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Description
Purified anti-IGFBP-3. The insulin-like growth factor system includes two receptors (IGF-1R and IGF-2R), two ligands (IGF-1 and IGF-2), and seven binding proteins (IGFBP1-7). The binding proteins are produced in the liver and bind to the IGFs with different affinities, thus regulating the interaction of the IGFs with their receptors. Insulin-like growth factor binding protein-3 (IGFBP-3) is the major serum carrier protein for IGF proteins. IGFBP-3 sequesters IGF in a stable ternary complex with the acid-labile subunit (ALS). IGFBP-3 binds IGF-1 with high affinity and specificity and modulates IGF-1 action. IGFBP-3 undergoes limited enzymatic proteolysis to generate small N-terminal fragments. These proteolytic products lose their affinity for IGF-1 and IGF-2. Nevertheless, they preserve IGF independent activity. In that sense, a 16 kD fragment (1-95-IGFBP-3) and the full length molecule can potentiate apoptosis in colorectal epithelial cells, and this apoptotic process is associated with the inhibition of TNF-α-induced NF-κB activity. In addition, IGFBP-3 has been detected in the cell nucleus and interacts with 9-cis retinoic acid receptor-alpha (RXR-α), which is a nuclear receptor that is required for the apoptosis-inducing effects of IGFBP-3. IGFBP-3R physically interacts and activates caspase-8 and mediates IGFBP-3-induced apoptosis and tumor suppression.
Immunogen
Human IGFBP-3, amino acids (Gly28-Glu291) (Accession# X64875) with an N-terminal Met, was expressed in 293E cells.
Other Names
Insulin-like growth factor binding protein 3, IGF-Binding Protein 3, Growth Hormone-Dependent Binding Protein, Binding Protein 29, IBP3, BP-53, IGFBP3