
These antibodies are validated on HuProtâ„¢ Human Protein Microarrays containing over 21,000 full-length human proteins, including the specific target of interest. LEARN MORE
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Analysis of Protein Array containing more than 19,000 full-length human proteins using Periostin (POSTN)-Monospecific Mouse Monoclonal Antibody (POSTN/3504). Z- and S- Score: The Z-score represents the strength of a signal that a monoclonal antibody (MAb) (in combination with a fluorescently-tagged anti-IgG secondary antibody) produces when binding to a particular protein on the HuProtTM array. Z-scores are described in units of standard deviations (SD's) above the mean value of all signals generated on that array. If targets on HuProtTM are arranged in descending order of the Z-score, the S-score is the difference (also in units of SD's) between the Z-score. S-score therefore represents the relative target specificity of a MAb to its intended target. A MAb is considered to specific to its intended target, if the MAb has an S-score of at least 2.5. For example, if a MAb binds to protein X with a Z-score of 43 and to protein Y with a Z-score of 14, then the S-score for the binding of that MAb to protein X is equal to 29.

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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 Î �VÎ �3 and Î �VÎ �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 Î � 1 (TGF Î � 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.
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