Detects mouse Periostin/OSF‑2 in direct ELISAs and Western blots. In direct ELISAs, approximately 50% cross-reactivity with recombinant rat Periostin/OSF-2 and less than 20% cross-reactivity with recombinant human Periostin/OSF-2 is observed.
Polyclonal Goat IgG
S. frugiperda insect ovarian cell line Sf 21-derived recombinant mouse Periostin/OSF‑2 Asn24-Gln811 Accession # Q62009
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
<0.10 EU per 1 μg of the antibody by the LAL method.
Measured by its ability to neutralize Periostin/OSF‑2-mediated adhesion of the ATDC5 mouse chondrogenic cell line. The Neutralization Dose (ND50) is typically 1-5 µg/mL in the presence of 5 µg/mL Recombinant Mouse Periostin/OSF‑2.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Cell Adhesion Mediated by Periostin/OSF‑2 and Neutralization by Mouse Periostin/ OSF‑2 Antibody.
Recombinant Mouse Periostin/OSF‑2 (Catalog # 2955‑F2), immobilized onto a microplate, supports the adhesion of the ATDC5 mouse chondrogenic cell line in a dose-dependent manner (orange line). Adhesion elicited by Recombinant Mouse Periostin/OSF‑2 (5 µg/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Mouse Periostin/ OSF‑2 Isoform 2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2955). The ND50 is typically 1-5 µg/mL.
Periostin/OSF‑2 in Rat Mesenchymal Stem Cells.
Periostin/OSF‑2 was detected in immersion fixed rat mesenchymal stem cells differentiated to osteoblasts using Goat Anti-Mouse Periostin/OSF‑2 Isoform 2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2955) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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.
R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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