Syndecan-2, previously known as fibroglycan, is a member of the syndecan family of Type 1 transmembrane proteins carrying heparan sulfate and chondroitin sulfate glycosaminoglycans. The syndecan family consists of four transmembrane proteoglycans divided into two subfamilies (Syndecan -1 , -3 and Syndecan-2 ,- 4) based on their sequence homology. The four syndecans have conserved cytoplasmic domains which enables them to associate with cytoskeletal proteins and signaling molecules. The cytoplasmic tail of Syndecan-2 has both serine and tyrosine phosphorylation sites. Non-covalent homodimerization of Syndecan-2 is dependent on the transmembrane domain. Syndecan-2 is expressed in endothelial, mesenchymal, carcinoma cells, and is the predominant syndecan expressed during embryonic development. It functions as a co-receptor for enzymes, growth factors, and cytokines, and contributes to the formation of cytokine gradients through extracellular shedding. Syndecan-2 interacts with high affinity receptors and integrins to modulate intracellular signaling. Syndecan is also involved in matrix assembly and remodeling. It controls laminin and fibronectin matrix assembly into a fibrillar matrix.