Noggin human

A bone morphogenetic protein (BMP) antagonist is coded by noggin. The node, notochord and dorsal somite shows its expression. It possess a cystine-knot domain, having two β-strand finger-like loops.

Noggin human has been used a supplement in 20% complete medium for isolation of crypts, establishment of human enteroid cultures. It has also been used as a growth factor supplement for pancreatic endoderm specification medium.

Noggin is essential for the normal mouse development. Noggin is required for cartilage morphogenesis and joint formation. It is also an inhibitor of bone morphogenic protein (BMPs) signaling, which is necessary for the growth and patterning of neural tube and somites. Studies indicate Noggin may play a critical role in the formation of gradients of BMP activity. Noggin is produced in the mesoderm in developing embryos and has been shown to have a high affinity to BMP binding protein. When Noggin binds to BMPs, inhibition occurs, preventing BMPs from interacting with receptors on the cell surface. Knockout mice lacking expression of Noggin die at birth from multiple defects including bony fusion of the appendicular skeleton. Noggin has a high binding affinity to heparin and heparan sulfate proteoglycans at the cell surface. Heparan sulfate-bound Noggin remains active and capable of binding BMP4 at the plasma membrane. Noggin can also be competitively displaced by heparin when bound to cells that express heparan sulfate proteoglycan.

Noggin is required for cartilage morphogenesis and joint formation. It is also an inhibitor of bone morphogenic protein (BMPs) signaling, which is necessary for the growth and patterning of neural tube and somites. Studies indicate Noggin may play a critical role in the formation of gradients of BMP activity. Noggin is produced in the mesoderm in developing embryos and has been shown to have a high affinity to BMP binding protein. When Noggin binds to BMPs, inhibition occurs, preventing BMPs from interacting with receptors on the cell surface. Studies indicate Noggin plays a critical role in the formation of gradients of BMP activity. Knockout mice lacking expression of Noggin die at birth from multiple defects including bony fusion of the appendicular skeleton.

Noggin has a high binding affinity to heparin and heparan sulfate proteoglycans at the cell surface. Heparan sulfate-bound Noggin remains active and capable of binding BMP4 at the plasma membrane. Noggin can also be competitively displaced by heparin when bound to cells that express heparan sulfate proteoglycan.

HumanKine Noggin is expressed in human HEK 293 cells using a scaleable suspension cell culture system. The protein is a highly stable, authentically glycosylated,disulfide linked 65 kDa homodimer. Production in human HEK 293 cells offers authentic glycosylation. Glycosylation contributes to stability in cell growth media and other applications.

The specific activity was determined by the dose dependent inhibition of rhBMP4 induced alkaline phosphate production by ATDC5 cells.

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