| Host: |
HEK293 |
| Note: |
STRICTLY FOR FURTHER RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description: |
Recombinant-Human CD94-N-His-Avi protein was developed from hek293 and has a target region of N-His-Avi. For use in research applications. |
| Conjugation: |
Biotin |
| Formulation: |
Lyophilised from 0.2 µm filtered PBS solution pH7.4. |
| Dilution Range: |
Upon receipt centrifuge vial to ensure maximal product extraction, recommended: 20sec, 5K RPM |
| Storage Instruction: |
The lyophilized protein is stable for at least 1 year from date of receipt at-20°C. |
| Endotoxin: |
Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg (1EU/µg). |
| Gene Symbol: |
KLRD1 |
| Gene ID: |
3824 |
| Uniprot ID: |
KLRD1_HUMAN |
| Immunogen Region: |
Ser34-Ile179 |
| Immunogen: |
DNA sequence encoding Human CD94 including a N-His-Avi tag was expressed in HEK293 Cells. The recombinant protein was then biotinylated site specific using the AVItag biotinylation technology. |
| Function | Immune receptor involved in self-nonself discrimination. In complex with KLRC1 or KLRC2 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule HLA-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia and non-classical MHC class Ib molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self. Primarily functions as a ligand binding subunit as it lacks the capacity to signal. KLRD1-KLRC1 acts as an immune inhibitory receptor. Key inhibitory receptor on natural killer (NK) cells that regulates their activation and effector functions. Dominantly counteracts T cell receptor signaling on a subset of memory/effector CD8-positive T cells as part of an antigen-driven response to avoid autoimmunity. On intraepithelial CD8-positive gamma-delta regulatory T cells triggers TGFB1 secretion, which in turn limits the cytotoxic programming of intraepithelial CD8-positive alpha-beta T cells, distinguishing harmless from pathogenic antigens. In HLA-E-rich tumor microenvironment, acts as an immune inhibitory checkpoint and may contribute to progressive loss of effector functions of NK cells and tumor-specific T cells, a state known as cell exhaustion. Upon HLA-E-peptide binding, transmits intracellular signals through KLRC1 immunoreceptor tyrosine-based inhibition motifs (ITIMs) by recruiting INPP5D/SHIP-1 and INPPL1/SHIP-2 tyrosine phosphatases to ITIMs, and ultimately opposing signals transmitted by activating receptors through dephosphorylation of proximal signaling molecules. KLRD1-KLRC2 acts as an immune activating receptor. On cytotoxic lymphocyte subsets recognizes HLA-E loaded with signal sequence-derived peptides from non-classical MHC class Ib HLA-G molecules, likely playing a role in the generation and effector functions of adaptive NK cells and in maternal-fetal tolerance during pregnancy. Regulates the effector functions of terminally differentiated cytotoxic lymphocyte subsets, and in particular may play a role in adaptive NK cell response to viral infection. Upon HLA-E-peptide binding, transmits intracellular signals via the adapter protein TYROBP/DAP12, triggering the phosphorylation of proximal signaling molecules and cell activation. (Microbial infection) Viruses like human cytomegalovirus have evolved an escape mechanism whereby virus-induced down-regulation of host MHC class I molecules is coupled to the binding of viral peptides to HLA-E, restoring HLA-E expression and inducing HLA-E-dependent NK cell immune tolerance to infected cells. Recognizes HLA-E in complex with human cytomegalovirus UL40-derived peptide (VMAPRTLIL) and inhibits NK cell cytotoxicity. (Microbial infection) May recognize HLA-E in complex with HIV-1 gag/Capsid protein p24-derived peptide (AISPRTLNA) on infected cells and may inhibit NK cell cytotoxicity, a mechanism that allows HIV-1 to escape immune recognition. (Microbial infection) Upon SARS-CoV-2 infection, may contribute to functional exhaustion of cytotoxic NK cells and CD8-positive T cells. On NK cells, may recognize HLA-E in complex with SARS-CoV-2 S/Spike protein S1-derived peptide (LQPRTFLL) expressed on the surface of lung epithelial cells, inducing NK cell exhaustion and dampening antiviral immune surveillance. |
| Protein Name | Natural Killer Cells Antigen Cd94Kp43Killer Cell Lectin-Like Receptor Subfamily D Member 1Nk Cell ReceptorCd Antigen Cd94 |
| Database Links | Reactome: R-HSA-198933Reactome: R-HSA-2172127Reactome: R-HSA-2424491 |
| Cellular Localisation | Cell MembraneSingle-Pass Type Ii Membrane Protein |
| Alternative Protein Names | Natural Killer Cells Antigen Cd94 proteinKp43 proteinKiller Cell Lectin-Like Receptor Subfamily D Member 1 proteinNk Cell Receptor proteinCd Antigen Cd94 proteinKLRD1 proteinCD94 protein |
Information sourced from Uniprot.org
12 months for antibodies. 6 months for ELISA Kits. Please see website T&Cs for further guidance
