The angiopoietin (Ang) family of growth factors includes four members, all of which bind to the endothelial receptor tyrosine kinase Tie2. Two of the Angs, Ang-1 and Ang-4, activate the Tie2 receptor, whereas Ang-2 and Ang-3 inhibit Ang-1-induced Tie2 phosphorylation. Angiopoietin-1 (Ang-1) is a secreted growth factor which binds to and activates the Tie-2 receptor tyrosine kinase. The factor enhances endothelial cell survival and capillary morphogenesis, and also limits capillary permeability. Ang-2 binds the same receptor but fails to activate it: hence, it is a natural inhibitor of Ang-1. Ang-2 destabilises capillary integrity, facilitating sprouting when ambient vascular endothelial growth factor (VEGF) levels are high, but causing vessel regression when VEGF levels are low. Tie-1 is a Tie-2 homologue but its ligands are unknown. Angiopoietin and Tie genes are expressed in the mammalian metanephros, the precursor of the adult kidney, where they may play a role in endothelial precursor growth. Tie-1-expressing cells can be detected in the metanephros when it first forms and, based on transplantation experiments, these precursors contribute to the generation of glomerular capillaries. During glomerular maturation, podocyte-derived Ang-1 and mesangial-cell-derived Ang-2 may affect growth of nascent capillaries. After birth, vasa rectae acquire their mature configuration and Ang-2 expressed by descending li mbs of loops of Henle would be well placed to affect the growth of this medullary microcirculation. Finally, preliminary data implicate angiopoietins in deregulated vessel growth in Wilms' kidney tumours and in vascular remodelling after nephrotoxicity. Altogether, existing data suggest that VEGF-A and Angiopoietins not only have quite different roles during vascular development, but also very complementary and coordinated roles. Human Ang-1 shares approximately 97% and 60% amino acid sequence identity with mouse Ang-1 and human Ang-2, respectively.
>90% by SDS-PAGE and analyzed by silver stain.
<1.0 EU/µg as determined by the LAL method
Fusion Protein Tag
Protein Accession No.
Amino Acid Sequence
s nqrrspensg rrynriqhgq caytfilpeh dgncresttd qyntnalqrd aphvepdfss qklqhlehvm enytqwlqkl enyivenmks emaqiqqnav qnhtatmlei gtsllsqtae qtrkltdvet qvlnqtsrle iqllenslst yklekqllqq tneilkihek nsllehkile megkhkeeld tlkeekenlq glvtrqtyii qelekqlnra ttnnsvlqkq qlelmdtvhn lvnlctkegv llkggkreee kpfrdcadvy qagfnksgiy tiyinnmpep kkvfcnmdvn gggwtviqhr edgsldfqrg wkeykmgfgn psgeywlgne fifaitsqrq ymlrielmdw egnraysqyd rfhignekqn yrlylkghtg tagkqsslil hgadfstkda dndncmckca lmltggwwfd acgpsnlngm fytagqnhgk lngikwhyfk gpsyslrstt mmirpldfhh hhhh
N-terminal Sequence Analysis
State of Matter
Predicted Molecular Mass
The predicted molecular weight of Recombinant Human ANG-1 is Mr 56 kDa. However, the actual molecular weight as observed by migration on SDS Page is Mr 70 kDa.
This recombinant protein was lyophilized from a 0.2 μm filtered solution in Tris-Citrate and sodium chloride (NaCl).
Storage and Stability
This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
Country of Origin
Next Day Ambient
NCBI Gene Bank
References & Citations
1. Agrawal, DK. et al. (2006) Curr Mol Med. 6(8):831-41.
2. Baek, HS. et al. (2006) Exp Clin Endocrinol Diabetes. 114(8):438-43.
3. Nicosia, RF. et al. (2006) Physiol Genomics. 27(1):20-8.
4. Bates, DO. et al. (2006) Microcirculation. 13(6):423-37.
5. Krüssel, JS. et al. (2006) Reprod Fertil Dev. 18(5):509-16.
6. Lee, KJ. et al. (2006) Cancer Res. 66 (12):6167-74.
IMPORTANT Use lot specific datasheet for all technical information pertaining to this recombinant protein.
Products are for research use only. Not for use in diagnostic or therapeutic procedures.