p-Vav1 (Y174) polyclonal antibody detects endogenous levels of Vav1 protein when phosphorylated at Tyr174.
The Vav gene was originally identified on the basis of its oncogenic activation during the course of gene transfer assays. The major translational product of the Vav proto-oncogene has been identified as a protein containing an array of structural motifs. Contained within its amino terminus are a helix-loop-helix domain and a leucine zipper motif similar to that of Myc family proteins; deletion of this region of p95Vav causes its oncogenic activation. In addition, p95Vav contains an SH2 domain, which could indicate its role as a substrate for tyrosine kinases. Expression of p95Vav is limited exclusively to cells of hematopoietic origin, including those of the erythroid, lymphoid and myeloid lineages.
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