ELISA with Human NKG2A&CD94 Protein 4822

Binding assay with Human NKG2A&CD94 Protein 4822

Human NKG2A&CD94 Protein 4822

$330.00 – $1,100.00

Summary

Expression: HEK293
Functional: Yes (binding assay)
Amino Acid Range: Arg100-Leu233(NKG2A) & Ser34-Ile179(CD94)

SKU: 4822parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P26715(NKG2A)&&Q13241(CD94)
express system	HEK293
product tag	C-mFc
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	The ligand-receptor assignment between HLA-G and NKG2A/CD94 is dependent of the amino acid composition in the HLA-G heavy chain. Understanding the biophysical basis of receptor-mediated events that lead to NK cell inhibition would help to remove non-tumor reactive cells and support personalized mild autologous NK cell therapies.
molecular weight	The protein has a predicted MW of 56.9 kDa. Due to glycosylation, the protein migrates to 70-90 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human NKG2A&CD94 Protein 4822

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
The ligand-receptor assignment between HLA-G and NKG2A/CD94 is dependent of the amino acid composition in the HLA-G heavy chain. Understanding the biophysical basis of receptor-mediated events that lead to NK cell inhibition would help to remove non-tumor reactive cells and support personalized mild autologous NK cell therapies.
Protein names NKG2-A/NKG2-B type II integral membrane protein (CD159 antigen-like family member A) (NK cell receptor A) (NKG2-A/B-activating NK receptor) (CD antigen CD159a)
Gene names KLRC1,KLRC1 NKG2A
Mass 26314Da
Function Immune inhibitory receptor involved in self-nonself discrimination. In complex with KLRD1 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 molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self (PubMed:18083576, PubMed:37264229, PubMed:9430220, PubMed:9486650). Upon HLA-E-peptide binding, transmits intracellular signals through two immunoreceptor tyrosine-based inhibition motifs (ITIMs) by recruiting INPP5D/SHP-1 and INPPL1/SHP-2 tyrosine phosphatases to ITIMs, and ultimately opposing signals transmitted by activating receptors through dephosphorylation of proximal signaling molecules (PubMed:12165520, PubMed:9485206). 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).; (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 (PubMed:32203188, 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).
Subellular location Cell membrane ; Single-pass type II membrane protein .
Tissues Predominantly expressed in NK cells (at protein level) (PubMed:20952657, PubMed:9430220, PubMed:9485206). Expressed in intraepithelial CD8-positive T cell subsets with higher frequency in gamma-delta T cells than alpha-beta T cells (at protein level) (PubMed:18064301). Expressed in memory gamma-delta T cells (at protein level) (PubMed:20952657). Restricted to a subset of memory/effector CD8-positive alpha-beta T cells (at protein level) (PubMed:12387742). Expressed in intratumoral NK and CD8-positive T cells (PubMed:30503213). Expressed in melanoma-specific cytotoxic T cell clones (at protein level) (PubMed:9485206). 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).
Structure Heterodimer with KLRD1; disulfide-linked (PubMed:18083576, PubMed:18332182, PubMed:18448674). KLRD1-KLRC1 heterodimer interacts with peptide-bound HLA-E-B2M heterotrimeric complex (PubMed:18083576). Competes with KLRC2 for its interaction with HLA-E (PubMed:18083576). Interacts (via ITIM) with INPP5D/SHIP-1 and INPPL1/SHIP-2 (via SH2 domain).
Post-translational modification Phosphorylated.
Domain The cytosolic N-terminus contains two immunoreceptor tyrosine-based inhibitory motifs (ITIMs
Target Relevance information above includes information from UniProt accession: P26715
The UniProt Consortium

Data

Human NKG2A&CD94, mFc Tag captured on CM5 Chip via Anti-mouse Antibody can bind Human HLA-E Complex Tetramer, His Tag with an affinity constant of 7.90 nM as determined in SPR assay (Biacore T200).

Immobilized Human NKG2A&CD94, mFc Tag at 0.5µg/ml (100µl/Well) on the plate. Dose response curve for Anti-NKG2A Antibody, hFc Tag with the EC50 of 12.4ng/ml determined by ELISA (QC Test).

Binding assay with Human NKG2A&CD94 Protein

Serial dilutions of Anti-NKG2A Antibody were added into Biotinylated Human HLA-E*01:03 Complex Tetramer, His Tag : Human NKG2A&CD94, mFc Tag binding reactioins. The half maximal inhibitiory concentration (IC50) is 0.15µg/ml.

The purity of Human NKG2A&CD94 is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Human NKG2A&CD94 Protein

Human NKG2A&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.