Active Recombinant Human IL1R1 Protein

Cat.No. : IL1R1-214H
Product Overview : Recombinant Human IL1R1 was expressed in HEK293.
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Description : This gene encodes a cytokine receptor that belongs to the interleukin-1 receptor family. The encoded protein is a receptor for interleukin-1 alpha, interleukin-1 beta, and interleukin-1 receptor antagonist. It is an important mediator involved in many cytokine-induced immune and inflammatory responses. This gene is located in a cluster of related cytokine receptor genes on chromosome 2q12.
Source : HEK293
Species : Human
Form : 1 x PBS
Bio-activity : The ED50 is 0.2 - 0.6 µg/ml, corresponding to a specific activity of 1.7 - 5.0 x 10^3 units/mg, determined by the dose dependent inhibition of D10.G4.1 cell proliferation.
Molecular Mass : 38 kDa
Endotoxin : Less than 0.01 ng per µg protein as determined by the LAL method.
Purity : >95%, as determined by Coomassie stained SDS-PAGE.
Concentration : Protein formulated and vialed at >50 ug/mL in specified buffer
Tag : Non
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

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Customer Reviews (3)

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Reviews
07/14/2022

    High stability.

    06/07/2017

      Suitable for ELISA.

      04/19/2017

        Effective in signaling studies.

        Q&As (10)

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        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? 10/01/2022

        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? 04/19/2022

        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? 12/26/2020

        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? 12/25/2020

        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? 07/25/2020

        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? 04/13/2020

        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? 02/22/2020

        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? 01/17/2020

        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? 09/09/2018

        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? 09/17/2017

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

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