Anti-Human CD162 (PSGL-1) PerCP-eFluor® 710

Description: This FLEG monoclonal antibody recognizes human CD162, which is also known as P-selectin glyocoprotein ligand-1 (PSGL-1). This 120-kDa protein exists as a homodimer on the surface of monocytes, neutrophils, granulocytes, peripheral T cells, some B cells, and a subset of CD34+ hematopoietic progenitor cells (HPCs) in the bone marrow. CD162 binds CD62P (P-selectin), CD62E (E-selectin), and CD62L (L-selectin) to mediate leukocyte interactions with each other as well as with activated platelets and endothelium. Thus, CD162 plays a critical role in leukocyte adhesion and rolling. Furthermore, the binding of CD162 to P-selectin on HPCs has been demonstrated to inhibit hematopoiesis. Studies have also demonstrated CD162 as the receptor for enterovirus 71.

References: Nishimura Y, Shimojima M, Tano Y, Miyamura T, Wakita T, Shimizu H. Nat Med. Human P-selectin glycoprotein ligand-1 is a functional receptor for enterovirus 71. 2009 Jul;15(7):794-7.

Davenpeck KL, Brummet ME, Hudson SA, Mayer RJ, Bochner BS. Activation of human leukocytes reduces surface P-selectin glycoprotein ligand-1 (PSGL-1, CD162) and adhesion to P-selectin in vitro. J Immunol. 2000 Sep 1;165(5):2764-72.

Lévesque JP, Zannettino AC, Pudney M, Niutta S, Haylock DN, Snapp KR, Kansas GS, Berndt MC, Simmons PJ. PSGL-1-mediated adhesion of human hematopoietic progenitors to P-selectin results in suppression of hematopoiesis. Immunity. 1999 Sep;11(3):369-78.