Rhesus SELP / P Selectin (His Tag) recombinant protein

Rhesus 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.

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

F7H811

Human Cells

A DNA sequence encoding the rhesus SELP (XP_001094728.1) (Met1-Ala771) was expressed with a polyhistidine tag at the C-terminus.

Rhesus

The recombinant rhesus SELP comprises 741 amino acids and has a calculated molecular mass of 81.2 KDa.

> 85 % as determined by SDS-PAGE