Cayman P-Selectin Glycoprotein Ligand-1/CD162 Extracellular Domain (human, recombinant; His- and Fc-tagged)

P-selectin glycoprotein ligand 1 (PSGL-1), also known as CD162, is a cell surface glycoprotein encoded by SELPLG in humans that binds to P-, E-, and L-selectins to mediate the rolling and tethering of immune cells on endothelium for migration into sites of inflammation.^1,2,3 It is expressed as a homodimer on myeloid and lymphoid cells, including platelets, and is composed of an extracellular domain, which contains branching sites for glycosylation and sulfation, a transmembrane domain, and a cytoplasmic domain.² PSGL-1 selectin binding requires post-translational modifications, including sulfation and glycosylation, and these modifications are constitutively present on PSGL-1 in innate immune cells and differentiated T cells.⁴ Ectopic expression of PSGL-1 in CD4⁺ T cells inhibits processing and incorporation of the HIV-1 envelope glycoprotein, disrupting attachment of viral progeny to target cells but does not inhibit HIV-1 infection.⁵ It also inhibits the incorporation of severe acute respiratory syndrome coronavirus (SARS-CoV) and SARS-CoV-2 spike glycoproteins into pseudovirions and blocks pseudovirus attachment and infection of target cells.³ Cayman’s PSGL-1 (human, recombinant; His- and Fc-tagged) protein is a disulfide-linked homodimer. The reduced monomer, composed of PSGL-1 (amino acids 18-295) fused to His-tagged human IgG1 Fc at its C-terminus, consists of 526 amino acids, has a calculated molecular weight of 57.1 kDa, and a predicted N-terminus of Leu18 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 110-120 kDa by SDS-PAGE under reducing conditions.

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