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Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP‐2
Author(s) -
Kirsch Thomas,
Nickel Joachim,
Sebald Walter
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01214-x
Subject(s) - ectodomain , bone morphogenetic protein , recombinant dna , bone morphogenetic protein 2 , chemistry , receptor , microbiology and biotechnology , size exclusion chromatography , biochemistry , biology , in vitro , enzyme , gene
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.