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.

Specification

• 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>
• 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 Information

• 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

Reviews

07/14/2022

High stability.

06/07/2017

Suitable for ELISA.

04/19/2017

Effective in signaling studies.

Q&As

How does the cellular localization of IL1R1 influence its responsiveness to ligands, and how can live-cell imaging techniques track its dynamic movement on the cell surface?

Live-cell imaging techniques track IL1R1's movement on the cell surface, revealing how cellular localization impacts its responsiveness to ligands.

How can advanced computational modeling and molecular dynamics simulations predict the allosteric changes in IL1R1's intracellular domain upon ligand binding, offering insights into its downstream signaling cascade?

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.

What are the mechanisms underlying IL1R1's dimerization and oligomerization, and how can FRET and cross-linking assays provide insights into its multimeric assembly?

FRET and cross-linking assays reveal the multimeric assembly of IL1R1, shedding light on its dimerization and oligomerization dynamics.

How does IL1R1's endocytosis and recycling affect its signaling duration, and how can confocal microscopy and flow cytometry unveil its intracellular trafficking patterns?

Confocal microscopy and flow cytometry visualize IL1R1's endocytosis and recycling, offering insights into its intracellular trafficking dynamics and signaling duration.

What are the intricate molecular details of IL1R1's recruitment of MyD88 and other adapter proteins upon ligand binding, and how can co-immunoprecipitation assays reveal these interactions?

Co-immunoprecipitation assays unravel the interactions between IL1R1 and adapter proteins, elucidating the molecular details of its intracellular signaling cascade.

How does the interaction between IL1R1 and accessory proteins like IL1RAP influence its ligand binding and intracellular signaling, and how can mutagenesis studies dissect these interfaces?

Mutagenesis studies dissect the interfaces between IL1R1 and accessory proteins like IL1RAP, uncovering their roles in ligand binding and signaling modulation.

How do the structural dynamics of IL1R1's extracellular domains modulate its binding to various ligands, and how can cryo-electron microscopy unveil these conformational changes?

Cryo-electron microscopy captures IL1R1's structural shifts during ligand binding, unveiling conformational changes that influence its ligand recognition.

What are the intricate crosstalk mechanisms between IL1R1 and other receptors in cell signaling networks, and how can proteomics-based studies dissect these interconnected pathways?

Proteomics-based studies uncover the crosstalk between IL1R1 and other receptors in signaling networks, unveiling their interconnected pathways.

What are the complex regulatory mechanisms governing IL1R1's expression and alternative splicing, and how can CRISPR-based approaches shed light on the functional consequences of these variations?

CRISPR-based approaches manipulate IL1R1 expression and alternative splicing, providing functional insights into the complex regulatory mechanisms governing its variations.

In what ways does IL1R1's post-translational modification landscape impact its downstream signaling, and how can phosphoproteomics offer a comprehensive view of its phosphorylation events?

Phosphoproteomics characterizes IL1R1's phosphorylation landscape, revealing how post-translational modifications shape its downstream signaling outcomes.