E-Selectin/CD62E (mouse, recombinant)

E-Selectin, also known as CD62E, is a glycoprotein encoded by the SELE gene in humans that has roles as a cellular adhesion molecule.^1,2 It is composed of an N-terminal C-type lectin-like domain, which recognizes carbohydrate ligands, an EGF-like domain, multiple short consensus repeats (SCRs), a transmembrane region, and a C-terminal cytoplasmic tail.^2,3 E-Selectin is constitutively expressed in bone marrow endothelial cells, where it has a role in maintaining the stem cell niche, and its expression is induced in vascular endothelial cells by inflammatory stimuli, such as TNF-α, IL-1β, or LPS.^2,1 It also exists as a soluble form that is shed from the cell surface via proteolytic cleavage.⁴ E-selectin recognizes and binds to a variety of glycoproteins and glycolipids expressed by leukocytes, hematopoietic cells, or cancer cells, including L-selectin, sialyl Lewis X (sLe^X), and E-selectin ligand-1 (ESL-1), as well as CD44 and CD43E.⁵ Binding of E-selectin to its ligands facilitates the tethering and rolling of infiltrating cells on endothelial cells and promotes their extravasation into inflamed tissues.² Sele^-/- mice exhibit reduced infiltration of metastatic cancer cells to the lung, and serum soluble E-selectin levels are elevated in patients with a variety of conditions, including atherosclerosis, type 1- and type 2 diabetes, sepsis, and multiple sclerosis.^6,7,8,9 Cayman's E-Selectin/CD62E Extracellular Domain (mouse, recombinant) protein can be used for cell-based assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of E-selectin (amino acids 29-564) fused to human IgG1 Fc at its C-terminus, consists of 777 amino acids, has a calculated molecular weight of 85.5 kDa, and a predicted N-terminus of Trp29 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 101 kDa due to glycosylation.

WARNING This product is not for human or veterinary use.

1. Silva, M., Videira, P.A., and Sackstein, R. E-selectin ligands in the human mononuclear phagocyte system: Implications for infection, inflammation, and immunotherapy. Front. Immunol. 8, 1878 (2018).

2. Tvaroška, I., Selvaraj, C., and Koča, J. Selectins-The two Dr. Jekyll and M_r. Hyde faces of adhesion molecules-A review. Molecules 25(12), 2835 (2020).

3. Aleisa, F.A., Sakashita, K., Lee, J.M., et al. Functional binding of E-selectin to its ligands is enhanced by structural features beyond its lectin domain. The Journal of Biological Chemisty 295(11), 3719-3733 (2020).

4. DeLisser, H.M., Christofidou-Solomidou, M., Sun, J., et al. Loss of endothelial surface expression of E-selectin in a patient with recurrent infections. Blood 94(3), 884-894 (1999).

5. Barthel, S.R., Gavino, J.D., Descheny, L., et al. Targeting selectins and selectin ligands in inflammation and cancer. Expert Opin. Ther. Targets 11(11), 1473-1491 (2007).

6. Hiratsuka, S., Goel, S., Kamoun, W.S., et al. Endothelial focal adhesion kinase mediates cancer cell homing to discrete regions of the lungs via E-selectin up-regulation. Proc. Natl. Acad. Sci. USA 108(9), 3725-3730 (2011).

7. Paterson, A.D., Lopes-Virella, M.F., Waggott, D., et al. Genome-wide association identifies the ABO blood group as a major locus associated with serum levels of soluble E-selectin. Arterioscler. Thromb. Vasc. Biol. 29(11), 1958-1967 (2009).

8. Cummings, C.J., Sessler, C.N., Beall, L.D., et al. Soluble E-selectin levels in sepsis and critical illness. Correlation with infection and hemodynamic dysfunction. Am. J. Respir. Crit. Care Med. 156(2 Pt 1), 431-437 (1997).

9. Tsukada, N., Miyagi, K., Matsuda, M., et al. Soluble E-selectin in the serum and cerebrospinal fluid of patients with multiple sclerosis and human T-lymphotropic virus type 1-associated myelopathy. Neurology 45(10), 1914-1918 (1995).