Recombinant Full Length Rat Interleukin-1 Receptor Type 2(Il1R2) Protein, His-Tagged

• Cat.No.: RFL13892RF
• Product Overview: Recombinant Full Length Rat Interleukin-1 receptor type 2(Il1r2) Protein (P43303) (14-416aa), fused to N-terminal His tag, was expressed in E. coli.

Specification

• Source: E.coli expression system
• Species: Rattus norvegicus (Rat)
• Tag: His
• Form: Lyophilized powder
• Protein length: Full Length of Mature Protein (14-416)
• AA Sequence: FTTPAVVHTGRVSESPVTSEKHPVL GDDCWFRGRDFKSELRLEGEPVVLR CPLVPHSDTSSSSRSLLTWSKSDSS QLIPGDEPRMWVKDDTLWVLPAVQQ DSGTYICTFRNASHCEQMSLELKVF KNTEASFPLVSYLQISALSSTGLLV CPDLKEFISSRTDGKIQWYKGSILL DKGNKKFLSAGDPTRLLISNTSMGD AGYYRCVMTFTYEGKEYNITRNIEL RVKGITTEPIPVIISPLETIPASLG SRLIVPCKVFLGTGTSSNTIVWWMA NSTFISVAYPRGRVTEGLHHQYSEN DENYVEVSLIFDPVTKEDLNTDFKC VATNPRSFQSLHTTVKEVSSTFSWG IALAPLSLIILVVGAIWIRRRCKRQ AGKTYGLTKLPTDNQDFPSSPNQIK EMK
• Purity: Greater than 90% as determined by SDS-PAGE.
• Applications: SDS-PAGE
• Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
• Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
• Storage Buffer: Tris/PBS-based buffer, 6% Trehalose, pH 8.0
• Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
• Gene Name: Il1r2
• Synonyms: Il1r2; Il-1r2; Il1rb; Interleukin-1 receptor type 2; IL-1R-2; IL-1RT-2; IL-1RT2; CD121 antigen-like family member B; IL-1 type II receptor; Interleukin-1 receptor beta; IL-1R-beta; Interleukin-1 receptor type II; CD antigen CD121b
• UniProt ID: P43303

Gene Information

• Gene Name: Il1r2
• Synonyms: Il1r2; Il-1r2; Il1rb; Interleukin-1 receptor type 2; IL-1R-2; IL-1RT-2; IL-1RT2; CD121 antigen-like family member B; IL-1 type II receptor; Interleukin-1 receptor beta; IL-1R-beta; Interleukin-1 receptor type II; CD antigen CD121b
• UniProt ID: P43303

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.