Mouse Periostin/OSF-2 Isoform 2 Biotinylated Antibody
Mouse Periostin/OSF-2 Isoform 2 Biotinylated Antibody Summary
Accession # Q62009
Mouse Periostin/OSF-2 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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.
- Clout, N.J. and D. Tisi (2003) Structure 11:197.
- Horiuchi, K. et al. (1999) J. Bone Miner. Res. 14:1239.
- Gillan, L. et al. (2002) Cancer Res. 62:5358.
- Litvin, J. et al. (2005) Anat. Rec. A Discov. Mol. Cell. Evol. Biol. 287A:1205.
- Lindner, V. et al. (2005) Arterioscler. Thromb. Vasc. Biol. 25:77.
- Kruzynska-Frejtag, A. et al. (2004) Dev. Dyn. 229:857.
- Yoshioka, N. et al. (2002) Exp. Cell Res. 279:91.
- Takeshita, S. et al. (1993) Biochem. J. 294:271.
- Callebaut, I. et al. (2003) Biochem. Biophys. Res. Commun. 300:619.
- Swiss-Prot Accession # Q62009.
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