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.|
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.
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.
Showing Results 1 - 4 of 4
Filter your results:
The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.
The document you requested is not available online. Please enter the Catalog Number and Lot Number below to have a document emailed to you at the address provided