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Human CD94 Protein 4535

$345.00$1,150.00

Summary

  • Expression: HEK293
  • Pure: Yes (HPLC)
  • Amino Acid Range: Ser34-Ile179
SKU: 4535parent Categories: , Tags: , , ,
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

Q13241

express system

HEK293

product tag

N-His-Avi

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

CD94 is an approximately 25 kDa type 2 transmembrane protein that plays an important role in regulating natural killer (NK) cell activation.CD94 plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.

molecular weight

The protein has a predicted MW of 19.8 kDa. Due to glycosylation, the protein migrates to 38-42 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human CD94 Protein 4535

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
CD94 is an approximately 25 kDa type 2 transmembrane protein that plays an important role in regulating natural killer (NK) cell activation.CD94 plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.
Protein names
Natural killer cells antigen CD94 (KP43) (Killer cell lectin-like receptor subfamily D member 1) (NK cell receptor) (CD antigen CD94)
Gene names
KLRD1,KLRD1 CD94
Mass
9606Da
Function
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 (PubMed:10023772, PubMed:18064301, PubMed:18083576, PubMed:37264229, PubMed:9486650, PubMed:9754572). Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self (PubMed:12387742, PubMed:18064301, PubMed:9430220). Primarily functions as a ligand binding subunit as it lacks the capacity to signal. {ECO:0000269|PubMed:10023772, ECO:0000269|PubMed:12387742, ECO:0000269|PubMed:18064301, ECO:0000269|PubMed:18083576, ECO:0000269|PubMed:37264229, ECO:0000269|PubMed:9430220, ECO:0000269|PubMed:9486650, ECO:0000269|PubMed:9754572}.; FUNCTION: KLRD1-KLRC1 acts as an immune inhibitory receptor. Key inhibitory receptor on natural killer (NK) cells that regulates their activation and effector functions (PubMed:30860984, PubMed:9430220, PubMed:9485206, PubMed:9486650). 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 (PubMed:12387742). 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 (PubMed:18064301). 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 (PubMed:30503213, PubMed:30860984). 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 (PubMed:12165520, PubMed:9485206). {ECO:0000269|PubMed:12165520, ECO:0000269|PubMed:12387742, ECO:0000269|PubMed:18064301, ECO:0000269|PubMed:30503213, ECO:0000269|PubMed:30860984, ECO:0000269|PubMed:9430220, ECO:0000269|PubMed:9485206, ECO:0000269|PubMed:9486650}.; FUNCTION: KLRD1-KLRC2 acts as an immune activating receptor (PubMed:15940674, PubMed:9655483). 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 (PubMed:30134159, PubMed:9754572). 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 (PubMed:20952657, PubMed:21825173). Upon HLA-E-peptide binding, transmits intracellular signals via the adapter protein TYROBP/DAP12, triggering the phosphorylation of proximal signaling molecules and cell activation (PubMed:15940674, PubMed:9655483). {ECO:0000269|PubMed:15940674, ECO:0000269|PubMed:20952657, ECO:0000269|PubMed:21825173, ECO:0000269|PubMed:30134159, ECO:0000269|PubMed:9655483, ECO:0000269|PubMed:9754572}.; FUNCTION: (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. {ECO:0000269|PubMed:10669413, ECO:0000269|PubMed:23335510}.; FUNCTION: (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. {ECO:0000269|PubMed:15751767}.; FUNCTION: (Microbial infection) Upon SARS-CoV-2 infection, may contribute to functional exhaustion of cytotoxic NK cells and CD8-positive T cells (PubMed:32859121). 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 (PubMed:32859121). {ECO:0000269|PubMed:32859121}.
Subellular location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20952657, ECO:0000269|PubMed:9485206}; Single-pass type II membrane protein {ECO:0000255}.
Tissues
TISSUE SPECIFICITY: Expressed in NK cell subsets (at protein level) (PubMed:21825173, PubMed:9430220, PubMed:9485206). Expressed in memory/effector CD8-positive alpha-beta T cell subsets (at protein level) (PubMed:12387742, PubMed:20952657). Expressed in melanoma-specific cytotoxic T cell clones (at protein level) (PubMed:9485206). Expressed in terminally differentiated cytotoxic gamma-delta T cells (at protein level) (PubMed:20952657). KLRD1-KLRC1 and KLRD1-KLRC2 are differentially expressed in NK and T cell populations, with only minor subsets expressing both receptor complexes (at protein level) (PubMed:20952657). {ECO:0000269|PubMed:12387742, ECO:0000269|PubMed:20952657, ECO:0000269|PubMed:21825173, ECO:0000269|PubMed:9430220, ECO:0000269|PubMed:9485206}.
Structure
SUBUNIT: Can form disulfide-bonded heterodimer with NKG2 family members KLRC1 and KLRC2 (PubMed:18083576, PubMed:18332182, PubMed:18448674, PubMed:9655483). KLRD1-KLRC1 heterodimer interacts with peptide-bound HLA-E-B2M heterotrimeric complex. KLRD1 plays a prominent role in directly interacting with HLA-E (PubMed:18083576). KLRD1-KLRC1 interacts with much higher affinity with peptide-bound HLA-E-B2M than KLRD1-KLRC2 (PubMed:10428963, PubMed:9486650). Interacts with the adapter protein TYROBP/DAP12; this interaction is required for cell surface expression and cell activation (PubMed:15940674, PubMed:9655483). {ECO:0000269|PubMed:10428963, ECO:0000269|PubMed:18083576, ECO:0000269|PubMed:18332182, ECO:0000269|PubMed:18448674, ECO:0000269|PubMed:9486650, ECO:0000269|PubMed:9655483}.
Target Relevance information above includes information from UniProt accession : Q13241
The UniProt Consortium

Data

HPLC of Human CD94 Protein
The purity of Human CD94 is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human CD94 Protein
Human CD94 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.




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