|Calculated MW||43201 Da|
|Other Names||P-selectin glycoprotein ligand 1, PSGL-1, Selectin P ligand, CD162, SELPLG|
|Target/Specificity||A synthetic peptide corresponding to residues in the extracellular region of PSGL-1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||P-Selectin Glycoprotein Ligand-1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture.|
|Cellular Location||Membrane; Single-pass type I membrane protein|
|Tissue Location||Expressed on neutrophils, monocytes and most lymphocytes|
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Provided below are standard protocols that you may find useful for product applications.
P-selectin glycoprotein ligand 1 (PSGL-1) is a mucin-like glycoprotein expressed on the surface of myeloid cells and serves as the high affinity counterreceptor for P-selectin. The PSGL-1-P-selectin interaction is calcium dependent and requires presentation of sialyl-Lewisx (sLex)-type structures on the O-linked glycans of PSGL-1. It is believed that a sulfotyrosine-containing segment of PSGL-1, in conjunction with sLex presented on O-linked glycans, constitutes the high affinity P-selectin-binding site (1). Studies have suggested that PSGL-1 needs to be tyrosine-sulfated, in addition to glycosylated with sLe(X), to successfully interact with P-selectin. the addition of tyrosine sulfation to glycosylated peptides (SGP3) creates a super ligand for P-selectin that supports slower rolling adhesion at all shear rates and supports rolling adhesion at much higher shear rates. Tyrosine sulfation has no similar effect on PSGL-1 rolling on E-selectin. Such functional distinctions in rolling dynamics are uniquely realized with a cell-free system, which permits precise, unambiguous identification of the functional activity of adhesive ligands (2).
1. Sako D, et al. Cell 83(2):323-31, 1995
2. Rodgers SD, Biophys J 81(4):2001-9, 2001
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