| Source: |
Escherichia coli |
| Molecular Weight: |
Approximately 46.4 kDa, a disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains. |
| AA Sequence: |
MQHYLHIRPA PSDNLPLVDL IEHPDPIFDP KEKDLNETLL RSLLGGHYDP GFMATSPPED RPGGGGGPAG GAEDLAELDQ LLRQRPSGAM PSEIKGLEFS EGLAQGKKQR LSKKLRRKLQ MWLWSQTFCP VLYAWNDLGS RFWPRYVKVG SCFSKRSCSV PEGMVCKPSK SVHLTVLRWR CQRRGGQRCG WIPIQYPIIS ECKCSC |
| Purity: |
> 95% by SDS-PAGE and HPLC analyses. |
| Biological Activity: |
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 × 105 IU/mg in the presence of 5 ng/mL BMP-4. |
| Physical Appearance: |
Sterile filtered white lyophilized (freeze-dried) powder. |
| Formulation: |
Lyophilized from a 0.2 μm filtered concentrated solution in 30% acetonitrile, 0.1% TFA. |
| Endotoxin: |
Less than 1 EU/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 10 mM HAc to a concentration less than 0.25 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions. |
| Stability & Storage: |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
1 month, 2 to 8°C under sterile conditions after reconstitution.
3 months, -20 to -70°C under sterile conditions after reconstitution. |
| Background: |
Noggin, encoded by the NOG gene, was initially discovered in Xenopus, where it plays a crucial role in inducing secondary axis formation in frog embryos. It functions by inhibiting ligands of the TGF-β family, thereby preventing them from binding to their respective receptors. Originally identified as an antagonist to BMP-4, Noggin has since been found to modulate the activities of other BMPs such as BMP-2, 7, 13, and 14. Its effects are not limited to a specific developmental stage but exert pleiotropic influences throughout early and later developmental processes.
Studies involving mouse knockouts of noggin have highlighted its involvement in various developmental processes, including neural tube fusion and joint formation. Recent findings suggest that mutations in evolutionarily conserved amino acid residues of Noggin are associated with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1).
Comparative analysis reveals that mature mouse Noggin shares a remarkable 99% and 83% amino acid sequence identity with its human and Xenopus counterparts, respectively. |
