Anti-PSGL-1/Selplg Antibody Picoband® Fluoro488 Conjugated

Selectin P ligand, also known as SELPLG or CD162 (cluster of differentiation 162), is a human gene. It is mapped to 12q16. This gene encodes a glycoprotein that functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. As such, this protein plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. This protein requires two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans, for its high-affinity binding activity. Aberrant expression of this gene and polymorphisms in this gene are associated with defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.

A SLe (x) -type proteoglycan, which through high affinity, calcium-dependent interactions with E- and P-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture.

1. Fuhlbrigge, R. C., Kieffer, J. D., Armerding, D., Kupper, T. S. Cutaneous lymphocyte antigen is a specialized form of PSGL-1 expressed on skin-homing T cells. Nature 389: 978-981, 1997. 2. Herron, M. J., Nelson, C. M., Larson, J., Snapp, K. R., Kansas, G. S., Goodman, J. L. Intracellular parasitism by the human granulocytic ehrlichiosis bacterium through the P-selectin ligand, PSGL-1. Science 288: 1653-1656, 2000. 3. Hidalgo, A., Weiss, L. A., Frenette, P. S. Functional selectin ligands mediating human CD34+ cell interactions with bone marrow endothelium are enhanced postnatally. J. Clin. Invest. 110: 559-569, 2002.