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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2.

Bone morphogenetic protein-2 (BMP-2) is a member of the transforming growth factor beta 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.[1]

References

  1. Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2. Kirsch, T., Nickel, J., Sebald, W. FEBS Lett. (2000) [Pubmed]
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