Weller A, Isenmann S, Vestweber D. Cloning of the mouse endothelial selectins. Expression of both E- and P-selectin is inducible by tumor necrosis factor alpha. J Biol Chem. 1992 Jul 25;267(21):15176-83.
Mouse P-Selectin, also known as GMP-140, LECAM-3, PADGEM, or CD62P, is a member of the Selectin family of cell surface glycoproteins. It is expressed by activated platelets and endothelial cells. The cDNA for Mouse P-Selectin encodes a 768 amino acid (aa) type I transmembrane protein. This protein comprises a 41 aa signal peptide, a 668 aa extracellular domain, a transmembrane domain, and a short (35 aa) cytoplasmic domain.
The extracellular domain of Mouse P-Selectin features an NH2-terminal C-type lectin domain and an EGF-like domain, succeeded by a series of complement factor A repeat homology domains. There is approximately 73% sequence homology between the extracellular domains of human and mouse P-Selectin.
P-Selectin is crucial for the adhesion of leukocytes and neutrophils to the endothelium. In conjunction with L-Selectin, it mediates the initial interaction between circulating leukocytes and endothelial cells, resulting in a characteristic 'rolling' phenomenon of leukocytes along the endothelium. Following this initial interaction, a stronger bond forms, involving E-Selectin, and subsequently ICAM-1 and VCAM-1. This sequence of events ultimately facilitates the extravasation of white blood cells through the blood vessel wall and into the surrounding tissue matrix.
Measured by the ability of the immobilized protein to support the adhesion of U937 human histiocytic lymphoma cells. The EC50 for this effect is less than 150ng/ml.
1μg (R: reducing condition, N: non-reducing condition).
The purity of P-Selectin/CD62P Fc Chimera Protein, Mouse is more than 95% determined by SEC-HPLC.