Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-β family, and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-β ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Recombinant Human Noggin is a 46 kDa disulfide-linked homodimer consisting of two 205 amino acid polypeptide chains. Monomeric noggin migrates at an apparent molecular weight of approximately 20.0-33.0 kDa by SDS PAGE analysis under reducing conditions.