Anti-GEP100 antibody produced in rabbit

GEP100 is predominantly expressed in peripheral blood leukocytes, brain, and spleen. GEP100 contains an ARF-activating Sec7 domain, a pleckstrin homology (PH) domain and an Q-like motif.

Anti-GEP100 antibody produced in rabbit is suitable for immunoblotting using human hepatoma cell line HepG2 to study the effect of GEP100/Arf6 on EGF-induced cell migration. It is suitable for western blot analysis at a working concentration of 1-2μg/mL using whole extracts of human MDA-MB-231 and mouse 4T1 cells.

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

The protein interacts with a-catenin and regulates cell adhesion, actin cytoskeleton remodeling and cell migration. It also activates Arf6 during integrin internalization, which in turn regulates both endocytosis and recycling of β1 integrins.

GEP100 (also called BRAG2) is a guanine nucleotideexchangingfactor (GEF) for Arf6. GEP100 induces breast cancer invasion and metastasis by specifically activating Arf6 in response to EGF stimulation. GEP100 phosphorylates epidermal growth factor receptor (EGFR) by the direct binding of its PH domain to two phosphorylated tyrosines (Tyr 1068/1086) in EGFR, which in turn activates Arf6. Overexpression of GEP100 together with Arf6 causes non-invasive MCF7 cells to become highly invasive.

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.

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