ULBP1 Human
Description
Product Specs
Product Science Overview
ULBP1 was initially identified due to its ability to bind to the human cytomegalovirus (HCMV) glycoprotein UL16 . Unlike traditional MHC class I proteins, ULBPs are glycosylphosphatidylinositol (GPI)-linked, lack an α3 domain, and do not associate with β2-microglobulin . The gene for ULBP1 is located in a cluster of ten related genes, six of which encode potentially functional glycoproteins .
ULBP1 functions as a ligand for the NKG2D receptor, an activating receptor found on NK cells, CD8+ αβ T cells, and γδ T cells . The binding of ULBP1 to NKG2D leads to the activation of several signal transduction pathways, including those of JAK2, STAT5, ERK, and PI3K kinase/Akt . This interaction is crucial for mediating natural killer cell cytotoxicity and stimulating anti-tumor immune responses .
In cytomegalovirus-infected cells, ULBP1 binds to the UL16 glycoprotein, preventing it from activating the immune system . This mechanism allows the virus to evade immune detection, highlighting the complex interplay between pathogens and the host immune system.
ULBP1 is frequently expressed by malignant transformed cells and stimulates anti-tumor immune responses . Its expression is associated with various diseases, including Peroxisome Biogenesis Disorder 1A and Myelodysplastic Syndrome . The ability of ULBP1 to activate NK cells and T-cells makes it a potential target for cancer immunotherapy.
Recombinant ULBP1 is produced using recombinant DNA technology, which involves inserting the ULBP1 gene into a suitable expression system to produce the protein in large quantities. This recombinant protein can be used in various research and clinical applications, including studying the immune response, developing cancer therapies, and understanding the mechanisms of immune evasion by viruses.
