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.  Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures.  Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14.  Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system.  Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis.  Recombinant Murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.

Source: E.coli

Synonyms: None

AA Sequence (monomer): MQHYLHIRPA PSDNLPLVDL IEHPDPIFDP KEKDLNETLL RSLLGGHYDP GFMATSPPED RPGGGGGPAG GAEDLAELDQ LLRQRPSGAM PSEIKGLEFS EGLAQGKKQR LSKKLRRKLQ MWLWSQTFCP VLYAWNDLGS RFWPRYVKVG SCFSKRSCSV PEGMVCKPSK SVHLTVLRWR CQRRGGQRCG WIPIQYPIIS ECKCSC

Purity: ≥ 95% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to inhibit 5.0 ng/ml of BMP-4 induced alkaline phosphatase production by ATDC5 chondrogenic cells. The expected ED₅₀ for this effect is 1.0-2.0 ng/ml of Noggin.