CD158f Monoclonal / APC / UP-R1
Product Details
| Description | CD158f, also known as KIR2DL5, is a polymorphic 60 kDa transmembrane glycoprotein with two Ig-like extracellular domains by which it recognize HLA class I molecules. Its long intracellular domain contains immunoreceptor tyrosine-based inhibitory motifs (ITIMs) that upon extracellular ligand-mediated phosphorylation serve as docking sites for inhibitory phosphatases, which results in blocking natural cytotoxicity as well as antibody-dependent cytotoxicity of the particular NK cell, and its adhesion toward target cells. Together with other killer inhibitory receptors CD158f is important for immunological tolerance to discriminate between normal and abnormal cells. Besides NK cells it is expressed on a small population of cytotoxic T cells. Expression of CD158f alleles is highly variable in the population. | |
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| Conjugate | APC | |
| Clone | UP-R1 | |
| Target Species | Human | |
| Applications | FC, ICC | |
| Supplier | EXBIO | |
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About CD158f
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 (KIR3DL3, KIR3DP1, KIR3DL4, KIR3DL2). 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. [provided by RefSeq, Jul 2008]
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 (KIR3DL3, KIR3DP1, KIR3DL4, KIR3DL2). 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. [provided by RefSeq, Jul 2008]
About APC
Allophycocyanin (APC) is a fluorescent protein derived from cyanobacteria and red algae and a potent donor fluorophore to create tandem dyes that can be excited off the 633-640 nm laser. APC has an excitation peak at 650 nm and a emission peak at 660 nm.
Allophycocyanin (APC) is a fluorescent protein derived from cyanobacteria and red algae and a potent donor fluorophore to create tandem dyes that can be excited off the 633-640 nm laser. APC has an excitation peak at 650 nm and a emission peak at 660 nm.
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162 CD158f antibodies from over 22 suppliers available with over 37 conjugates.
