Catalog # DX2275
unphosphorylated Dok1 (Ser-450) Peptide
Size 50 μg
Doks are a family of adaptor proteins that recruit SH2-containing molecules involved in various cell signaling pathways. Six Dok proteins (Dok1 to Dok6) have been identified and each has an N-terminal pleckstrin homology domain, a central phosphotyrosine binding domain, and a C-terminal region containing multiple tyrosine residues. When phosphorylated, these tyrosines can serve as docking sites for SH2 domain-containing proteins. Dok1 (p62dok) has been shown to bind Ras-GAP, Nck, and Csk. Several tyrosine phosphorylation sites have been identified for Dok1. One site, Tyr-362 (Tyr-361 mouse), is phosphorylated by c-Abl, is required for Nck binding, and may be critical for filopodia formation during fibroblast spreading on fibronectin. Alternatively, Dok1 activity is also regulated by serine phosphorylation. IκB Kinase β phosphorylates several serine sites including Ser-450 in vitro, and TNFα, IL-1, and radiation treatment lead to phosphorylation of Ser-443, Ser-446, and Ser-450 in vivo. Phosphorylation of these serine sites may be required for Dok-mediated inhibition of MAPK signaling and stimulation of cell motility.
Lee, S. et al. (2004) Proc. Nat. Acad. Sci. 101(50):17416.
Woodring, P.J. (2004) J Cell Biol. 165(4):493.
Kashige, N. et al. (2000) Proc. Nat. Acad. Sci. 97(5):2093.
Noguchi, T. et al. (1999) EMBOJ 18(7):1748.
*For more information, see UniProt Accession Q99704
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: