CD158f Mouse anti-Human, APC, Clone: UP-R1, eBioscience, Mouse Monoclonal Antibody, Each

Details

This UP-R1 monoclonal antibody recognizes human CD158f, also known as KIR2DL5. CD158f is an inhibitory receptor and a member of the KIR (Killer cell Ig-like receptors) family of receptors, which recognizes subsets of HLA alleles. Expression is found mainly on a subset of NK cells with minimal expression also present on a minor subset of T lymphocytes in some individuals. This new member of the family is highly polymorphic and expression is not found on many human donors. Activation of the receptor and tyrosine phosphoryaltion recruits SHP-2 and SHP-1 to the ITIM cytoplasmic domain. The UP-R1 antibody has been shown to inhibit NK cytotoxicity. Applications Reported This UP-R1 antibody has been reported for use in flow cytometric analysis. Applications Tested This UP-R1 antibody has been pre-titrated and tested by flow cytometric analysis of normal human peripheral blood cells. This can be used at 5 µL (0.25 µg) per test. A test is defined as the amount (µg) of antibody that will stain a cell sample in a final volume of 100 µL. Cell number should be determined empirically but can range from 105 to 108 cells/test. Excitation 633-647 nm; Emission 660 nm; Laser Red Laser. Filtration 0.2 μm post-manufacturing filtered.Killer cell immunoglobulin-like receptors (KIRs) are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. The KIR genes are polymorphic and highly homologous and they are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). The gene content of the KIR gene cluster varies among haplotypes, although several framework genes are found in all haplotypes. The KIR proteins are classified by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM), while KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. The ligands for several KIR proteins are subsets of HLA class I molecules; thus, KIR proteins are thought to play an important role in regulation of the immune response.