Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

Tie2 (AB33) Mouse mAb #4224

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H B Endogenous 160 Mouse IgG1

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

Protocols

Specificity / Sensitivity

Tie2 (AB33) Mouse mAb detects endogenous levels of Tie2 in various endothelial cell lines. It does not cross-react with related proteins.

Source / Purification

Monoclonal antibody is produced by immunizing animals with recombinant Tie2 protein fragments corresponding to the extracellular domain of human Tie2.

Western Blotting

Western Blotting

Western blot analysis of extracts from human umbilical vein endothelial cells (HUVEC) and bovine aortic endothelial cells (BAEC), using Tie2 (AB33) Mouse mAb.

Background

Tie2/Tek is a receptor tyrosine kinase (RTK) expressed almost exclusively on endothelial cells. It is critical for vasculogenesis and could be important for maintaining endothelial cell survival and integrity in adult blood vessels as well as tumor angiogenesis (1-3). A family of ligands known as the angiopoietins binds to Tie2. Interestingly, these ligands appear to have opposing actions; Angiopoietin-1 (Ang1) and Angiopoietin-4 (Ang4) stimulate tyrosine phosphorylation of Tie2; Angiopoietin-2 (Ang2) and Angiopoietin-3 (Ang3) can inhibit this phosphorylation (4,5). Downstream signaling components, including Grb2, Grb7, Grb14, SHP-2, the p85 subunit of phosphatidylinositol 3-kinase, and p56/Dok-2 interact with Tie2 in a phosphotyrosine-dependent manner through their SH2 or PTB domains (6,7). Tyr992 is located on the putative activation loop of Tie2 and is a major autophosphorylation site (8).

  1. Ward, N.L. and Dumont, D.J. (2002) Semin. Cell Dev. Biol. 13, 19-27.
  2. Jones, N. and Dumont, D.J. (2000) Cancer Metastasis Rev. 19, 13-17.
  3. Partanen, J. and Dumont, D.J. (1999) Curr. Top. Microbiol. Immunol. 237, 159-172.
  4. Ellis, L. M. et al. (2002) Oncology 16, 31-35.
  5. Koh, G. Y. et al. (2002) Exp. Mol. Med. 34, 1-11.
  6. Jones, N. et al. (1999) J. Biol. Chem. 274, 30896-30905.
  7. Jones, N. et al. (2003) Mol. Cell. Biol. 23, 2658-2668.
  8. Murray, B. W. et al. (2001) Biochem. 40, 10243-10253.

Application References

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

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