Recombinant Rat Il1r1, Fc-His tagged

• Cat.No.: Il1r1-4088R
• Product Overview: Recombinant Rat Il1r1 (NP_037255.3) extracellular domain (Met 1-Lys 352), fused with the C-terminal His-tagged Fc region of mouse IgG1, was produced in Human Cell.

Specification

• Source: HEK293
• Species: Rat
• Tag: His&Fc
• Form: Lyophilized from sterile 50 mM Tris, pH 8.0.
  Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
• Molecular Mass: The recombinant rat IL1R1/mFc is a disulfide-linked homodimer. The reduced monomer comprises 562 amino acids and predicts a molecular mass of 64.6 kDa. The apparent molecular mass of the ratIL1R1/mFc monomer is approximately 90-95 kDa in SDS-PAGE under reducing conditions due to glycosylation.
• Protein length: Met 1-Lys 352
• Endotoxin: < 1.0 EU per μg protein as determined by the LAL method.
• Purity: > 85 % as determined by SDS-PAGE
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C
  Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4℃ before opening to recover the entire contents.

Gene Information

• Gene Name: Il1r1 interleukin 1 receptor, type I [ Rattus norvegicus ]
• Official Symbol: Il1r1
• Synonyms: IL1R1; interleukin 1 receptor, type I; interleukin-1 receptor type 1; p80; IL-1R-1; IL-1RT1; IL-1RT-1; IL-1R-alpha; interleukin-1 receptor alpha; interleukin-1 receptor type I; CD121 antigen-like family member A; interleukin 1 beta receptor type 1 soluble form; interleukin 1 bete receptor type 1 long transmembrane form; interleukin 1 beta receptor type 1 short transmembrane form
• Gene ID: 25663
• mRNA Refseq: NM_013123
• Protein Refseq: NP_037255

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.