Recombinant Human Endoglycan/PODXL2 Protein, CF

Human Endoglycan, also called Podocalyxin-like 2 protein (PODXL2), is an extensively O-glycosylated type I transmembrane protein in the CD34 family of sialomucins (1, 2). Mature human Endoglycan consists of a 468 amino acid (aa) extracellular domain that contains an N-terminal acidic domain characterized by several polyglutamate tracts, a mucin domain, and a membrane-proximal globular domain. Within the extracellular domain, human Endoglycan shares 74% amino acid identity with both mouse and rat Endoglycan. Alternative splicing may generate a short isoform that lacks aa 336-411. Following the extracellular domain is a single transmembrane spanning helix and a charged cytoplasmic tail that contains a C-terminal PDZ-domain binding motif (1, 3). The cytoplasmic domain of Endoglycan has been shown to bind to Na⁺/H⁺ exchanger regulatory factor-1 (NHERF-1), which acts as a scaffolding protein that links membrane proteins to the actin cytoskeleton (4). Human Endoglycan exists as a disulfide-linked homodimer that is expressed in vascular endothelium, smooth muscle, hematopoietic precursor populations and leukocyte subpopulations (1, 5). Endoglycan functions through its interactions with selectins and is involved in leukocyte-endothelial cell adhesion although depending on cellular context and post-translational modifications, Endoglycan may also demonstrate anti-adhesive properties (3, 5).