Human sP-selectin Platinum ELISA

Description: The human sP-selectin ELISA is an enzyme-linked immunosorbent assay for the quantitative detection of human sP-selectin.

P-selectin belongs to the selectin family of adhesion molecules. P-selectin acts as a receptor that supports binding of leukocytes to activated platelets and endothelium.

P-selectin is a 140 kDa protein that is highly glycosylated. The cDNA derived amino acid sequence predicts a molecule with a series of cysteine-rich domains.

P-selectin is located in membranes of a granules in unstimulated platelets and redistributed to the cell surface upon platelet activation. P-selectin is also present in endothelial cells in membranes of Weibel-Palade bodies and megakaryocytes.

The physiologic role of P-selectin might be the mediation of initial leukocyte adhesion to activated endothelium during acute inflammation. It may work in concert with E-selectin to direct early, regionally specific adherence of neutrophils and monocytes at sites of acute inflammation. A soluble form of P-selectin found in serum and plasma has been described which might represent a proteolytic fragment or more likely a soluble splice variant lacking the transmembrane domain.

Excessive accumulation of neutrophils on the endothelial surface accompanied by high exposure of P-selectin has been implicated in a number of inflammatory disorders, including adult respiratory distress syndrome, acute lung injury, ischemia-reperfusion injury, Gram-negative septic shock, thrombotic diseases and rheumatoid arthritis. Malignant cells were shown to express receptors for P-selectin suggesting an important role for P-selectin in tumor formation and metastasis.

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