Recombinant Human Angiopoietin-1, Biotinylated Protein Summary
|Details of Functionality
Measured by its ability to inhibit serum deprivation induced apoptosis in HUVEC human umbilical vein endothelial cells. Kwak, H.J. et al
. (1999) FEBS Letters 448
:249. The ED50
for this effect is 10-40 ng/mL in the presence of 5 μg/mL of a cross-linking antibody, Mouse Anti-polyHistidine Monoclonal Antibody (Catalog # MAB050
Mouse myeloma cell line, NS0-derived human Angiopoietin-1 protein
Ser20-Phe498, with a C-terminal 6-his tag
Accession # Q5HYA0
|Structure / Form
| Protein/Peptide Type
>90%, by SDS-PAGE with silver staining
<1.0 EU per 1 μg of the protein by the LAL method.
56 kDa (unlabeled).
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.
Packaging, Storage & Formulations
|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.
Lyophilized from a 0.2 μm filtered solution in Tris-Citrate and NaCl with BSA as a carrier protein.
>90%, by SDS-PAGE with silver staining
Reconstitute at 10 μg/mL in PBS containing at least 0.1% human or bovine serum albumin.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Angiopoietin-1, Biotinylated Protein
- 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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