Bone morphogenetic Protein 2

he transforming growth factor-beta (TGF-beta) super-family consists of a large number of growth and differentiation factors, such as TGF-betas, activins, inhibins, growth and differentiation factors (GDFs), and bone morphogenetic proteins (BMPs).  These TGF beta ligands act through specific serine/threonine type I and Type II receptor kinases (1).  These type I and II receptor kinases subsequently activate Smad proteins, which then propagate the signals into the nucleus to regulate target gene expression.   Several BMP isotypes have been identified  (BMP1 through MP16) have been recovered through molecular cloning.  Recombinant protein products from several of these clones (BMP2-BMP16) are members of the TGF-beta super-family of regulatory ligands.  There exist high degree of amino acid sequence homology between BMP5, BMP6, and BMP7, that constitute a subfamily within the BMPs.  The signaling systems of BMP are highly conserved from flies to mammals and have been shown to be important in the development of multiple organs.

The bone morphogenetic proteins (BMP) are implicated in several inductive differentiation processes in vertebrate ontogeny and patterning of nervous system.  Recently, these proteins have also emerged as candidates for regulating survival of mesencephalic dopaminergic and sympathetic neurons.  It has been shown that several bone morphogenetic proteins are induced in 14 day developing embryonic rat dorsal root ganglia (2).  BMPs exert survival promoting effects and positively modulate the effects of neurotrophins on sensory neurons (3).   BMP2 is a 471amino acid protein with an apparent MW of 58 kDa.  BMP2 transforms the human bone marrow-derived mesenchymal stem cells (MSCs) in to chondrocytic phenotype in high-density cultures (3).  Recent studies suggest that BMP2 induced ectopic bone formation involves both endochondral and intramembranous ossification (4).  Except for BMP-1, which is a metalloprotease, all other BMPs appears to be members of the TGF-beta regulatory molecules.  BMP1 plays important roles in regulating the deposition of fibrous extracellular matrix in vertebrates, including provision of the procollagen C-proteinase activity that processes the major fibrillar collagens I-III. Biglycan, a small leucine-rich proteoglycan, is a nonfibrillar extracellular matrix component with functions that include the positive regulation of bone formation (5). 

The BMP1-selective antibodies were generated against peptides form unique regions of the BMP1 protein.  FabGennix Inc. has  generated epitope specific rabbit anti-BMP4 and BMP8 polyclonal antibodies utilizing linear and cyclic peptide sequences.  These antibodies have been fully characterized for cross reactivity with other members of the bone morphogenetic proteins and other proteins.  Limited quantities of the antigenic blocking peptide and western blot positive control for BMP1 antibodies are also available.

For research use only, not for diagnostic or therapeutic use.