EEA1, or Early Endosome Antigen 1, is a phospholipid-binding protein essential for endosomal membrane trafficking and fusion, and is a useful endosomal marker. We at Novus Biologicals have an extensive EEA1 antibody catalog, with antibodies that have been cited in many publications.
In 2005, R. Bhattacharya, et al. used antibodies from our EEA1 catalog to investigate the role of dynamin-2 in regulating VEGFR2-mediated endothelial signalling. VEGFR-2, or Vascular Endothelial Growth Factor Receptor-2 (also called KDR) is a receptor tyrosine kinase enzyme which regulates a number of signalling pathways in vascular endothelial cells, in response to its ligand Vascular Permeability Factor (VPF)/VEGF. Regulation includes chemotactic, mitogenic, permeability and survival signals. However, the endothelial distribution of VEGFR-2 is uncertain, as is its mechanism of action.
It was shown that VEGFR-2 is localized on the plasma membrane, the endosomes and the perinuclear region of endothelial cells (ECs). EEA1 antibody assays showed that VEGFR-2 co-localizes with EEA1. It was also seen to bind with caveolin-1 and dynamin-2 - a signal transducing GTP enzyme which plays a role in receptor endocytosis. Furthermore, a coimmunoprecipitation assay to test the interaction of VEGFR-2 and dynamin-2 showed that dynamin-2 must be present for EC signalling and survival to occur. Overexpression of a mutated form of dynamin lacking a GTP domain led to selective inhibition of VEGFR-2 and formation of endosomal vesicles, which led to cell cycle arrest via p21 induction.
The conclusion was that dynamin-2 is an important regulator of VEGFR-2 function and expression, and is an important factor in VPF/VEGF induced angiogenesis. Our EEA1 antibody database has since proven important in studies into early endosomal transport regulation by EHD4.
Novus Biologicals offers many EEA1 reagents for your research needs including:
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