Invitrogen™ Mouse Periostin (Postn) ELISA Kit

Description

The Mouse Periostin (Postn) ELISA quantitates Ms Periostin in mouse serum, plasma, or cell culture medium. The assay will exclusively recognize both natural and recombinant Ms Periostin. Principle of the method The Mouse Periostin solid-phase sandwich ELISA (enzyme-linked immunosorbent assay) is designed to measure the amount of the target bound between a matched antibody pair. A target-specific antibody has been pre-coated in the wells of the supplied microplate. Samples, standards, or controls are then added into these wells and bind to the immobilized (capture) antibody. The sandwich is formed by the addition of the second (detector) antibody, a substrate solution is added that reacts with the enzyme-antibody-target complex to produce measurable signal. The intensity of this signal is directly proportional to the concentration of target present in the original specimen. Rigorous validation Each manufactured lot of this ELISA kit is quality tested for criteria such as sensitivity, specificity, precision, and lot-to-lot consistency. See manual for more information on validation.

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.