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Species
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Human
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Accession
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Q13253
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GeneID
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9241
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Source
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Escherichia coli.
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Molecular Weight
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重组人头蛋白Approximately 46.3 kDa, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.
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Quantity
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5µg/20µg/1000µg
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AA Sequence
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MQHYLHIRPA PSDNLPLVDL IEHPDPIFDP KEKDLNETLL RSLLGGHYDP GFMATSPPED RPGGGGGAAG GAEDLAELDQ LLRQRPSGAM PSEIKGLEFS EGLAQGKKQR LSKKLRRKLQ MWLWSQTFCP VLYAWNDLGS RFWPRYVKVG SCFSKRSCSV PEGMVCKPSK SVHLTVLRWR CQRRGGQRCG WIPIQYPIIS ECKCSC
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Purity
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> 95 % by SDS-PAGE and HPLC analyses.
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Biological Activity
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重组人头蛋白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 3.0 ng/ml, corresponding to a specific activity of > 3.3 × 105 IU/mg in the presence of 5 ng/ml rHuBMP-4.
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Physical Appearance
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Sterile Filtered White lyophilized (freeze-dried) powder.
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Formulation
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Lyophilized from a 0.2 μm filtered concentrated solution in 30 % acetonitrile, 0.1 % TFA.
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Endotoxin
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Less than 1 EU/μg of rHuNoggin as determined by LAL method.
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Reconstitution
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重组人头蛋白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.
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Storage
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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.
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重组人头蛋白
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Reference
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1. Davis SWandCamper SA. 2007. Dev Biol, 305: 145-60.
2. Zhu W, Kim J, Cheng C, et al. 2006. Bone, 39: 61-71.
3. Oxley CD, Rashid R, Goudie DR, et al. 2008. Horm Res, 69: 221-6.
4. Bayramov AV, Eroshkin FM, Martynova NY, et al. 2011. Development, 138: 5345-56.
5. Secondini C, Wetterwald A, Schwaninger R, et al. 2011. PLoS One, 6: e16078.
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Background
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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-β 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 human Noggin shares 99 %, 99 %, 98 %, 97 % and 89 % a.a. sequence identity with mouse, rat, bovine, equine and chicken Noggin, respectively.
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