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Bone morphogenetic protein 4 (BMP-4) is a member of the highly conserved transforming growth factor β (TGF-β) superfamily. Mature BMP-4 is a disulfide-linked homodimeric protein consisting of two 116-amino-acid residue subunits, and is generated by the proteolytic removal of the signal peptide and propeptides (Xiao et al.). BMP-4 binds to type I and type II receptors on cells. This binding results in the phosphorylation of receptor 1, which in turn leads to the phosphorylation of Smad proteins, before going on to act as transcription factors (Zhang et al.). BMPs have been shown to be key regulators of embryogenesis and are known to play a role in the growth and differentiation of various cell types, including embryonic stem (ES) cells, induced pluripotent stem (iPS) cells, mesenchymal cells, epithelial cells, hematopoietic cells, and neuronal cells (Chadwick et al.; Graham et al.; Jones et al.; Lengerke et al.; Zhang et al.). This product is animal component-free (ACF).
Figure 1. Biological Activity and Molecular Mass of Human Recombinant BMP-4, ACF
(A) The biological activity of Human Recombinant BMP-4, ACF was tested using a BMP4-responsive luciferase reporter assay in transfected HEK293T cells. Firefly luciferase activity is normalized to the control Renilla luciferase activity. The EC50 is defined as the effective concentration of the growth factor at which BMP-4 response is at 50% of maximum. The EC50 in the above example is 30.2 pM (0.72 ng/mL).
(B) 3 μg of Human Recombinant BMP-4, ACF was resolved with SDS-PAGE under reducing (+) and non-reducing (-) conditions and visualized by Coomassie Blue staining. Human Recombinant BMP-4, ACF has a predicted molecular mass of 24 kDa (dimer).
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