Anti-Mouse/Rat CD90.1 (Thy-1.1) (Clone OX-7) - Purified <i>in vivo </i>GOLD™ Functional Grade (C851-GRP)

CD90/Thy-1 (murine CD90.1/Thy-1.1) is a cell surface glycoprotein that was the first protein of the immunoglobulin superfamily to be discovered5. The 25 kDa core protein is N-glycosylated at three sites, leading to isoforms with a range of molecular masses (25-37 kDa). CD90 is composed of a single V-like immunoglobulin domain anchored by a disulfide bond between Cys 28 and Cys 104. Despite its lack of an intracellular domain, CD90 is located in the outer leaflet of lipid rafts at the cell membrane, allowing signaling functions by cis- and trans-interactions with a variety of proteins, including G inhibitory proteins, the Src family kinase (SFK) members src and c-fyn, and tubulin. CD90 has been found to play a role in numerous cellular activities, such as cell adhesion, apoptosis, metastasis, inflammation, and fibrosis. In mouse strains expressing CD90.1, it is expressed on early-stage hematopoietic cells in bone marrow, thymocytes, and circulating mature T cells. The OX-7 antibody has been reported to induce leukocyte activation, glomerular nephritis, apoptosis in glomerular mesangial cells, and vascular permeability. CD90 can be used as a marker for a variety of stem cells and for the axonal processes of mature neurons. Diseases associated with CD90 dysfunction include nasopharyngeal carcinoma and thymoma.