Catalog Number:  C22-128-09
Source:  Escherichia coli.
Molecular Weight:  Approximately 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.
Quantity:  5μg/20μg/1000μg
AA Sequence:  MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPPEDRPG
 GGGGPAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLRRKLQMWL
 WSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSV PEGMVCKPSK SVHLTVLRWR
 CQRRGGQRCG WIPIQYPIIS ECKCSC
Purity:  >95% by SDS-PAGE and HPLC analyses.
Biological Activity:  Fully biologically active when compared to standard. The ED50 determined by inhibiting BMP-4-
 induced alkaline phosphatase production ofmurine ATDC5 cells is less than 2 ng/ml, corresponding to a specific activity of＞ 5.0 × 105 IU/mg in the presence of 5ng/ml BMP-4.
Physical Appearance:  Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation:  Lyophilized from a 0.2μm filtered concentrated solution in 30% acetonitrile, 0.1% TFA.
Endotoxin:  Less than 1EU/μg of rMuNoggin as determined by LAL method.
Reconstitution:  We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the
 bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/mL. Stock solutions should be
 apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in
 appropriate buffered solutions.
Storage:  This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage,
 preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For
 maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to
 -70°C. Avoid repeated freeze/thaw cycles.
Usage:  This material is offered by Shanghai Corning Bio-Tech for research, laboratory or further
 evaluation purposes. NOT FOR HUMAN USE.

Murine Noggin
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.