Novus' biologically active proteins are stringently purified to provide only the safest and most highly effective proteins available. This protein was expressed in E. coli, purified by HPLC, QC tested by SDS-PAGE and Western Blot and validated on appropriate cell lines for bioactivity. All HPLC and bioactivity data is provided for your assurance.
Details of Functionality
Noggin Protein is fully biologically active when compared to standard. The ED50 as determined by inhibiting BMP-4-induced alkaline phosphatase production of murine ATDC5 cells is less than 2 ng/ml, corresponding to a specific activity of > 5.0 x 10^5 IU/mg in the presence of 5 ng/ml BMP-4
>95% pure by SDS-PAGE
Less than 1 EU/ug of Noggin as determined by LAL method.
46.4 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Lyophilized from a 0.2 um filtered concentrated solution in 30 % acetonitrile, 0.1 % TFA.
>95% pure by SDS-PAGE
Recommended to centrifuge prior to opening. Reconstitute in 10 mM HAc to a concentration less than 0.25mg/mL. Apportion stock solutions into working aliquots and store at <-20C.
This lyophilized preparation is stable at 2-8 degrees C, but should be kept at -20 degrees C for long term storage, preferably desiccated. Upon reconstitution, the preparation is most stable at -20 to -80 degrees C, and can be stored for one week at 2-8 degrees C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20 degrees C to -80 degrees C. Avoid repeated freeze/thaw cycles.
Alternate Names for Recombinant Mouse Noggin Protein
symphalangism 1 (proximal)
synostoses (multiple) syndrome 1
Noggin encoded by the NOG gene, was first isolated from Xenopus, having the function of inducing secondary axis formation in frog embryos. It inhibits TGF-beta family ligands and preventing them from binding to their corresponding receptors. Noggin was originally found as a BMP-4 antagonist, and then has been shown to modulate the activities of other BMPs (BMP-2, 7, 13 and 14). Additionally, it has pleiotropic effect, both in early development and later stages. 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. In recent report, proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) have relation with the mutant of evolutionarily conserved amino acid residues of Noggin. Mature mouse Noggin shares 99% and 83% a.a. sequence identity with human and Xenopus Noggin, respectively.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.
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