Noggin is a secreted homodimeric glycoprotein that is an antagonist of bone morphogenetic proteins (BMPs). Mature Human Noggin contains an N-terminal acidic region, a central basic heparin-binding segment and a C-terminal cysteine-knot structure. Noggin is very highly  conserved among vertebrates, such that mature human Noggin shares 99%, 99%, 98%, 97% and 89% aa sequence identity with mouse, rat bovine, equine and chicken Noggin, respectively.  Secreted  Noggin probably remains close to the cell surface due to its binding of  heparin-containing  proteoglycans. Noggin binds some BMPs such as BMP4 with high affinity and others such as BMP7 with lower affinity. It antagonizes BMP bioactivities by blocking epitopes on BMPs that are needed for binding to both type I and type II receptors. Noggin is expressed in defined areas of the adult central nervous system and peripheral tissues such as lung, skeletal muscle and skin.  During culture of  human embryonic stem cells  (hESC) or  neural stem cells under certain conditions, addition of Noggin to  antagonize  BMP activity  may allow stem cells to proliferate while maintaining their undifferentiated state, or alternatively, to differentiate into dopaminergic neurons.