Anti-Human CD105 Antibody Pair

Product Description: Endoglin (ENG), also known as CD105, is a type I membrane glycoprotein primarily associated with human vascular endothelium. It is part of the TGF-beta receptor complex and plays a crucial role in angiogenesis, which is essential for tumor growth, survival, and metastasis of cancer cells. Structurally, endoglin consists of a homodimer of 180 kDA stabilized by intermolecular disulfide bonds, with a large extracellular domain, a hydrophobic transmembrane domain, and a short cytoplasmic tail. Functionally, it acts as an auxiliary receptor for the TGF-beta receptor complex, modulating responses to TGF-beta1, TGF-beta3, activin-A, BMP-2, BMP-7, and BMP-9, and is involved in cytoskeletal organization, affecting cell morphology and migration. Mutations in the ENG gene are associated with hereditary hemorrhagic telangiectasia type 1 (HHT1), a disorder characterized by vascular malformations and bleeding. The protein's expression is regulated during heart development, and experimental mice lacking the endoglin gene die due to cardiovascular abnormalities. Protein Function: Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis (PubMed:21737454, PubMed:23300529). Required for normal structure and integrity of adult vasculature (PubMed:7894484). Regulates the migration of vascular endothelial cells (PubMed:17540773). Required for normal extraembryonic angiogenesis and for embryonic heart development (By similarity). May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (By similarity). May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors (PubMed:1692830). Acts as a TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors (PubMed:21737454, PubMed:22347366, PubMed:23300529, PubMed:8370410). Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3 (PubMed:21737454, PubMed:22347366, PubMed:23300529) [The Uniprot Consortium]