Insulin-like growth factor binding protein 6, also known as IGFBP-6, is a member of the IGF binding protein superfamily. The IGFBPs are present in serum, in virtually all biological fluids, tissue extracts, and conditioned medium from a variety of cell lines. They appear to be present and conserved in lower species, which suggests a functionally important role throughout evolution. The amino-terminal and carboxyl-terminal sequences of the IGFBPs are conserved between the various binding proteins, whereas the mid-region of the IGFBPs shows considerable variation between the different members of this family. The IGF system is essential for physiological growth, and it takes part in a number of diseases, including cancer. IGF activity is modulated by a family of high-affinity IGFBPs, and IGFBP-6 is distinctive because of its marked binding preference for IGF-II over IGF-I. Besides regulating both IGF-II and IGF-I, IGFBP-6 also has IGF-independent effects that include the inhibition of angiogenesis and promotion of cancer cell migration. Additionally, IGFBP-6 was found to interact with the vitamin D receptor. This interaction plays a critical role of vitamin D3 in osteoblast differentiation. IGFBP-6 is expressed in ovarian cells, prostatic cells, and fibroblasts. IGFBP-6 is found predominantly in cerebral spinal fluid and serum. Human IGFBP-6 shares a 73% amino acid sequence homology with its mouse counterpart.
Size
100 μg
Concentration
n/a
Applications
BA
Other Names
Insulin-like growth factor binding protein 6, IBP6, IGFBP6