NOGGIN

Noggin belongs to a group of diffusible proteins which bind to ligands of the TGF-beta family and regulate their activity by inhibiting their access to signaling receptors. 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 human Noggin is a 46.2 kDa non-disulfide-linked homodimer consisting of a total of 206 amino acid residues.

NOG; SYM1; SYNS1

9241

Q13253

NP_005441

NM_005450

17q22

Human

Chicken, Mouse, Human

QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC

< 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 ATDC chondrogenic cells. The expected ED50 for this effect is 2.0-3.0 ng/ml of Noggin.

205

Lyophilized

46 kDa

HEK 293 cells