Mouse GDF-5/BMP-14 Antibody

Growth Differentiation Factor 5 (GDF-5), also known as cartilage-derived morphogenetic protein 1 (CDMP-1), is a member of the bone morphogenetic protein (BMP) family which belongs to the transforming growth factor  beta (TGF-beta) superfamily. GDF-5 is synthesized as a large precursor protein that consists of an N-terminal 19 amino acid (aa) signal sequence, a 362 aa pro region and a 120 aa C-terminal mature peptide. Mature GDF-5 is a homodimeric protein which contains the characteristic seven conserved cysteine residues. GDF-5, GDF-6, and GDF-7, which share 80-86% identity, define a new subgroup within the BMP family. Like other TGF-beta superfamily proteins, GDF-5 is highly conserved across species. At the amino acid sequence level, mature human and mouse GDF-5 are 98% identical. It has been reported that GDF-5 has multiple functions including regulation of myogenesis, regulation of chondrogenesis, bone morphogenesis, and neuron differentiation and survival. GDF-5 response is mediated by the formation of hetero-oligomeric complexes of type I (BMPR-IB) and type II (BMPR-II or Activin R-II) sereine/threonine kinase receptors, and the activation of Smad proteins (Smad 1, 5, and 8).