| Overview |
| bs-70454r |
| Dok1 (Ser-450), Phosphospecific Antibody |
| WB |
| This antibody was cross-adsorbed to an unphosphorylated Dok1 (Ser-450) peptide before affinity purification using phospho-Dok1 (Ser-450) peptide. The purified antibody detects a band at 62 kDa* corresponding to Dok1 in western blots of human Jurkat cells, but does not detect this band after lambda phosphatase treatment. |
| Human, Mouse, Rat |
| Specifications |
| Unconjugated |
| Rabbit |
| Phospho-Dok1 (Ser-450) synthetic peptide (coupled to KLH) corresponds to amino acids surrounding serine 450 in human Dok1. |
| Ser-450 |
| Polyclonal |
| #REF! |
| IgG |
| Antigen Affinity purification |
| PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
| Storage at -20C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20C. |
| Target |
| Q99704 |
| p62DOK |
| Doks are a family of adaptor proteins that include six Dok proteins (Dok1 to Dok6), which have 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. I_B Kinase _ phosphorylates several serine sites including Ser-450 in vitro, and TNF_, 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. |
| Application Dilution |
| WB |
1:300-5000 |
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