Recombinant Human Noggin, Insect Cells Derived

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.

QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC

Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cells. The ED50 for this effect is 0.04-0.2 μg/mL in the presence of 50 ng/mL of Recombinant Human BMP-4.

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.

Approximately 23.0 kDa on SDS-PAGE under reducing conditions, containing 205 amino acids, and a molecular mass about 47.9 kDa homodimer under non-reducing conditions (Molecular size on SDS-PAGE will appear at approximately 50-80 kDa) .