The secreted polypeptide NOGGIN, encoded by the NOG gene, belongs to a group of diffusible proteins which bind to ligands of the TGF-β superfamily and regulate their activity by inhibiting their access to signaling receptors. It binds and inactivates for example bone morphogenetic protein-4 (BMP4) and 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. By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, NOGGIN may have a principal role in creating morphogenic gradients. It appears to have pleiotropic effect, both early in development as well as in later stages. 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 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 NOGGIN 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 NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse. Recombinant human NOGGIN produced in 293 cells is a glycosylated 46 kDa disulfide-linked homodimer 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.
Human NOG expressed in 293 cells
CAT# CSC-CTK0549-20 (20 μg); CAT# CSC-CTK0549-100 (100 μg)
Greater than 95% as determined by SDS-PAGE and RP-HPLC analysis.
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.
Less than 1 EU/μg.
Lyophilized from a sterile-filtered protein solution.
Please centrifuge product briefly before opening the vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water or 10 mM acetate to a concentration of 0.1- 1.0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized powder, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein should be stored long-term in undiluted working aliquots at –20°C and is stable for at least 3 months under these conditions. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze / thaw cycles.
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