The WASP family members include WASP, N-WASP and WAVE (WASP-family verprolin homologous protein) proteins. WAVE proteins (also termed SCAR, WASF proteins), include three isoforms WAVE-1, WAVE-2 and WAVE-3. Expression of WAVE-1 and WAVE-3 isoforms is restricted to the brain, while WAVE-2 is ubiquitously expressed. WAVE-1-3 have structures like WASP and N-WASP; these include two conserved domains: a WAVE homology domain (WHD), also known as SCAR homology domain (SHD), a C-terminal acidic domain that binds to the Arp2/3 complex; and a central core domain composed of proline-rich sequences that interact with cofilin and various SH3 proteins.
Immunogen
synthetic peptide corresponding to amino acids 540-559 located at the C-terminus of human WAVE-1. The sequence is identical in several species, including mouse and rat WAVE-1 and is conserved (75% sequence identity) in other WAVE isoforms.
Application
Anti-WAVE antibody produced in rabbit has been used in immunoblotting.
Biochem/physiol Actions
WAVE proteins also play key roles in the induction of various actin remodelling processes including membrane ruffling and lamellipodia formation. WAVE proteins bind to phosphatidylinositol-3,4,5 triphosphate (PI-3,4,5P3) formed by PI3-kinase, thus facilitating WAVE translocation to the plasma membrane. WAVE proteins are thought to mediate Rac activity indirectly via the target protein IRSp53 or by binding to a macromolecular complex that includes PIR121, Nck-associated protein 1 (Nap1), Abi, and HSPC300 proteins.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
Miki H, et al.
Nature, 408(6813), 732-732 (2000)
Purification and architecture of the ubiquitous Wave complex
Gautreau A, et al.
Proceedings of the National Academy of Sciences of the USA, 101(13), 4379-4383 (2004)
Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
Eden S, et al.
Nature, 418(6899), 790-790 (2002)
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