P-Selectin (SELP)
(Selectin P (Granule Membrane Protein 140kDa, Antigen CD62) (SELP))
Type de proteíne
Recombinant
Attributs du protein
AA 42-771
Origine
Humain
Source
HEK-293 Cells
Purification/Conjugué
Cette P-Selectin protéine est marqué à la His tag.
Séquence
AA 42-771
Attributs du produit
This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 81.8 kDa. The protein migrates as 110-125 kD under reducing (R) condition (SDS-PAGE) due to glycosylation.
SELP
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
P-selectin (SELP) is also known as CD62 antigen-like family member P, granule membrane protein 140 (GMP-140), leukocyte-endothelial cell adhesion molecule 3 (LECAM3) and platelet activation dependent granule-external membrane protein (PADGEM). SELP functions as a cell adhesion molecule (CAM) on the surfaces of activated endothelial cells, which line the inner surface of blood vessels, and activated platelets. In unactivated endothelial cells, it is stored in granules called Weibel-Palade bodies. In unactivated platelets SELP is stored in α-granules. The primary ligand for SELP is P-selectin glycoprotein ligand-1 (PSGL-1) which is expressed on almost all leukocytes, although P-selectin also binds to heparan sulfate and fucoidan. Furthermore, SELP has a functional role in metastasis of tumor similar to E-selectin, which can help cancer cells invade into bloodstream for metastasis and provided locally with multiple growth factors respectively.