Noggin human

Noggin (NOG) belongs to a group of diffusible proteins which bind to ligands of the TGF (transforming growth factor)-β family and regulate their activity by inhibiting their access to signaling receptors. The protein is secreted and exists as a disulfide-linked homodimer. The gene NOG is mapped to human chromosome 17q22. Recombinant human Noggin is a 23.1kDa non-disulfide-linked homodimer consisting of a total of 206 amino acid residues.

Noggin (NOG) human has been used as a BMP antagonist.

Noggin (NOG) was originally identified as a BMP-4 (bone morphogenetic protein 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. Transgenic mice over-expressing Noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. In mice, loss of noggin causes malformations in skeletal system. In mouse noggin is associated with tissue patterning by participating in cell differentiation, cell proliferation and apoptosis in the developing embryo. Mutations in the gene is associated with several disorders, including proximal symphalangism, multiple synostoses, tarsal/carpal coalition syndrome and Teunissen–Cremers syndrome. It is a gene which is also linked with conductive hearing loss. Polymorphism in the gene might be associated with reduced risk of nonsyndromic cleft lip with or without cleft palate (NSCLP).

Lyophilized without any additives.

Centrifuge the vial prior to opening. Avoid freeze-thaw cycles.

Reconstitute in water to a concentration of 0.1 to 1.0 mg/mL. Note: Due to solubility reasons the protein should be kept at low pH. This solution can then be diluted into other aqueous buffers.