Thermo Fisher Scientific Phospho-DOK1/DOK2 (Tyr362, Tyr337) Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

1:1,000

-

Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

Phospho-Dok1 (Tyr-362) synthetic peptide (coupled to KLH) corresponds to amino acids surrounding tyrosine 362 in human Dok1. This sequence is conserved in Dok1 from rat and mouse (Tyr-361), and has high homology to Dok2 (Tyr-337). The site is not conserved in other Dok family members.

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

0.5 mg/mL

Purification

Antigen affinity chromatography

Storage buffer

PBS with 1mg/mL BSA, 50% glycerol

Contains

0.05% sodium azide

Storage conditions

-20° C, Avoid Freeze/Thaw Cycles

Shipping conditions

Wet ice

RRID

AB_2942909

Product Specific Information

This antibody was cross-adsorbed to a phosphotyrosine peptide before affinity purification using phospho-Dok1 (Tyr-362) 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 alkaline phosphatase treatment. Similar to Dok1 (Ser-450) antibody, this antibody also detects an 80 kDa band that has not been identified.

Target Information

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. IkappaB Kinase beta phosphorylates several serine sites including Ser-450 in vitro, and TNFalpha, 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.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.