Recombinant Rat Tie-2 Fc Chimera Protein, CF

• Reactivity: Rt
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Rat Tie-2 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. Immobilized rrTie-2/Fc Chimera at 4 µg/mL (100 µL/well) can bind rhAngiopoietin-2 with a linear range of 0.8-50 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived rat Tie-2 protein
  

  Rat Tie-2 (Ala23-Leu743) Accession # NP_001099207	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: NP_001099207
• N-terminal Sequence: Ala23
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 107.3 kDa (monomer).
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 120-140 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Rat Tie-2 Fc Chimera Protein, CF

• angiopoietin-1 receptor
• CD202b antigen
• CD202b
• EC 2.7.10
• EC 2.7.10.1
• hTIE2
• p140 TEK
• soluble TIE2 variant 1
• soluble TIE2 variant 2
• TEK tyrosine kinase, endothelial
• TEK
• Tie2
• Tie-2
• TIE2CD202b
• Tunica interna endothelial cell kinase
• Tyrosine-protein kinase receptor TEK
• Tyrosine-protein kinase receptor TIE-2
• venous malformations, multiple cutaneous and mucosal
• VMCM
• VMCM1

Background

Tie-2, also known as Tek, is a 145 kDa, type I transmembrane glycoprotein receptor tyrosine kinase that is a receptor for angiopoietins (1). The 1120 amino acid (aa) rat Tie-2 precursor contains an 18 aa signal sequence, a 723 aa extracellular domain (ECD), a 25 aa transmembrane segment, and a 354 aa cytoplasmic tail (2). The ECD contains two C2 Ig-like domains, three EGF-like motifs, and three fibronectin type III repeats. The cytoplasmic region has a split tyrosine kinase domain and presumably autophosphorylates as a ligand-induced homodimer (3). Rat Tie-2 ECD shares 96%, 90% and 89% aa identity with mouse, human and bovine Tie-2, respectively, and 47% aa identity with rat Tie-1 ECD. Cells known to express Tie-2 include embryonic and adult endothelial cells, hematopoietic stem cells and a circulating population of proangiogenic Tie-2 expressing monocytes (TEM) (4 - 7). A soluble form of Tie-2, most likely the result of proteolytic cleavage, is found in serum (8). The four angiopoietins are ligands of Tie-2. Ang-1 and Ang-4 are Tie-2 activators, while Ang-2 and Ang-3 can be activators or inhibitors, depending on context (1, 9). Tie-2 is said to be important for maintaining vascular integrity. It mediates endothelial cell-smooth muscle cell communication, and inhibits endothelial cell apoptosis, thus maintaining endothelial cell survival (10 - 12). It is also absolutely required for embryonic development of the endocardium (3, 10, 13). While not essential for embryonic hematopoiesis, Ang-1 production by osteoblasts promotes quiescence ofTie-2-expressing bone marrow stem cells. This quiescence is critical for maintaining an ongoing hematopoietic capability (12, 14, 15).

1. Eklund, L and B. R. Olsen (2006) Exp. Cell Res. 312:630.
2. Maisonpierre, P.C. et al. (1993) Oncogene 8:1631.
3. Vikkula, M. et al. (1996) Cell 87:1181.
4. Asahara, T. et al. (1997) Science 275:964.
5. Dallabrida, S.M. et al. (2003) Biochem. Biophys. Res. Commun. 311:563.
6. Takakura, N. et al. (1998) Immunity 9:677.
7. DePalma, M. et al. (2005) Cancer Cell 8:211-226.
8. Reusch, P. et al. (2001) Angiogenesis 4:123.
9. Lee, H.J. et al. (2004) FASEB J. 18:1200.
10. Jones, N. et al. (2001) EMBO Rep. 2:438.
11. Wong, A. L. et al. (1997) Circ. Res. 81:567.
12. Hamaguchi, I. et al. (2006) Blood 107:1207.
13. Puri, M.C. et al. (1999) Development 126:4569.
14. Puri, M.C. and A. Bernstein (2003) Proc. Natl. Acad. Sci. USA 100:12753.
15. Arai, F. et al. (2004) Cell 118:149.

Bioinformatics

• Uniprot:
  • NP_001099207()