| Field | Specification |
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| Alternative Names | Interferon lambda receptor 1 (IFNLR1); partial; Interferon lambda receptor 1(IFN-lambda receptor 1)(IFN-lambda-R1)(Cytokine receptor class-II member 12)(Cytokine receptor family 2 member 12)(CRF2-12)(Interleukin-28 receptor subunit alpha)(IL-28 receptor subunit alpha)(IL-28R-alpha)(IL-28RA)(Likely interleukin or cytokine receptor 2)(LICR2) |
| Conjugate | |
| Endotoxin Level | |
| Expression System | |
| Form | Liquid or Lyophilized powder |
| Molecular Weight | |
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| UniProt # |
Overview
Recombinant Human Interferon lambda receptor 1 (IFNLR1), partial is a recombinant protein reagent derived from Homo sapiens (Human) and produced in E.coli. It is commonly used to support Immunology research by enabling binding assays, assay development and protein–protein interaction studies in controlled in vitro settings.
Key elements and design rationale
- Expressed region: 21-228aa. Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.
- Expression system: E.coli. Expression host can influence folding and the presence/absence of post-translational modifications.
- Tag / fusion: N-terminal 6xHis-SUMO-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.
- Molecular weight (reported): 36.6 kDa. Apparent size may vary with tags, processing, and gel conditions.
When comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.
Biological background
The gene commonly associated with this target is IFNLR1. IFNLR1 refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Homo sapiens (Human) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt/NCBI) and the recent literature for the specific organism and isoform.
Research relevance and current trends
- Profiling immune signaling nodes and cytokine pathways across cell types and activation states.
- Studying ligand–receptor interactions that shape immune cell communication and effector function.
- Building quantitative assays to compare pathway modulation by genetic or pharmacologic perturbations.
Relevance: The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state. Determines the cell type specificity of the lambda interferon action. Shows a more restricted pattern of expression in the epithelial tissues thereby limiting responses to lambda interferons primarily to epithelial cells of the respiratory, gastrointestinal, and reproductive tracts. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium.
Common research applications
- Assay and standard development for immunoassays or binding-based detection methods.
- Protein–protein interaction studies (e.g., receptor–ligand or complex assembly) using purified components.
- Structure–function analysis, including domain mapping or evaluation of sequence variants.
In quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative/positive controls and, where possible, orthogonal assay formats that support the same conclusion.
Notes for experimental interpretation
- Recombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.
- Tag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.
- Species and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.
- E. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
