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Insulin-like growth factor-binding protein 7(IGFBP-7) is a secreted glycosylated protein that contains threeprotein domain modules. IGFBP7 contains an N-terminal IGFBP domain, followed by a Kazal-type serineproteinase inhibitor domain and a C-terminal immunoglobulin-like C2-type domain. Human and mouse IGFBP7are highly homologous and share 94% aa sequence identity. It is expressed in many normal tissues and incancer cells. It is abundantly expressed in high endothelial venules (HEVs) of blood vessels in the secondarylymphoid tissues. It binds IGF and insulin with very low affinity and has been shown to enhance the mitogenicactions of IGF and insulin. IGFBP7 also has IGF/insulin-independent activities. It interacts with heparan sulfateproteoglycans, type IV collagen, and specific chemokines. It supports weak cell adhesion, promotes cellspreading on type IV collagen, and stimulates the production of the potent vasodilator PGI2. It modulatestumor cell growth and has also been implicated in angiogenesis.