Recombinant Human IL1R1 Protein, C-His-tagged

• Cat.No.: IL1R1-064H
• Product Overview: Recombinant Human IL1R1 Protein with C-His tag was expressed in E. coli.

Specification

• Description: Three structurally related ligands for IL-1Rs have been described. Theseinclude two agonists, IL-1α and IL-1β, and a specific receptor antagonist, IL-1Rα. Among the activities regulated by IL-1 are fever, acute phase responses, degradation of connective tissue and immunostimulatory activities. The IL-1Rα molecule also binds specifically to IL-1Rs, but fails to initiate intracellular responses. Two distinct IL-1Rs have been identified, each of which belongs to the Ig superfamily and is widely expressed in a broad range of cells and tissues. Although many cell types co-express type I and type II receptors, there is no evidence that these constitute subunits of a single complex. The type II receptor has a short 29 amino acid cytoplasmic domain that does not seem sufficient for signaling while in fact there is considerable evidence arguing that IL-1 signals exclusively through the type I IL-1R.
• Source: E. coli
• Species: Human
• Tag: His
• Molecular Mass: ~35 kDa
• AA Sequence: LEADKCKEREEKIILVSSANEIDVR PCPLNPNEHKGTITWYKDDSKTPVS TEQASRIHQHKEKLWFVPAKVEDSG HYYCVVRNSSYCLRIKISAKFVENE PNLCYNAQAIFKQKLPVAGDGGLVC PYMEFFKNENNELPKLQWYKDCKPL LLDNIHFSGVKDRLIVMNVAEKHRG NYTCHASYTYLGKQYPITRVIEFIT LEENKPTRPVIVSPANETMEVDLGS QIQLICNVTGQLSDIAYWKWNGSVI DEDDPVLGEDYYSVENPANKRRSTL ITVLNISEIESRFYKHPFTCFAKNT HGIDAAYIQLIYPVTNFQK
• Purity: Transferred into competent cells and the supernatant was purified by NI column affinity chromatography and the purity is > 85% (by SDS-PAGE).
• Notes: For research use only, not for use in diagnostic procedure.
• Storage: Store at 4 centigrade short term. Aliquot and store at -20 centigrade long term. Avoid freeze-thaw cycles.
• Concentration: ≥0.5 mg/mL
• Storage Buffer: PBS, 4M Urea, pH7.4

Gene Information

• Gene Name: IL1R1 interleukin 1 receptor, type I [ Homo sapiens (human) ]
• 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

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.