Recombinant Human Spinesin Protein, CF

Spinesin, encoded by the TMPRSS5 gene, is a member of type II transmembrane serine proteases (TTSPs) (1). Human Spinesin contains the following structural domains: a short N-terminal cytoplasmic tail (amino acid residues 1-49), a transmembrane domain (residues 50-70), a stem region and a serine protease domain (residues 71-457) (2). The domain structure of Spinesin is common to other TTSPs, many of which have additional domains. The stem region of Spinesin contains a scavenger receptor-like domain. The ectodomain of human Spinesin (residues 71-457) was expressed and purified as a single chain pro-enzyme. The deduced amino acid sequence contains a Leu instead of a Phe residue at position 369; the former is identical to the mouse protein (3, 4). The pro-enzyme can be activated and the resulting enzyme activity can be measured as described in the Activity Assay Protocol.