E-Selectin/CD62E (mouse, recombinant)

Territorial Availability: Available through Bertin Technologies only in France

• Correlated keywords
  • CD6 2E glyco protein trans membrane cyto plasmic TNF? IL1? sLe X ESL1 CD 44 CD 43E Trp 29 SDSPAGE HEK 293 Ig G1 ELAM 1 LECAM 2 SELE ESEL CD 62
• Product Overview:
  E-Selectin, also known as CD62E, is a glycoprotein encoded by the SELE gene in humans that has roles as a cellular adhesion molecule.{60878,60879} 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.{60879,60880} 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-?, IL-1?, or LPS.{60879,60878} It also exists as a soluble form that is shed from the cell surface via proteolytic cleavage.{60881} 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 (sLeX), and E-selectin ligand-1 (ESL-1), as well as CD44 and CD43E.{60882} 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.{60879} 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.{60883,60884,60885,60886} 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.