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NOG Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q13253 |
|---|---|
| Clone Names | 90723226 |
| Gene ID | 9241 |
|---|---|
| Other Names | Noggin, NOG |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | NOG |
|---|---|
| Function | Inhibitor of bone morphogenetic proteins (BMP) signaling which is required for growth and patterning of the neural tube and somite. Essential for cartilage morphogenesis and joint formation. Inhibits chondrocyte differentiation through its interaction with GDF5 and, probably, GDF6 (PubMed:21976273, PubMed:26643732). |
| Cellular Location | Secreted. |
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Provided below are standard protocols that you may find useful for product applications.
Background
The secreted polypeptide, encoded by this gene, binds andinactivates members of the transforming growth factor-beta(TGF-beta) superfamily signaling proteins, such as bonemorphogenetic protein-4 (BMP4). By diffusing through extracellularmatrices more efficiently than members of the TGF-beta superfamily,this protein may have a principal role in creating morphogenicgradients. The protein appears to have pleiotropic effect, bothearly in development as well as in later stages. It was originallyisolated from Xenopus based on its ability to restore normaldorsal-ventral body axis in embryos that had been artificiallyventralized by UV treatment. The results of the mouse knockout ofthe ortholog suggest that it is involved in numerous developmentalprocesses, such as neural tube fusion and joint formation.Recently, several dominant human NOG mutations in unrelatedfamilies with proximal symphalangism (SYM1) and multiple synostosessyndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiplejoint fusion as their principal feature, and map to the same region(17q22) as this gene. All of these mutations altered evolutionarilyconserved amino acid residues. The amino acid sequence of thishuman gene is highly homologous to that of Xenopus, rat and mouse.
References
Rudnik-Schoneborn, S., et al. Am. J. Med. Genet. A 152A (6), 1540-1544 (2010) :Song, K., et al. J. Biol. Chem. 285(16):12169-12180(2010)Mangold, E., et al. Nat. Genet. 42(1):24-26(2010)Gutierrez, S.J., et al. Acta Odontol Latinoam 23(1):13-19(2010)Zhao, J., et al. BMC Med. Genet. 11, 96 (2010) :
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