Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs has established a broad range of platforms for developing novel antibodies or equivalents. These cutting-edge technologies enable our scientists to meet your demands from different aspects and tailor the most appropriate solution that contributes to the success of your projects.
HighlightsWith deep understanding in antibody-related realms and extensive project experience, Creative Biolabs offers a variety of references to help you learn more about our capacities and achievements, including infographic, flyer, case study, peer-reviewed publications, and all kinds of knowledge that can assist your projects. You are also welcome to contact us directly for more specific solutions.
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Killer cell lectin like receptor C1 (KLRC1, NKG2A) is a type II single transmembrane receptor encoded by KLRC1 gene, which is mainly expressed on the cell membrane surfaces of NK cells and CD8⁺T cells. This receptor can combine with KLRD1(CD94) through disulfide bonds to form a heterodimer functional complex, which is an important inhibitory regulatory molecule on lymphocyte surface. The structure of KLRC1 protein includes a short cytoplasmic tail with dual ITIM inhibitory motifs, a single transmembrane helix and a large extracellular C-type lectin domain. Its extracellular functional region can specifically recognize HLA-E ligands on the surface of target cells, providing a structural basis for receptor ligand binding and downstream signal transduction.
A large number of structural studies have confirmed that the extracellular lectin domain of KLRC1 can specifically bind to HLA-E peptide complex, and then recruit intracellular phosphatase molecules, start downstream inhibitory signals, and block the excessive transmission of cytotoxic signals of lymphocytes. In the absence of this inhibition mechanism, the killing activity of NK cells will be out of control, which will easily lead to autoimmune damage. KLRC1 can effectively restrain the overactivation of lymphocytes and maintain the balance between immune homeostasis and autoimmune tolerance in the microenvironment of lymphoid tissue by establishing a stable immunosuppression signal threshold. Lymphocytes can dynamically regulate the expression abundance of KLRC1 on the cell membrane surface according to their own activation state, and form a gradient inhibition signal during contact with the target cells expressing HLA-E, so as to accurately adapt to the regulation requirements of different immune scenarios. At the same time, the highly conserved calcium-binding residues in the lectin domain can stabilize the ligand-receptor complex structure at the contact interface of physiological cells, ensure the efficient and accurate transmission of immunosuppressive signals mediated by KLRC1, and play a key role in maintaining immune balance and avoiding abnormal immune killing.
Variants within KLRC1 extracellular lectin regions could reduce HLA-E binding affinity and weaken inhibitory signal transmission in primary immune cell models. No other NKG2 paralog fully duplicates KLRC1’s dual ITIM-mediated inhibitory capacity, though other KLRC family receptors carry partial ligand overlap. KLRC1 localizes exclusively to outer plasma leaflets after heterodimerization with CD94, never dissociating into soluble cytoplasmic pools. Its type II transmembrane topology separates it from soluble immune mediators, holding dual roles in HLA-E ligand sensing and intracellular phosphatase recruitment. Reduced KLRC1 expression lowers inhibitory signal output and elevates off-target lymphocyte cytotoxicity, making this receptor a suitable research target for NK immune checkpoint analysis.
Fig. 1 Schematic of KLRC1 (NKG2A)‑CD94 inhibitory and NKG2C‑CD94 activating receptor complexes recognizing HLA‑E‑peptide ligands on target cells.1
The biological functions of integral membrane KLRC1 NKG2A receptor are focused on HLA-E ligand capture and ITIM-dependent inhibitory signaling:
Creative Biolabs offers purified KLRC1 membrane protein samples produced under unified preparation workflows, including full-length KLRC1 constructs and isolated extracellular lectin domain variants. Truncated fragments cannot support complete CD94 heterodimerization and phosphatase recruitment activity, while full-length forms fit NK inhibitory receptor research. All batches receive uniform quality screening. Functional assessments may only be performed under simulated lipid bilayer microenvironment setups. Lectin ligand pocket structure is preserved across batches for comparative HLA binding testing. Full-length KLRC1 samples retain intact HLA-E contact surfaces post-purification, supporting reliable detection of transient receptor-ligand complexes in functional comparative analysis.
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Creative Biolabs provides cell research models with adjustable KLRC1 expression levels, suitable for structural observation of type II C-type lectin immune receptors and HLA ligand interaction research. Sample assessment covers sustained membrane detection and CD94 heterodimer binding analysis, enabling side-by-side comparison of inhibitory signal strength under varying KLRC1 abundances. These cell models can be paired with cytotoxicity detection schemes to track NK activity shifts linked to receptor dosage changes.
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Anti-KLRC1 recombinant antibodies are generated via standardized workflows, compatible with NK cell membrane localization mapping and CD94-KLRC1 heterodimer complex identification. The antibody series supports multi-dimensional visualization of KLRC1 distribution within lymphoid tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for KLRC1 research:
KLRC1 may act as a type II transmembrane inhibitory receptor, heterodimerizing with CD94 to bind HLA-E and transmit intracellular phosphatase-mediated inhibitory signals.
KLRC1 expression status might modulate NK cell cytotoxic thresholds, serving as a key mediator of lymphoid self-tolerance biological processes.
No, all KLRC1 related products and services are strictly for research use only, and cannot be applied in clinical workflows. All material design and functional screening are optimized exclusively for basic laboratory research, without meeting clinical application criteria.
Offerings include full-length KLRC1 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on lectin receptor heterodimerization and immune checkpoint signaling.
Laboratory analysis schemes may include HLA peptide complex binding assays to assess lectin-ligand interaction capacity under simulated lipid bilayer environments.
