WAVE1 (N-terminal region) Antibody

The Wiskott–Aldrich syndrome protein (WASP) family is involved in various pathways that regulate actin cytoskeletal organization. This family includes WASP, N-WASP, and three WAVE/SCAR isoforms, WAVE1, 2, and 3. WAVE proteins play key roles in actin-mediated cell events, such as membrane ruffling and lamellipodia formation. WAVEs contain an N-terminal WAVE homology domain, a basic domain, a Proline-rich region, and carboxy terminal verprolin, cofilin, and acidic (VCA) region. WAVEs are thought to act downstream of the Rac GTPase, connecting Rac activation to induction of Arp 2/3-mediated actin polymerization. Regulation of WAVE activity can occur through tyrosine phosphorylation. Src phosphorylation of WAVE1 at Tyr-125 enhances binding to the Arp2/3 complex, and is required for WAVE inhibition of Arp2/3-mediated stress fiber formation. By contrast, WAVE2 phosphorylation of Tyr-150 by Abl may enhance Arp2/3 complex actin nucleation and microspike formation in fibroblasts. Thus, site-specific tyrosine phosphorylation may be important for controlling specific activities of WAVE proteins.

The antibody detects an 80 kDa* protein corresponding to the molecular mass of WAVE1 on SDS-PAGE immunoblots of human SYF cSrc-transformed, HUVEC, and K562 cells, as well as rat PC12 cells and mouse C2C12 cells. This sequence has high homology with similar regions in rat and mouse WAVE1, and has less than 50% homology to similar regions in human WAVE2 and WAVE3.