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mouse anti human vegfr2  (Proteintech)


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    Proteintech mouse anti human vegfr2
    Mouse Anti Human Vegfr2, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 222 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse anti human vegfr2/product/Proteintech
    Average 96 stars, based on 222 article reviews
    mouse anti human vegfr2 - by Bioz Stars, 2026-02
    96/100 stars

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    Image Search Results


    Vascular abnormality induced by insufficient Cav-1 is likely mediated by aberrant VEGFR2 and VE-Cadherin. Cav-1, VEGFR2 and VE-Cadherin protein content were assessed in total cell lysates ( A , D – F ), the soluble fraction B , G and H and the particular fraction C , I and J of Cav-1 depleted HUVECs and controls. Representative images ( A – C ), as well as quantifications obtained by pixel density assessments, are shown ( D – J ). Proteins from γ-tubulin, HSP90, and Na/K-ATPase served as loading control for total cell lysate, the soluble, and the membrane fraction, respectively. n = 4. Cav-1, VEGFR2 and VE-Cadherin were assessed in total cell lysates and in biotinylated cell surface proteins of Cav-1 depleted and control ECs ( K – P ). Representative images K and quantifications obtained by pixel density assessments are shown ( L – P ). n = 4. Con: control, Cav1 siRNA: Cav-1 depleted, T: total, S: soluble, M: membranous particular. *p < 0.05, **p < 0.01, ***p < 0.001

    Journal: Molecular Medicine

    Article Title: Sufficient Cav-1 levels in the endothelium are critical for the maintenance of the neurovascular unit in the retina

    doi: 10.1186/s10020-023-00749-9

    Figure Lengend Snippet: Vascular abnormality induced by insufficient Cav-1 is likely mediated by aberrant VEGFR2 and VE-Cadherin. Cav-1, VEGFR2 and VE-Cadherin protein content were assessed in total cell lysates ( A , D – F ), the soluble fraction B , G and H and the particular fraction C , I and J of Cav-1 depleted HUVECs and controls. Representative images ( A – C ), as well as quantifications obtained by pixel density assessments, are shown ( D – J ). Proteins from γ-tubulin, HSP90, and Na/K-ATPase served as loading control for total cell lysate, the soluble, and the membrane fraction, respectively. n = 4. Cav-1, VEGFR2 and VE-Cadherin were assessed in total cell lysates and in biotinylated cell surface proteins of Cav-1 depleted and control ECs ( K – P ). Representative images K and quantifications obtained by pixel density assessments are shown ( L – P ). n = 4. Con: control, Cav1 siRNA: Cav-1 depleted, T: total, S: soluble, M: membranous particular. *p < 0.05, **p < 0.01, ***p < 0.001

    Article Snippet: Primary antibodies used: lectin conjugated with fluorescein isothiocyanate (FITC) (L9381, Sigma-Aldrich, Taufkirchen, Germany); lectin conjugated with fluorescein isothiocyanate (TRITC) (L5264, Sigma-Aldrich, Taufkirchen, Germany); anti-Ionized calcium-binding adapter molecule1 (IBa1) (019-19741, Wako, Osaka, Japan); Anti-NG2 Chondroitin Sulfate Proteoglycan Antibody (AB5320, Sigma-Aldrich, Taufkirchen, Germany); monoclonal anti-actin, α-smooth muscle -Cy3™ antibody (α-SMA-Cy3) (C6198, Sigma-Aldrich, Taufkirchen, Germany); Rabbit-anti-VEGFR2 (55B11, Cell Signaling, Frankfurt, Germany), rabbit-anti-VE-Cadherin (D87F2, Cell signaling, Frankfurt, Germany), mouse-anti-caveolin-1 (sc-894, Santa Cruz Biotechnology, Heidelberg, Germany), rabbit-anti-albumin (55442, MP Bio, Eschwege, Germany), goat-anti-CD74 (sc-5438, Santa Cruz Biotechnology, Heidelberg, Germany), rabbit-anti-GFAP (Z0334, DAKO, Jena, Germany), mouse-anti-tubulin (T6557, Sigma-Aldrich, Taufkirchen, Germany), rabbit-anti-HSP90 (4874, Cell Signaling, Frankfurt, Germany), mouse-anti-Na/K-ATPase (MA3-915, ABR, Limerick, USA); goat-anti-human VEGFR2 (AF357, R&D, Nordenstadt, Germany); rabbit-anti-human VE-Cadherin (D87F2) XP® (2500, Cell Signaling, Frankfurt, Germany); mouse-anti-p120-catenin (sc-23872, Santa Cruz Biotechnology, Heidelberg, Germany).

    Techniques: Membrane