Recombinant Mouse Noggin

Noggin is a secreted glycoprotein predominantly expressed by the dorsal mesoderm during embryogenesis that inhibits TGF-β signal transduction by binding to TGF-β family ligands and preventing them from binding to their corresponding receptors. Noggin is expressed in condensing cartilage and immature chondrocytes.¹ Noggin plays a key role in neural induction by inhibiting BMP4, along with other TGF-β signaling inhibitors such as chordin and follistatin. Noggin plays a crucial role in bone development, joint formation, and neural tube fusion.

The biological activity of Mouse Noggin was determined by its ability to inhibit rhBMP-4 induced alkaline phosphatase production by ATDC5 cells. The expected ED₅₀ for this effect is typically 0.06 - 0.3 μg/ml in the presence of 75 ng/ml of rhBMP-4.

Fc Fusion Protein

The DNA sequence encoding the signal peptide from human CD33 joined with amino acid residues 20 - 232 of mouse noggin was fused to the Fc region of human IgG1 via a polypeptide linker. The chimeric protein was expressed in a mouse myeloma cell line, NS0.

Leu20

Lyophilized

The predicted molecular weight of Recombinant Mouse Noggin is Mr 50 kDa. However, the actual molecular weight as observed by migration on SDS-PAGE is Mr 55-60 kDa.

50

This recombinant protein was 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) pH 7.2 – 7.3 with no calcium, magnesium, or preservatives.

This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.

Next Day Ambient

1. Harland, RM. et al. (1998) Science 280: 1455