Description: PL1 is a monoclonal antibody that recognizes a membrane-distal epitope on PSGL-1 and blocks binding of PSGL-1 to immobilzed P-selectin, fluid-phase P-selectin to leukocytes, and neutrophils to P-selectin under both static and a range of shear stress conditions.
BMS164 is suitable for immunohistological stainings on paraffin sections.
BMS164 is suitable for stainings in FACS analysis.
BMS164 is suitable for Western blotting.
BMS164 blocks binding of PSGL-1 to P-selectin and L-selectin.
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.