Mouse Noggin Antibody

Noggin was originally cloned based on its dorsalizing activity in Xenopus embryos. Mammalian Noggins were subsequently identified and cloned from human, mouse and rat cDNA libraries. Mouse Noggin cDNA encodes a 232 amino acid (aa) residue precursor protein with 19 aa residue putative signal peptide that is cleaved to generate the 213 aa residue mature protein which is secreted as a homodimeric glycoprotein. Noggin is a highly conserved molecule. Mature mouse Noggin shares 99% and 83% aa sequence identity with human and Xenopus Noggin, respectively. Noggin has a complex pattern of expression during embryogenesis. In the adult, Noggin is expressed in the central nervous system and in several adult peripheral tissues such as lung, skeletal muscle and skin. Noggin has been shown to be a high-affinity BMP (bone morphogenetic protein) binding protein that antagonizes BMP bioactivities.