Endostatin murine

Endostatin was originally isolated from the conditioned media of EOMA, a murine hemangioendothelioma non-metastatic cell line. It is a derivative of collagen XVIII, and is the C-terminal 20kDa peptide of the same. Collagen XVIII is a proteoglycan present in the basement membrane and vascular walls. Proteases such as, cathepsin L and matrix metalloproteases, cleave the C-terminal domain containing protease sensitive region. It has a partly arginine-rich globular fold, which acts as the heparin-binding epitope.

Endostatin is a potent inhibitor of angiogenesis and tumor growth in vitro and in vivo; specifcally inhibits endothelial cell proliferation.

Endostatin is a potent inhibitor of angiogenesis and tumor growth in vitro and in vivo; specifcally inhibits endothelial cell proliferation. Recombinant Endosatin expressed in yeast causes G1 arrest of endothelial cells, and endostatin treatment results in apoptosis of HUVE and HMVE cells.

Endostatin is an endogenous inhibitor of angiogenesis, and in vitro inhibits the migration of endothelial cells. Collagen XVIII is cleaved to form endostatin, and this system might act as the negative control of angiogenesis. During wound healing, endostatin decreases the amount of blood vessels that function normally, along with the matrix density in granulation tissue. However, it does not have an overall impact on wound healing. As it is a potent inhibitor of angiogenesis, it also strongly suppresses tumor growth.

17 mM citric-phosphate buffer, pH 6.2.

US Patent 5,854,205. Sold under license from CMCC.