Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2
Abstract
Bone morphogenetic protein-2 (BMP-2) is a member of the transforming growth factor β superfamily which induces bone formation and regeneration, and important steps during early embryonic development. BMP-2 signals via oligomerization of type I and type II serine/threonine kinase receptors. We report here expression of the extracellular domain of the human type IA receptor for BMP-2 (BMPR-IA) in Escherichia coli. This soluble form of BMPR-IA (sBMPR-IA) was purified employing a BMP-2 affinity column. Gel filtration experiments and analysis of gel filtration fractions by polyacrylamide electrophoresis and densitometry reveal that BMP-2 forms a defined 1:2 complex with sBMPR-IA that can be purified and hopefully used for crystallization studies.
- Publication:
-
FEBS Letters
- Pub Date:
- January 2000
- DOI:
- 10.1016/S0014-5793(00)01214-X
- Bibcode:
- 2000FEBSL.468..215K
- Keywords:
-
- Bone morphogenetic protein-2;
- Bone morphogenetic protein receptor type IA;
- Transforming growth factor β superfamily;
- Binding stoichiometry;
- BMP-2;
- bone morphogenetic protein-2;
- sBMPR-IA;
- soluble bone morphogenetic protein receptor type IA;
- TGF-β;
- transforming growth factor β;
- ActR-II;
- activin receptor type II;
- IL;
- interleukin;
- IFN-γ;
- interferon-γ;
- NGF;
- nerve growth factor;
- VEGF;
- vascular endothelial growth factor;
- ECD;
- extracellular domain;
- MW;
- molecular weight;
- PAGE;
- polyacrylamide gel electrophoresis