PODXL2 polyclonal antibody

Endoglycan, also known as podocalyxin-like 2, exists as a disulfide-dependent homodimer and belongs to the CD34 family of proteins. It is a proteoglycan modified with chondroitin sulfate chains and (with appropriate post-translational modifications) functions as an L-selectin ligand, interacting via sulfation on two tyrosine residues. Endoglycan contains a membrane proximal globular domain, a single pass transmembrane domain, a mucin-like domain and a highly acidic N-terminal with O-linked sLex structures. It is widely expressed with distribution including endothelial cells, hematopoietic precursors and leukocyte subpopulations. Endoglycan is similar to PSGL-1 in that it also exhibits catch-slip transitional bonds. These bonds help to mediate the rolling and tethering of circulating leukocytes on vascular surfaces, typically during immune surveillance and inflammation. The ligand activity of Endoglycan is dependent on sialylation and fucosylation and may mediate adhesion events.