Recombinant Human Angiopoietin-1, Biotinylated Protein
Recombinant Human Angiopoietin-1, Biotinylated Protein Summary
Product Specifications
Ser20-Phe498, with a C-terminal 6-his tag
Accession # Q5HYA0
Analysis
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
BT923
| Formulation | Lyophilized from a 0.2 μm filtered solution in Tris-Citrate and NaCl with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 10 μg/mL in PBS containing at least 0.1% human or bovine serum albumin. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
BT923/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in Tris-Citrate and NaCl. |
| Reconstitution | Reconstitute at 100 μg/mL in PBS. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: Angiopoietin-1
Angiopoietin-1 (Ang-1) is a secreted glycoprotein that plays a critical role in the development and maintenance of the vascular system (1, 2). It contains a N-terminal coiled-coil region and a C-terminal fibrinogen-like domain separated by a short flexible region (3, 4). Mature human Angiopoietin-1 shares 97% amino acid sequence identity with mouse and rat Angiopoietin-1. It is expressed by vascular smooth muscle cells and pericytes as an approximately 70 kDa molecule that associates into
disulfide-linked homotrimers, tetramers, and pentamers (3, 5). Angiopoietin-1 binds and activates the receptor tyrosine kinase Tie-2, and its association into tetramers is important for full Tie-2 activation (3, 4). Angiopoietin-1 ligation of Tie-2 on vascular endothelial cells (EC) induces the development and branching of blood vessels (6, 7). In sub-confluent EC (i.e. during angiogenesis), Angiopoietin-1 promotes EC motility and Tie-2 localization at the trailing edge of the cell (8). In confluent EC (i.e. in homeostasis), multimeric Angiopoietin-1 enhances vascular integrity by promoting the in trans homotypic association of Tie-2 between EC or with the substratum (8, 9). In addition, Angiopoietin-1 suppresses several VEGF-induced effects on the vasculature including endothelial permeability, stretch-induced release of Angiopoietin-2, and up-regulation of the leukocyte adhesion molecules VCAM-1, ICAM-1, and E-Selectin (10-12). Angiopoietin-1 also interacts with a variety of integrins and the extracellular matrix independently of Tie-2 (13, 14). These interactions support the adhesion, migration and stress resistance of EC, fibroblasts, and myocytes (13, 14). Angiopoietin-1 can protect against pulmonary arterial hypertension (5), reduce the extent of fibrosis and remodeling in infarcted diabetic myocardium (15), and enhance tumor progression and metastasis (16).
- Koh, G.Y. (2012) Trends Mol. Med. 19:31.
- Suri, C. et al. (1996) Cell 87:1171.
- Davis, S. et al. (1996) Cell 87:1161.
- Kim, K.-T. et al. (2005) J. Biol. Chem. 280:20126.
- Kugathasan, L. et al. (2009) J. Exp. Med. 206:2221.
- Suri, C. et al. (1998) Science 282:468.
- Jeansson, M. et al. (2011) J. Clin. Invest. 121:2278.
- Saharinen, P. et al. (2008) Nat. Cell. Biol. 10:527.
- Fukuhara, S. et al. (2008) Nat. Cell Biol. 10:513.
- Jho, D. et al. (2005) Circ. Res. 96:1282.
- Korff, T. et al. (2012) Cardiovasc. Res. 94:510.
- Kim, I. et al. (2001) Circ. Res. 89:477.
- Carlson, T.R. et al. (2001) J. Biol. Chem. 276:26516.
- Dallabrida, S.M. et al. (2005) Cardiovasc. Res. 96:e8.
- Samuel, S.M. et al. (2010) Diabetes 59:51.
- Holopainen, T. et al. (2009) Cancer Res. 69:4656.
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