|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||101289 Da|
|Other Names||Guanine nucleotide exchange factor VAV2, VAV-2, VAV2|
|Target/Specificity||A synthetic peptide corresponding to residues on human Vav2 was used as an immunogen. This antibody detects Vav2 phosphorylated on Tyr172 as well as unphosphorylated Vav2.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Vav2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly (By similarity).|
|Tissue Location||Widely expressed.|
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Provided below are standard protocols that you may find useful for product applications.
The Vav family are Rho/Rac guanosine nucleotide exchange factors (GEFs), consisting of three members in mammalian cells (Vav, Vav2, Vav3) and one in nematodes (CelVav) (1). Vav and Vav2 are members of the dbl family of guanine nucleotide exchange factors (GEF) for the rho/rac family of GTP binding proteins. Vav is expressed primarily in hematopoietic cells, while vav2 has a wider tissue distribution (2). Vav2 serves as a guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Unlike Vav1, whose expression is restricted to cells of hematopoietic origin, Vav2 is broadly expressed. Recently, Vav2 has been identified as a substrate for the epidermal growth factor (EGF) receptor. EGF receptor phosphorylates Vav2 on all three possible phosphorylation sites, Tyr-142, Tyr-159, and Tyr-172. results suggest that EGF regulates Vav2 activity basically through phosphatidylinositol 3-kinase activation, whereas tyrosine phosphorylation of Vav2 may rather be necessary for mediating protein-protein interactions (3)
1. Bustelo XR, et al. Rev Oncog 7:65-88, 1996.
2. Denkinger DJ, et al. Biochem Biophys 149(1-3):253-62,
3. Tamas P, et al. J Biol Chem 278(7):5163-71, 2002.
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