Human ULBP‑1 Biotinylated Antibody

ULBP-1 is a member of a family of cell-surface proteins that function as ligands for human NKG2D. ULBP-1 has also been described under the names RaeT1I (retinoic acid early transcript), ALCAN-beta, and NKG2DL1. The name ULBP-1 derives from the original identification of three proteins, ULBP-1, -2, and -3, as ligands for the human cytomegalovirus glycoprotein UL16; they were designated UL16 binding proteins (ULBP). The gene for ULBP-1 resides in a cluster of ten related genes, six of which encode potentially functional glycoproteins. Amino acid sequence identity within this family ranges from 30 - 95%. These proteins are distantly related to MHC class I proteins, but they possess only the alpha 1 and alpha 2 Ig-like domains, and they have no capacity to bind peptide or interact with beta 2-microglobulin. They are anchored to the membrane via a GPI-linkage. ULBP-1 and several other family members are known to bind to human NKG2D, an activating receptor expressed on NK cells, NKT cells, gamma delta T cells, and CD8⁺ alpha beta T cells. Engagement of NKG2D results in the activation of cytolytic activity and/or cytokine production by these effector cells. ULBP-1 is expressed on some tumor cells and has been implicated in tumor surveillance (1 - 8).