Periostin (PN), also designated osteoblast-specific factor 2 (OSF-2), is a disulfide linked protein originally isolated as a osteoblast-specific factor. Periostin is a secreted protein that binds heparin and functions as a ligand for alpha(V)beta(3) and alpha(V)beta(5) integrins. In preosteoblasts, Periostin acts as a cell adhesion molecule and plays a role in osteoblast recruitment, spreading and attachment. Periostin is mainly detected in lower gastrointestinal tract, aorta, stomach, placenta, uterus and breast tissues but is up-regulated in epithelial ovarian tumors and overexpressed in breast cancer. Expression of Periostin is increased by bone morphogenetic protein (BMP2) and transforming growth factor beta 1(TGF beta 1). Periostin contains a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain, which shows homology with the insect protein fasciclin, and a C-terminal domain.
Samples:
FFPE tissue
Target:
Human Periostin
IHC0356H
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