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rabbit polyclonal abs against β3 integrin  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc rabbit polyclonal abs against β3 integrin
    Rabbit Polyclonal Abs Against β3 Integrin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 288 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal abs against β3 integrin/product/Cell Signaling Technology Inc
    Average 95 stars, based on 288 article reviews
    rabbit polyclonal abs against β3 integrin - by Bioz Stars, 2026-03
    95/100 stars

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    Santa Cruz Biotechnology rabbit polyclonal integrin β3
    FIGURE 2 | Overexpression of <t>integrin</t> <t>β3</t> affects PAK1phosphorylation levels. When integrin β3 is overexpressed in HT1080 cells, mechanical stimulation produces an increase in p-PAK1 levels, which suggests that integrin β3 signaling is required for the activation of PAK1. The empty vector represents cells that have been mock transfected using GFP plasmid. ∗P < 0.05 by the Student’s t-test; n = 3. Error bars represent the SEM.
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    Cell Signaling Technology Inc rabbit anti integrin β3 polyclonal antibody
    FIGURE 2 | Overexpression of <t>integrin</t> <t>β3</t> affects PAK1phosphorylation levels. When integrin β3 is overexpressed in HT1080 cells, mechanical stimulation produces an increase in p-PAK1 levels, which suggests that integrin β3 signaling is required for the activation of PAK1. The empty vector represents cells that have been mock transfected using GFP plasmid. ∗P < 0.05 by the Student’s t-test; n = 3. Error bars represent the SEM.
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    Cell Signaling Technology Inc rabbit polyclonal anti mouse β3 integrin
    FIGURE 2 | Overexpression of <t>integrin</t> <t>β3</t> affects PAK1phosphorylation levels. When integrin β3 is overexpressed in HT1080 cells, mechanical stimulation produces an increase in p-PAK1 levels, which suggests that integrin β3 signaling is required for the activation of PAK1. The empty vector represents cells that have been mock transfected using GFP plasmid. ∗P < 0.05 by the Student’s t-test; n = 3. Error bars represent the SEM.
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    FIGURE 2 | Overexpression of integrin β3 affects PAK1phosphorylation levels. When integrin β3 is overexpressed in HT1080 cells, mechanical stimulation produces an increase in p-PAK1 levels, which suggests that integrin β3 signaling is required for the activation of PAK1. The empty vector represents cells that have been mock transfected using GFP plasmid. ∗P < 0.05 by the Student’s t-test; n = 3. Error bars represent the SEM.

    Journal: Frontiers in cell and developmental biology

    Article Title: The Role of PAK1 in the Maturation of Invadopodia During Transient Mechanical Stimulation.

    doi: 10.3389/fcell.2019.00269

    Figure Lengend Snippet: FIGURE 2 | Overexpression of integrin β3 affects PAK1phosphorylation levels. When integrin β3 is overexpressed in HT1080 cells, mechanical stimulation produces an increase in p-PAK1 levels, which suggests that integrin β3 signaling is required for the activation of PAK1. The empty vector represents cells that have been mock transfected using GFP plasmid. ∗P < 0.05 by the Student’s t-test; n = 3. Error bars represent the SEM.

    Article Snippet: The following antibodies were used: rabbit polyclonal total PAK1 (1:1000; Bethyl Laboratories), rabbit monoclonal Ser-144 p-PAK1 (1:1000; Cell Signaling Technologies), rabbit polyclonal integrin β3 (1:300; Santa Cruz), mouse monoclonal GAPDH (1:7000; Millipore), HRP tagged anti-mouse (1:8000; Thermo Fisher Scientific) and HRP tagged anti-rabbit (1:10000; Amersham).

    Techniques: Over Expression, Activation Assay, Plasmid Preparation, Transfection

    FIGURE 8 | Working model of the pathway to maturation of invadopodia when cancer cells are stimulated by transient tugging forces. The above signaling pathway is proposed to lead to the enhanced invasion observed in fibrosarcoma cells when transient tugging forces are applied through a three-dimensional mechano-invasion assay. Invadopodia elongate and secrete more MMP-2 when the protein expression of integrin beta-3 is downregulated in response to tugging forces. Cofilin is most active when it is not phosphorylated and serves as a kinase substrate of LIMK1, which is activated by PAK1 and subsequently Rac1. Rac1 and LIMK1 have not yet been confirmed to participate in this mechanosensitive pathway.

    Journal: Frontiers in cell and developmental biology

    Article Title: The Role of PAK1 in the Maturation of Invadopodia During Transient Mechanical Stimulation.

    doi: 10.3389/fcell.2019.00269

    Figure Lengend Snippet: FIGURE 8 | Working model of the pathway to maturation of invadopodia when cancer cells are stimulated by transient tugging forces. The above signaling pathway is proposed to lead to the enhanced invasion observed in fibrosarcoma cells when transient tugging forces are applied through a three-dimensional mechano-invasion assay. Invadopodia elongate and secrete more MMP-2 when the protein expression of integrin beta-3 is downregulated in response to tugging forces. Cofilin is most active when it is not phosphorylated and serves as a kinase substrate of LIMK1, which is activated by PAK1 and subsequently Rac1. Rac1 and LIMK1 have not yet been confirmed to participate in this mechanosensitive pathway.

    Article Snippet: The following antibodies were used: rabbit polyclonal total PAK1 (1:1000; Bethyl Laboratories), rabbit monoclonal Ser-144 p-PAK1 (1:1000; Cell Signaling Technologies), rabbit polyclonal integrin β3 (1:300; Santa Cruz), mouse monoclonal GAPDH (1:7000; Millipore), HRP tagged anti-mouse (1:8000; Thermo Fisher Scientific) and HRP tagged anti-rabbit (1:10000; Amersham).

    Techniques: Invasion Assay, Expressing