LRG1, also known as leucine-rich alpha-2-glycoprotein, is a member of leucine-rich repeat (LRR) family. It is neutrophilic expressed during granulocyte differentiation. It has been shown to be involved in protein-protein interaction, signal transduction, and cell adhesion and development. It binds directly to the TGF-beta accessory receptor endoglin, which, in the presence of TGF-beta1, results in promotion of the pro-angiogenic Smad1/5/8 signaling pathway. It promotes proliferation and inhibits apoptosis in colorectal cancer cells via RUNX1 activation. It is a key physiological regulator of dendrite complexity of hippocampal pyramidal neurons. It physically interacts with TrkB and attenuates BDNF signaling. Recombinant human LRG1, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques.
Poids moléculaire
35.4kDa (321aa) 40-57kDa (SDS-PAGE under reducing conditions)