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Human NOG Protein expressed in Escherichia coli (E. coli) - ABIN1080387
Guan, Du, Lv, Qu, Fu, Yuan et al.: Oxygen-glucose deprivation preconditioning protects neurons against oxygen-glucose deprivation/reperfusion induced injury via bone morphogenetic protein-7 mediated ERK, p38 and Smad signalling ... in Clinical and experimental pharmacology & physiology 2016
Human NOG Protein expressed in Escherichia coli (E. coli) - ABIN413676
Umezu, Yamanouchi, Iida, Miura, Tomooka: Follistatin-like-1, a diffusible mesenchymal factor determines the fate of epithelium. in Proceedings of the National Academy of Sciences of the United States of America 2010
The secreted polypeptide, encoded by this gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, this protein may have a principal role in creating morphogenic gradients. The protein appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of the ortholog suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified\; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as this gene. All of these mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of this human gene is highly homologous to that of Xenopus, rat and mouse.
symphalangism 1 (proximal)
, noggin 1
, noggin protein