Human SELP / P Selectin (His Tag) recombinant protein

Human SELP / P Selectin (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

P selectin (SELP) is a 140kDa protein that is stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. SELP mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1. P selectin is a cell adhesion molecule on the surface of activated endothelial cells. Cellular adhesion molecules are a large family of proteins that attach the cytoskeleton and intracellular signaling cascades with the extracellular environment. SELP is a calcium-dependent receptor for myeloid cells that binds to sialylated forms of Lewis blood group carbohydrate antigens on neutrophils and monocytes. This protein redistributes to the plasma membrane during platelet activation and degranulation and mediates the interacton of activated endothelial cells or platelets with leukocytes.

P-selectin

GRMP; PADGEM; LEUKOCYTE-ENDOTHELIAL CELL ADHESION MOLECULE 3; LECAM3; CD62 ANTIGEN-LIKE FAMILY MEMBER P; PSEL; P-SELECTIN; CD62; PLATELET ACTIVATION DEPENDENT GRANULE-EXTERNAL MEMBRANE PROTEIN; GRANULE MEMBRANE PROTEIN 140; CD62P; GMP140; RP1-86F14.2; GMP-140

P16109

SELP; GMRP; GRMP

Human Cells

A DNA sequence encoding the human SELP (AAN06828.1) extracellular domain (Met 1-Ala 771) was fused with a polyhistidine tag at the C-terminus.

Human

The secreted recombinant human SELP consists of 741 amino acids and has a predicted molecular mass of 81.3 kDa. The apparent molecular mass of the protein is approximately 120 kDa in SDS-PAGE under reducing conditions due to glycosylation.

> 90 % as determined by SDS-PAGE