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. Author manuscript; available in PMC: 2012 Jul 10.
Published in final edited form as: J Cell Biochem. 2007 Jun 1;101(3):695–711. doi: 10.1002/jcb.21224

Fig. 8.

Fig. 8

Validation of periostin virus. A: Schematic of Periostin showing the fasciclin domains (Fas1–4), signal sequence (S.S.), cysteine rich domain (Cys), heparin binding domain (green ovals), putative glycosylation site, and stop codon (red asterisk). Below the periostin schematic is a representation of the two adenoviruses (LacZ and mouse periostin) generated for experimentation (HA-hemagluttinin epitope tag fused at the carboxyl-terminus of periostin, ITR-Internal terminal repeat, CMV-cytomegalovirus promoter, red asterisk-stop codon). B: Western blot for periostin (OX) or LacZ adenoviral infected HEK293 cells under reducing (with β-mercaptoethanol: β-ME) or non-reducing conditions (without β-ME). Under non-reducing conditions, periostin migrates as both a monomer and a dimer and is capable of being secreted into the supernatant. Periostin is also seen still attached to the cells, suggesting its ability to be matricellular.