Active Recombinant Human IL1R1, Fc-tagged, Biotinylated
Cat.No. : | IL1R1-627H |
Product Overview : | The recombinant human IL1R1 ECD is expressed as a 557 amino acid protein consisting of Leu18 -Lys336 region of IL1R1 (UniProt accession #P14778) and a C-terminal Fc from human IgG1, which exists as a dimer under non-reducing conditions. |
Availability | February 15, 2025 |
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Source : | Human cells |
Species : | Human |
Tag : | Fc |
Form : | Supplied at 0.5 mg/ml in sterile PBS pH7.4 (carrier free & preservative free). The purified recombinant protein was labeled with Biotin (3-5 Biotin per molecule). |
Bio-activity : | Interacts with human IL1α and IL1β, and blocks IL1-dependent signaling activity with a typical ED50 of 0.3 - 0.8 μg/ml |
Molecular Mass : | Calculated molecular mass (kDa): 63.4; Estimated by SDS-PAGE under reducing condition (kDa): 75-80 (probably due to glycosylation). |
AA Sequence : | LEADKCKEREEKIILVSSANEIDVR PCPLNPNEHKGTITWYKDDSKTPVS TEQASRIHQHKEKLWFVPAKVEDS GHYYCVVRNSSYCLRIKISAKFVEN EPNLCYNAQAIFKQKLPVAGDGGLV CPYMEFFKNENNELPKLQWYKDCK PLLLDNIHFSGVKDRLIVMNVAEKH RGNYTCHASYTYLGKQYPITRVIEF ITLEENKPTRPVIVSPANETMEVD LGSQIQLICNVTGQLSDIAYWKWNG SVIDEDDPVLGEDYYSVENPANKRR STLITVLNISEIESRFYKHPFTCF AKNTHGIDAAYIQLIYPVTNFQKST TENLYFQGSTGTHTCPPCPAPELLG GPSVFLFPPKPKDTLMISRTPEVT CVVVDVSHEDPEVKFNWYVDGVEVH NAKTKPREEQYNSTYRVVSVLTVLH QDWLNGKEYKCKVSNKALPAPIEK TISKAKGQPREPQVYTLPPSREEMT KNQVSLTCLVKGFYPSDIAVEWESN GQPENNYKTTPPVLDSDGSFFLYS KLTVDKSRWQQGNVFSCSVMHEALH NHYTQKSLSLSPGK |
Endotoxin : | <0.1 eu per 1 μg of purified recombinant protein determined by the lal>0.1> |
Purity : | >95% judged by SDS-PAGE under reducing condition |
Storage : | The product is shipped at 4°C. Upon receipt, centrifuge the product briefly before opening the vial. It is recommended to store small aliquots at the temperature below –20°C for long-term storage and the product is stable for 3 months. The undiluted protein can be stored at 4°C for no more than 2 weeks. Avoid repeated freeze-thaw cycles. |
Gene Name : | IL1R1 interleukin 1 receptor, type I [ Homo sapiens ] |
Official Symbol : | IL1R1 |
Synonyms : | IL1R1; interleukin 1 receptor, type I; IL1R, IL1RA; interleukin-1 receptor type 1; CD121A; D2S1473; IL-1R-1; IL-1RT1; IL-1RT-1; antigen CD121a; interleukin receptor 1; interleukin-1 receptor alpha; interleukin-1 receptor type I; CD121 antigen-like family member A; interleukin 1 receptor alpha, type I; P80; IL1R; IL1RA; IL-1R-alpha; |
Gene ID : | 3554 |
mRNA Refseq : | NM_000877 |
Protein Refseq : | NP_000868 |
MIM : | 147810 |
UniProt ID : | P14778 |
Chromosome Location : | 2q12 |
Pathway : | Amoebiasis, organism-specific biosystem; Amoebiasis, conserved biosystem; Apoptosis, organism-specific biosystem; Apoptosis, conserved biosystem; Cytokine Signaling in Immune system, organism-specific biosystem; Cytokine-cytokine receptor interaction, organism-specific biosystem; Cytokine-cytokine receptor interaction, conserved biosystem; |
Function : | interleukin-1 receptor activity; interleukin-1, Type I, activating receptor activity; platelet-derived growth factor receptor binding; protease binding; protein binding; receptor activity; signal transducer activity; transmembrane signaling receptor activity; |
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Not For Human Consumption!
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Customer Reviews (3)
Write a reviewHigh stability.
Suitable for ELISA.
Effective in signaling studies.
Q&As (10)
Ask a questionLive-cell imaging techniques track IL1R1's movement on the cell surface, revealing how cellular localization impacts its responsiveness to ligands.
Advanced computational modeling and molecular dynamics simulations predict allosteric changes in IL1R1's intracellular domain upon ligand binding, revealing insights into its downstream signaling cascade.
FRET and cross-linking assays reveal the multimeric assembly of IL1R1, shedding light on its dimerization and oligomerization dynamics.
Confocal microscopy and flow cytometry visualize IL1R1's endocytosis and recycling, offering insights into its intracellular trafficking dynamics and signaling duration.
Co-immunoprecipitation assays unravel the interactions between IL1R1 and adapter proteins, elucidating the molecular details of its intracellular signaling cascade.
Mutagenesis studies dissect the interfaces between IL1R1 and accessory proteins like IL1RAP, uncovering their roles in ligand binding and signaling modulation.
Cryo-electron microscopy captures IL1R1's structural shifts during ligand binding, unveiling conformational changes that influence its ligand recognition.
Proteomics-based studies uncover the crosstalk between IL1R1 and other receptors in signaling networks, unveiling their interconnected pathways.
CRISPR-based approaches manipulate IL1R1 expression and alternative splicing, providing functional insights into the complex regulatory mechanisms governing its variations.
Phosphoproteomics characterizes IL1R1's phosphorylation landscape, revealing how post-translational modifications shape its downstream signaling outcomes.
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