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Recombinant Human IL1R2, DDDDK tagged

Cat.No. : IL1R2-474H
Product Overview : Recombinant Human IL1R2 (NP_004624.1) (Met1-Glu343), fused with five amino acids (DDDDK) at the C-terminus, was produced in Human Cells.
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Source : Human Cells
Species : Human
Tag : DDDDK
Predicted N Terminal : Phe 14
Form : The recombinant human IL1R2 consists of 336 amino acids and predicts a molecular mass of 38.4 KDa. It migrates as an approximately 49 KDa band in SDS-PAGE under reducing conditions.
Molecular Mass : The recombinant human IL1R2 consists of 336 amino acids and predicts a molecular mass of 38.4 KDa. It migrates as an approximately 49 KDa band in SDS-PAGE under reducing conditions.
Endotoxin : < 1.0 eu per μg of the protein as determined by the LAL method.
Purity : >95 % as determined by SDS-PAGE
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 Name : IL1R2 interleukin 1 receptor, type II [ Homo sapiens ]
Official Symbol : IL1R2
Gene ID : 7850
mRNA Refseq : NM_004633
Protein Refseq : NP_004624
MIM : 147811
UniProt ID : P27930
Chromosome Location : 2q12

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
10/10/2022

    High specificity.

    09/12/2020

      Good for flow cytometry.

      09/20/2016

        Suitable for co-immunoprecipitation.

        Q&As (10)

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        What are the functional implications of IL1R2's intracellular domain, and how can engineered receptor constructs shed light on its contributions? 07/14/2021

        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? 04/29/2021

        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? 01/29/2021

        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? 01/04/2020

        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? 05/28/2019

        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? 03/14/2019

        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? 01/06/2019

        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? 10/09/2018

        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? 01/28/2018

        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? 06/05/2016

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

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