| Literature DB >> 22381466 |
Chandramohan Kattamuri1, David M Luedeke, Thomas B Thompson.
Abstract
Bone morphogenetic proteins (<span class="Gene">BMPs) are secreted protein ligands that control numerous biological processes, such as cell differentiation and cell proliferation. Ligands are regulated by a large number of structurally diverse extracellular antagonists. PRDC or protein related to DAN and cerberus is a BMP antagonist of the DAN family, which is defined by a conserved pattern of cysteine residues that form a ring structure. Here we present the expression and purification of recombinant mouse PRDC (mPRDC) from bacterial (Escherichia coli) inclusion bodies through oxidative refolding. Functional mPRDC was isolated from a nonfunctional component through reverse phase chromatography and shown to inhibit BMP2 and BMP4 in a cell-based luciferase reporter assay. Recombinant mPRDC also bound directly to BMP2, BMP4 and BMP7, but not activin A. Furthermore, circular dichroism indicated that mPRDC is folded and contains a higher than anticipated helical content for a DAN family member protein.Entities:
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Year: 2012 PMID： 22381466 PMCID： PMC3319168 DOI： 10.1016/j.pep.2012.02.010
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650