Recombinant Rat Il1r2, Fc tagged

• Cat.No.: Il1r2-8737R
• Product Overview: Recombinant Rat Il1r2 (P43303) (Met1-Glu355), fused with the Fc region of human IgG1 at the C-terminus, was produced in Human Cell.

Specification

• Source: Human Cells
• Species: Rat
• Tag: Fc
• Form: Lyophilized from a 0.2μm filtered solution of PBS, pH 7.4
• Molecular Mass: The recombinant rat IL1R2/Fc is a disulfide-linked homodimer. The reduced monomer comprises 583 amino acids and has a predicted molecular mass of 65.2 kDa. The apparent molecular mass of the protein is approximately 90 and 33 kDa in SDS-PAGE under reducing conditions.
• Endotoxin: < 1.0 eu per μg of the protein as determined by the LAL method.
• Stability: Samples are stable for up to twelve months from date of receipt at -70oC.
• Storage: Store it under sterile conditions at -20oC~-70oC. 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. Centrifuge the vial at 4℃ before opening to recover the entire contents.

Gene Information

• Gene Name: Il1r2 interleukin 1 receptor, type II [ Rattus norvegicus ]
• Official Symbol: Il1r2
• Gene ID: 117022
• mRNA Refseq: NM_053953
• Protein Refseq: NP_446405

Reviews

10/10/2022

High specificity.

09/12/2020

Good for flow cytometry.

09/20/2016

Suitable for co-immunoprecipitation.

Q&As

What are the functional implications of IL1R2's intracellular domain, and how can engineered receptor constructs shed light on its contributions?

The intracellular domain of IL1R2 has functional significance; engineered constructs clarify its role.

How does IL1R2's glycosylation affect its interaction with IL-1 ligands, and how can glycoproteomics methods elucidate these glycosylation sites?

Glycosylation of IL1R2 affects its IL-1 ligand interaction, and glycoproteomics methods can reveal critical glycosylation sites.

In what ways can engineered IL1R2 variants with altered domains provide insights into its molecular mechanisms and potential therapeutic applications?

Engineered IL1R2 variants offer insights into its mechanisms and therapeutic potential.

In what ways does IL1R2's presence influence the downstream signaling of IL-1 ligands through its competition with IL1R1, and how can genetic manipulation techniques help unravel this interplay?

IL1R2's presence impacts IL-1 ligand signaling through competition with IL1R1; genetic manipulations unveil this interaction.

How do post-translational modifications, particularly ubiquitination, influence IL1R2's stability and turnover?

Post-translational modifications, including ubiquitination, influence IL1R2's stability.

How does IL1R2's expression respond to inflammatory cues, and what role do transcription factors play in its regulatory network?

IL1R2 expression responds to inflammation; transcription factors play a role in its regulation.

What insights can super-resolution microscopy offer regarding IL1R2's intracellular trafficking and subcellular localization dynamics?

Super-resolution microscopy helps understand IL1R2's trafficking and subcellular dynamics in detail.

What specific structural features of IL1R2 enable it to function as a decoy receptor, and how can X-ray crystallography provide a detailed understanding of its ligand binding mechanisms?

Specific structural elements of IL1R2 contribute to its decoy role; X-ray crystallography provides insights into ligand binding.

How does the shedding of IL1R2's ectodomain contribute to its role as a soluble decoy receptor, and which enzymes are involved in this process?

Ectodomain shedding contributes to IL1R2's soluble decoy role; specific enzymes are involved.

What significance does IL1R2's interaction with IL-1 receptor accessory proteins hold in terms of its decoy function?

IL1R2's interaction with accessory proteins is significant for its decoy function.