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• W2899661502 abstract "Binding of a BMP to its cognate cell surface receptors is the initiating step in the BMP signaling cascade. Thus, knowing which BMP-receptor complexes form is vital for understanding the physiological activities of a particular BMP. Here, we describe a surface plasmon resonance (SPR)-based, high-throughput approach that allows fast identification and evaluation of BMP-receptor complexes. Briefly, the extracellular, BMP-binding domains of receptors are produced as human IgG1-Fc-fusion proteins. The Fc moiety enables simple capture of the Fc-receptor-fusion protein on the sensor chip, supports a highly reproducible, uniform approach of surface regeneration, and ensures full activity of the receptor moiety. BMPs are injected over the captured receptors at one concentration (approximately 60-100 nM), permitting stratification of high-affinity, medium-affinity, and low-affinity binders. Using this concentration range, equilibrium dissociation constants for high-affinity and medium-affinity binders can be estimated with good accuracy and with great precision from the single injection binding curves." @default.
• W2899661502 created "2018-11-16" @default.
• W2899661502 creator A5030497885 @default.
• W2899661502 creator A5074597936 @default.
• W2899661502 date "2018-11-10" @default.
• W2899661502 modified "2023-09-23" @default.
• W2899661502 title "High-Throughput, Biosensor-Based Approach to Examine Bone Morphogenetic Protein (BMP)–Receptor Interactions" @default.
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• W2899661502 doi "https://doi.org/10.1007/978-1-4939-8904-1_5" @default.
• W2899661502 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6319254" @default.
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