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- SPECIES: Human
- SOURCE SPECIES: HEK293 cells
- RECOMBINANT PROTEIN SEQUENCE: QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC
- BIOLOGICAL ACTIVITY: Biological activity was 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.
Properties
- PURITY: Greater than 95% by SDS-PAGE gel and HPLC analyses.
Endotoxin level is less than 0.1 ng per μg (1EU/μg). - PHYSICAL STATE: Lyophilized
- STORAGE CONDITIONS: The lyophilized Noggin recombinant protein is stable for at least 2 years from date of receipt at -20°C. Reconstituted Noggin is stable for at least 3 months when stored in working aliquots with a carrier protein at -20°C. As with any protein, exposing Noggin recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.
Additional Info
- NCBI OFFICIAL SYMBOL: NOG
- ADDITIONAL NAMES: SYM1, SYNS1, Noggin
- Protein Accession Number: NP_005441.1
- PROTEIN GI NUMBER: 4885523
- NCBI GENE ID NUMBER: 9241
Background
- 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.
Disclaimer
- FOR RESEARCH USE ONLY
For additional information, visit ProSci's Terms & Conditions Page. - Disclaimer: This product is for research use only.
Shipping Info
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