/journal.pgen.1012092

    Figure Lengend Snippet: (A(A) GST pull-down assay was performed for the interaction of ADF4 with CAP1. In vitro phosphorylation assay was performed, followed by GST pull-down. OST1 K50R indicates the kinase-dead form of OST1. λ-PPase, Lambda Protein Phosphatase. The loading amounts of His-CAP1, GST-ADF4 and GST were detected by CBB staining.(B) Relative protein levels of His-CAP1 in (A). The intensity of His-band was measured using ImageJ software. Three independent experiments were provided for the data statistics. Values are means ± SD ( n = 3). Different letters indicate statistically significant differences by one-way ANOVA with Tukey’s test ( P < 0.05). (C) Analysis of the interaction of CAP1 using Co-IP assay before and after 50 μΜ ABA treatment for 3 h. CAP1-6Flag was immunoprecipitated using anti-Flag-M2 agrose, and immunoblotting assays were performed using anti-Flag and anti-MYC antibodies. (D) Relative protein levels of ADF4 in (C). The intensity was measured using ImageJ software. Four independent experiments were provided for the data statistics. Values are means ± SD (n = 4). Asterisk indicates statistically significant differences (*P < 0.05, Student’s t- test, two-sided). (E) The interactions of the phosphomimic variant of CAP1 S246/249/250/253-256D and CAP1 with ADF4 were analyzed using in vitro GST pull-down assay. The loading was detected by CBB staining. (F) The interactions of the phosphomimic variant of CAP1 S246/249/250/253-256D and CAP1 with ADF4 were analyzed using LCI (Luciferase Complementation Imaging) assay. The indicated constructs were transiently expressed in N. benthamiana leaves. Leaves were photographed 3-day after infiltration. (G) Representative confocal images of F-actin. F-actin was incubated with indicated proteins for 30 min before staining with Alexa488-Phalloidin. Scale bar = 5 μm. (H) Quantification of the length of F-actin in (G) by ImageJ. More than 100 filaments were measured for each treatment. Values are mean ± SEM. * P < 0.05, as determined by one-way ANOVA with Tukey’s test. (I) Depolymerization of F-actin (10% pyrene labeled). F-actin disassembly was monitored by tracking the decrease in pyrene fluorescence per minute. a.u., arbitrary units. Values indicate mean ± SD ( n = 3 biological repeats). CAP1 (3 μM), ADF4 (3 μM), OST1 (1 μM), F-actin (3 μM).

    Article Snippet: GST-RCAR12 or GST (5 μg) were incubated with His-CAP1 (5 μg) and 25 μL glutathione S-Sepharose 4B (GS4B, GE Healthcare, PA, USA) resin in 500 μL binding buffer containing 25 mM Tris, pH 7.5, 150 mM NaCl, 1% Triton X-100 and ABA.

    Techniques: Pull Down Assay, In Vitro, Phospho-proteomics, Staining, Software, Co-Immunoprecipitation Assay, Immunoprecipitation, Western Blot, Variant Assay, Luciferase, Imaging, Construct, Incubation, Labeling, Fluorescence