FluoBolt™- ASPORIN

Asporin is an extracellular matrix protein consisting of 380 amino acids that is secreted as a dimer, acts as a direct binding partner for TGF-β1 and, like decorin and biglycan, belongs to the Small Leucine-Rich Protein (SLRP) class I family. In addition to their homology at the genetic and molecular level, these are characterised in particular by a sequence of leucine repeats (leucine rich repeats, LRRs) flanked by cysteine disulphide bridges. In contrast to other members of the SLRP class I family, asporin has no glycosaminoglycan binding site, but a number of unique aspartic acid repeats at the N-terminus. The main biological function of this protein is probably the regulation of TGF-β1 activity, to which it binds directly.