Members of the Wiskott-Aldrich sydrome protein (WASP) family regulate the formation of actin-based cell structures in many cell types. These proteins contain C-terminal actin-binding domains that can stimulate actin polymerization. In addition, these proteins bind the ARP2/3 complex, which can nucleate actin polymerization at sites that lead to branched actin structures. WASP is expressed primarily in hematopoietic cells, while its homolog N-WASP is widely expressed. These proteins have 48% identity in human with the highest homology in the functional regions of these proteins. Serine and tyrosine phosphorylation regulates the activity of both proteins. WASP is observed as a 63 kDa protein in hematopoietic cells, while N-WASP is observed as a 65 kDa in many tissues, especially brain.
Higgs, H.N. & Pollard, T.D. (2001) Annu Rev Biochem 70:649-676.
Baba, Y. et al. (1999) Blood 93:2003.
*For more information, see UniProt Accession O00401
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Kalwa, H. & Michel, T. (2011) J Biol Chem 286:2320. (WB: bovine aortic endothelial cells)
Pichot, C. et al. (2010) Cancer Res. 70:8347. (WB: human MDA-MB-231 cells)
Anitei, M. et al. (2010) Nature Cell Biol. 12:330. (WB: human HeLa cells)
Pichot, C. et al. (2009) British J Cancer. 1 10. (WB: breast cancer cell lines)
Elias, BC et al. (2015) J Cell Sci. 128(23):4293. (WB: mouse kidney duct cells)
Hartig, S.M. et al. (2009) J Cell Sci. 122:2283. (WB: rat L6 myoblasts)
This kit contains: