Recombinant Mouse Endorepellin His-tag Protein, CF Summary
Glu3683-Ser4383, with a C-terminal 6-His tag
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 300 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||
Immobilized Recombinant Mouse Endorepellin supports theadhesion of SVEC4‑10 mouse vascular endothelial cells. The ED50 for thiseffect is 0.75‑4.5 μg/mL.
2 μg/lane of Recombinant Mouse Endorepellin/Perlecan was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 85-95 kDa.
Endorepellin is an 80 kDa glycoprotein derived from the C-terminal end of the heparan sulfate proteoglycan Perlecan. Human Perlecan is an approximately 850 kDa basement membrane heparan sulfate proteoglycan containing multiple LDLR, EGF-like, Laminin-like, and immunoglobulin-like domains. Mouse Perlecan lacks several of the EGF, Laminin-like and Ig-like domains found in the human protein (1-3). Mouse Endorepellin, also termed Domain V (DV) of Perlecan, consists of three Laminin G domains separated by a single EGF-like domain. Mouse Endorepellin shares 89% amino acid sequence identity with human Endorepellin. Endorepellin has been shown to broadly inhibit angiogenesis, including endothelial cell migration, collagen-induced capillary morphogenesis, and blood vessel growth (4). Endostatin, an inhibitor of Endorepellin, has been shown to bind Endorepellin directly and block its anti-angiogenic activity (4). Endorepellin can be further processed into a 26 kDa fragment, termed LG3, containing the third Laminin G-like domain of Endorepellin. LG3 possesses anti-angiogenic activity of its own and its release is mediated by either Cathepsin L or BMP-1/Tolloid family cleavage (4-7). Endorepellin binds to Integrin alpha 2/ beta 1, preventing the integrin-dependent adhesion of vascular endothelial cells (EC) to fibronectin and collagen I (7, 8). Additionally, Endorepellin binds to VEGF R1 and VEGF R2 on EC (10). Its binding to VEGF R2 and Integrin alpha 2/beta 1 on EC induces the association and down‑regulation of both proteins, resulting in a reduction in EC migration and overall antiangiogenic activity (4, 7-10). Endorepellin has been shown to disrupt tumor vasculature and inhibit tumor growth, invasion and angiogenesis (8, 11), and it has recently been proposed as a potential stroke therapy by helping with brain repair following injury (12).
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