Recombinant Rat Tie-2 His-tag Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Rat Tie-2 His-tag (Catalog # 10458-T2)
is immobilized at 0.5 µg/mL (100 µL/well), Recombinant Human Angiopoietin-2 His‑tag (Catalog #
623-AN) binds with an ED 50 of 0.4-3.6 ng/mL. |
Source |
Mouse myeloma cell line, NS0-derived rat Tie-2 protein Ala23-Leu743, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Ala23 & Met24 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
82 kDa. 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 |
95-108 kDa, under 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 |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in 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 His-tag Protein, CF
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 of Tie-2-expressing bone marrow stem cells.
This quiescence is critical for maintaining an ongoing hematopoietic capability
(12, 14, 15).
- Eklund, L. and B. R. Olsen (2006) Exp. Cell Res. 312:630.
- Maisonpierre, P.C. et al. (1993) Oncogene 8:1631.
- Vikkula, M. et al. (1996) Cell 87:1181.
- Asahara, T. et al. (1997) Science 275:964.
- Dallabrida, S.M. et al. (2003) Biochem. Biophys. Res. Commun. 311:563.
- Takakura, N. et al. (1998) Immunity 9:677.
- DePalma, M. et al. (2005) Cancer Cell 8:211.
- Reusch, P. et al. (2001) Angiogenesis 4:123.
- Lee, H.J. et al. (2004) FASEB J. 18:1200.
- Jones, N. et al. (2001) EMBO Rep. 2:438.
- Wong, A. L. et al. (1997) Circ. Res. 81:567.
- Hamaguchi, I. et al. (2006) Blood 107:1207.
- Puri, M.C. et al. (1999) Development 126:4569.
- Puri, M.C. and A. Bernstein (2003) Proc. Natl. Acad. Sci. USA 100:12753.
- Arai, F. et al. (2004) Cell 118:149.
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