Versican G1 Domain (human, recombinant)

Versican is a secreted proteoglycan and member of the hyalectan family of proteoglycans. It is composed of an N-terminal G1 domain containing a secretory signal peptide, an immunoglobulin-like motif, and two proteoglycan tandem repeats followed by two glycosaminoglycan (GAG) binding regions, alpha-GAG and beta-GAG, and a C-terminal G3 domain containing two EGF-like repeats, a carbohydrate recognition domain, and a complement-binding protein-like motif. Alternative splicing of versican produces four isoforms (V0-V3) that are expressed in a tissue- and development-specific manner and differ based on the GAG-binding region, containing either alpha- and beta-GAG (V0), beta-GAG only (V1), alpha-GAG only (V2), or no GAG-binding regions (V3). Versican is expressed in a variety of tissues, including connective tissue, cartilage, neural tissues, and vessels. It interacts with a variety of ligands, including hyaluronan at the G1 domain and fibulin-1 and -2 at the G3 domain. It is involved in tissue and organ development, including cardiac development, and is a structural macromolecule of the extracellular matrix (ECM) in various tissues in adulthood. Versican levels are increased in tumor tissue or peritumoral stromal cells in a wide range of cancers and are associated with poor outcomes. Mutations in VCAN, the gene encoding versican, are the cause of Wagner syndrome, a hereditary vitreoretinopathy characterized by early-onset syneresis and accelerated liquefaction of the vitreous. Cayman's Versican G1 Domain (human, recombinant) protein can be used for binding assay, ELISA, and Western blot (WB) applications.