Noggin Protein, Human Recombinant

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 human Noggin is a 46 kDa disulfide-linked homodimer (120-10C) consisting of two 206 amino acid polypeptide chains. Monomeric glycosylated Noggin migrates at an apparent molecular weight of approximately 28.0-33.0 kDa by SDS PAGE analysis under reducing conditions.

Product Source: HEK293 cells

Research Category
Stem Cell Research

Research Sub Category
Growth Factors & Receptors

Cross Reactivty
Mouse, Chicken

Product is filtered through a 0.2 micron filter before lyophilization.

Store at -20°C for up to 6 months from date of receipt.

Bioactivity assay: 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.

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