Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

p56Dok-2 Antibody #3914

Applications Reactivity Sensitivity MW (kDa) Source
W H (M) Transfected Only 56 to 58 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

p56Dok-2 Antibody detects transfected levels of total p56Dok-2 proteins. The antibody does not cross-react with other p62Dok family members.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the residues at the carboxy-terminal sequence of human p56Dok-2. The antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from Jurkat, 32D and BaF3 cells, transfected with p56Dok-2 and/or anti-CD2-treated as indicated, using p56Dok-2 Antibody.

Background

Docking proteins are substrates of tyrosine kinases that function in the recruitment and assembly of specific signal transduction molecules. There are five members in the p62dok family, p62Dok (Dok-1), p56Dok-2 (Dok-2, or DoK-R), Dok-3, Dok-4 and Dok-5 (1-3), characterized by the presence of an amino-terminal PH domain, a central PTB domain and numerous potential sites of tyrosine phosphorylation. Tyrosine phosphorylation of p56Dok-2 occurs upon stimulation of cells with a variety of stimuli, or in cells transformed by oncogenic tyrosine kinases such as v-Src and Bcr-Abl (3-5). Based on the presence of several signaling domains (PH, PTB domain, tyrosine residue and proline-rich regions), it has been proposed that the p62dok family act as docking proteins that link RTKs to signal transduction pathways. p56Dok-2 has been proposed to be a negative regulator of cytokine-induced proliferation in T cells (5). Phosphorylated Tyr351 of p56Dok-2 mediates an association with the SH2 domain of Nck (4).

  1. Master, Z. et al. (2001) EMBO J. 20, 5919-5928.
  2. Grimm, J. et al. (2001) J. Cell. Biol. 154, 345-354.
  3. Cristofano, A. D. et al. (1998) J. Biol. Chem. 273, 4827-4830.
  4. Jones, N. and Dumont, D.J. (1999) Curr. Biol. 9, 1057-1060.
  5. Nemorin, J.G. and Duplay, P. (2000) J. Biol. Chem. 275, 14590-14597.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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