|Application ||WB, E|
|Other Accession||Q62809, P97466, NP_005441.1|
|Calculated MW||25774 Da|
|Antigen Region||84-111 aa|
|Other Names||Noggin, NOG|
|Target/Specificity||This NOG antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 84-111 amino acids from the Central region of human NOG.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||NOG Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|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 (PubMed:21976273).|
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Provided below are standard protocols that you may find useful for product applications.
The secreted polypeptide, encoded by this gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, this protein may have a principal role in creating morphogenic gradients. The protein appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of the ortholog suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as this gene. All of these mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of this human gene is highly homologous to that of Xenopus, rat and mouse.
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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