Recombinant Human IL1R2 protein, His-tagged
Cat.No. : | IL1R2-2200H |
Product Overview : | Recombinant Human IL1R2 protein(NP_004624.1)(Phe14-Glu343), fused with C-terminal His tag, was expressed in HEK293. |
Availability | February 10, 2025 |
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Source : | HEK293 |
Species : | Human |
Tag : | C-His |
Protein length : | Phe14-Glu343 |
Form : | Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 5% trehalose is added as protectant before lyophilization. |
Bio-activity : | Immobilized Human IL-1R2, His Tag at 5ug/ml (100ul/Well) on the plate. Dose response curve for Biotinylated Human IL-1 Beta, His Tag with the EC50 of 0.38ng/ml determined by ELISA. |
Molecular Mass : | The protein has a predicted MW of 38.9 kDa. Due to glycosylation, the protein migrates to 55-65 kDa based on Tris-Bis PAGE result. |
Endotoxin : | Less than 1EU per μg by the LAL method. |
Purity : | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
Storage : | Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. |
Reconstitution : | Centrifuge tubes before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water. |
Gene Name : | IL1R2 interleukin 1 receptor, type II [ Homo sapiens ] |
Official Symbol : | IL1R2 |
Synonyms : | IL1R2; interleukin 1 receptor, type II; IL1RB; interleukin-1 receptor type 2; CD121b; CDw121b; IL-1R-2; IL-1RT2; IL-1RT-2; IL-1R-beta; antigen CDw121b; IL-1 type II receptor; interleukin-1 receptor beta; interleukin-1 receptor type II; CD121 antigen-like family member B; type II interleukin-1 receptor, beta; MGC47725; |
Gene ID : | 7850 |
mRNA Refseq : | NM_004633 |
Protein Refseq : | NP_004624 |
MIM : | 147811 |
UniProt ID : | P27930 |
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Not For Human Consumption!
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Customer Reviews (3)
Write a reviewHigh specificity.
Good for flow cytometry.
Suitable for co-immunoprecipitation.
Q&As (10)
Ask a questionThe intracellular domain of IL1R2 has functional significance; engineered constructs clarify its role.
Glycosylation of IL1R2 affects its IL-1 ligand interaction, and glycoproteomics methods can reveal critical glycosylation sites.
Engineered IL1R2 variants offer insights into its mechanisms and therapeutic potential.
IL1R2's presence impacts IL-1 ligand signaling through competition with IL1R1; genetic manipulations unveil this interaction.
Post-translational modifications, including ubiquitination, influence IL1R2's stability.
IL1R2 expression responds to inflammation; transcription factors play a role in its regulation.
Super-resolution microscopy helps understand IL1R2's trafficking and subcellular dynamics in detail.
Specific structural elements of IL1R2 contribute to its decoy role; X-ray crystallography provides insights into ligand binding.
Ectodomain shedding contributes to IL1R2's soluble decoy role; specific enzymes are involved.
IL1R2's interaction with accessory proteins is significant for its decoy function.
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