Nogin (diervrij)

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.

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

< 0.01 ng/µg of protein (< 0.1 EU/µg)

≥ 98% by SDS-PAGE gel and 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