Noggin Human

Noggin was initially identified as a BMP-4 antagonist, critical for the proper formation of the head and other dorsal structures during embryonic development . It modulates the activities of several BMPs, including BMP-2, BMP-4, BMP-7, BMP-13, and BMP-14 . By binding to these BMPs, Noggin inhibits their access to signaling receptors, thereby regulating cellular responses based on the local concentration of the signaling molecules .

Recombinant human Noggin is typically produced in various expression systems, including mouse myeloma cell lines (NS0) and HEK293 cells . It is a disulfide-linked homodimer consisting of two 205 amino acid polypeptide chains, with a molecular weight of approximately 46 kDa . The protein is glycosylated and migrates at an apparent molecular weight of 28-33 kDa by SDS-PAGE analysis under reducing conditions .

Noggin’s biological activity is determined by its ability to inhibit BMP-induced alkaline phosphatase production in chondrogenic cells . For instance, it can inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cells, with an effective dose (ED50) ranging from 0.0200-0.160 μg/mL in the presence of 50 ng/mL of recombinant human BMP-4 .

Recombinant human Noggin is widely used in research to study its role in various biological processes and disease mechanisms. It is particularly significant in the fields of developmental biology, neurobiology, and stem cell research . For example, targeted deletion of Noggin in mice results in prenatal death and severe skeletal malformations, highlighting its critical role in skeletal development . Conversely, overexpression of Noggin in mature osteoblasts leads to impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis .

Recombinant human Noggin is typically lyophilized from a filtered solution and can be reconstituted in PBS containing at least 0.1% human or bovine serum albumin . It is shipped at ambient temperature and should be stored at -20 to -70 °C to maintain stability and activity .