Active Recombinant Cynomolgus IL1R1, Fc tagged
Cat.No. : | IL1R1-148C |
Product Overview : | Recombinant Cynomolgus IL1R1 (G7NAT4) (Met1-Thr332), fused with the Fc region of human IgG1 at the C-terminus, was produced in Human Cells. |
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Source : | HEK293 |
Species : | Cynomolgus |
Tag : | 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. |
Bio-activity : | Measured by its binding ability in a functional ELISA. Immobilized human IL1RA at 10 μg/ml (100 μl/well) can bind Cynomolgus IL1R1-Fc, The EC50 of Cynomolgus IL1R1-Fc is 0.04-0.08 μg/mL. |
Molecular Mass : | The recombinant cynomolgus IL1R1 is a disulfide-linked homodimer. The reduced monomer comprises 553 amino acids and has a calculated molecular mass of 62.9 KDa.The apparent molecular mass of the protein is approximately 73-93 KDa respectively in SDS-PAGE. |
Protein length : | Met1-Thr332 |
Endotoxin : | < 1.0 EU per μg protein as determined by the LAL method. |
Purity : | > 95 % 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. |
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Not For Human Consumption!
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Customer Reviews (3)
Write a reviewHigh stability.
Suitable for ELISA.
Effective in signaling studies.
Q&As (10)
Ask a questionLive-cell imaging techniques track IL1R1's movement on the cell surface, revealing how cellular localization impacts its responsiveness to ligands.
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.
FRET and cross-linking assays reveal the multimeric assembly of IL1R1, shedding light on its dimerization and oligomerization dynamics.
Confocal microscopy and flow cytometry visualize IL1R1's endocytosis and recycling, offering insights into its intracellular trafficking dynamics and signaling duration.
Co-immunoprecipitation assays unravel the interactions between IL1R1 and adapter proteins, elucidating the molecular details of its intracellular signaling cascade.
Mutagenesis studies dissect the interfaces between IL1R1 and accessory proteins like IL1RAP, uncovering their roles in ligand binding and signaling modulation.
Cryo-electron microscopy captures IL1R1's structural shifts during ligand binding, unveiling conformational changes that influence its ligand recognition.
Proteomics-based studies uncover the crosstalk between IL1R1 and other receptors in signaling networks, unveiling their interconnected pathways.
CRISPR-based approaches manipulate IL1R1 expression and alternative splicing, providing functional insights into the complex regulatory mechanisms governing its variations.
Phosphoproteomics characterizes IL1R1's phosphorylation landscape, revealing how post-translational modifications shape its downstream signaling outcomes.
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