epitope corresponding to amino acids 221-380 mapping within an internal region of Osteoadherin of human origin
recommended for detection of Osteoadherin of mouse, rat and human origin by WB, IP, IF and ELISA; also reactive with additional species, including bovine and porcine
Osteoadherin Background Information Osteoadherin (OSAD) is a bone proteoglycan containing keratan sulfate that belongs to the small leucine-rich proteoglycan (SLRP) family. Osteoadherin promotes Integrin åv∫3-mediated cell binding. The central region of Osteoadherin consists of eleven B-type, leucine-rich repeats ranging in length from 20 to 30 residues. The full, primary sequence of Osteoadherin contains four putative sites for tyrosine sulfation, three of which are at the N-terminal end of the molecule, six assumed sites for N-linked glycosylation, and a large and very acidic C-terminal domain, which is unique to Osteoadherin. Expression of Osteoadherin is limited to extracellular space and the extracellular matrix, as it is a secreted protein.
