NOGGIN

Noggin belongs to a group of diffusible proteins which 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 is 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 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.

NOG; SYM1; SYNS1

18121

P97466

NP_032737

NM_008711

11 C; 11 50.5 cM

Mouse

Mouse, Human, Chicken

MQHYLHIRPA PSDNLPLVDL IEHPDPIFDP KEKDLNETLL RSLLGGHYDP GFMATSPPED RPGGGGGPAG GAEDLAELDQ LLRQRPSGAM PSEIKGLEFS EGLAQGKKQR LSKKLRRKLQ MWLWSQTFCP VLYAWNDLGS RFWPRYVKVG SCFSKRSCSV PEGMVCKPSK SVHLTVLRWR CQRRGGQRCG WIPIQYPIIS ECKCSC

< 0.1 ng/µg of protein (< 1EU/µg)

> 95% by SDS-PAGE & HPLC analyses

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.

206

Lyophilized

46.4 kDa

E. coli