Mouse Periostin/OSF‑2 Isoform 2 Biotinylated Antibody

Mouse Periostin, also known as OSF-2 (osteoblast-specific factor 2) is a 170 kDa, secreted, homodimeric protein that belongs to the periostin family of the FAS1 superfamily of molecules (1‑4). It is a TGF-beta inducible molecule that serves as both an adhesion molecule and tumor suppressor (2, 5, 6, 7). It is synthesized as a 838 amino acid (aa) precursor that contains a 23 aa signal sequence and an 815 aa mature region (2, 8). It is unknown if the molecule has any significant glycosylation (2). Based on human OSF-2, the homodimer is not disulfide-linked (3). The molecule consists of two distinct regions. The N-terminus contains an 55 aa EMI domain, while the C-terminus contains four, 130 aa fasciculin type 1 (or FAS1) domains. The EMI domain is cysteine-rich and shows a highly basic alpha -helix (9). Each FAS1 repeat exhibits a novel 7-stranded beta -wedge with a multiple alpha -helix fold (1, 8). Multiple alternate splice forms are known to exist C-terminal (aa 672‑812) to the four-fold FAS1 repeats. These mature molecules are 760, 761, 787 and 788 aa in length and show block deletions of 54 aa, 27 aa and/or 28 aa (10). The significance of the alternate splice forms is not clear. They do, however, appear to be temporally regulated (6). OSF-2 is known to bind to alpha _v beta ₃ and alpha _v beta ₅ integrins (3). It is synthesized by smooth muscle cells, fibroblasts and osteoblasts (2, 5, 7). Mature mouse OSF-2 shares 98%, 92% and 91% aa identity with rat, canine and human OSF‑2, respectively.