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rabbit polyclonal anti integrin β3  (Millipore)


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    Millipore rabbit polyclonal anti integrin β3
    Rabbit Polyclonal Anti Integrin β3, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+integrin+%CE%B23/rabbit+anti+integrin+%CE%B1+3/pmc04982633-64-34-39
    Average 90 stars, based on 1 article reviews
    rabbit polyclonal anti integrin β3 - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    other:

    Article Title: Regional Regulation of Purkinje Cell Dendritic Spines by Integrins and Eph/Ephrins
    Article Snippet: Antibodies used in Purkinje cell experiment are: mouse monoclonal anti Calbindin (Swant 1/2000), guinea pig polyclonal anti calbindin (Synaptic System), chicken polyclonal anti calbindin (Swant 1/2000), rabbit polyclonal anti integrin β1 (Chemicon AB1952 1/500), rabbit polyclonal anti integrin β3 (Chemicon 1/500), rabbit polyclonal anti integrin β4 (Chemicon 1/500), rabbit polyclonal anti integrin α3 extracellular domain Ralph3.2 (Santa Cruz), rabbit polyclonal anti integrin α3 cytoplasmic domain (Chemicon AB1920 1/500), rabbit polyclonal anti integrin α5 extracellular domain (Chemicon AB1921 1/500), rabbit polyclonal anti integrin α5 cytoplasmic domain (Chemicon AB1928 1/500), rabbit polyclonal anti integrin αV (Chemicon), mouse monoclonal anti PSD95 (Affinity Bioreagents MA1-046, 1/500), rabbit polyclonal anti VGluT1 (Synaptic System), guinea pig polyclonal anti VGluT2 (Synaptic System), rabbit polyclonal anti pFAK (Santa Sruz), MAP2, Alexa fluor-conjugated secondary antibodies series were all purchased from Invitrogen and used at a dilution of 1/1000.



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    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 <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 <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 <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