IL1RAP / IL-1RAcP Protein, Human, Recombinant (His & Fc Tag)

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IL1RAP / IL-1RAcP Protein, Human, Recombinant (His & Fc Tag): Product Information

Purity
> 95 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
1. Measured by its ability to bind with biotinylated human IL1R2-His (Cat:10111-H08H)in a functional ELISA.
2. Immobilized human IL1R3-Fch at 10 μg/mL (100ul/well) can bind biotinylated human IL1B-His (Cat:10139-H07E). The EC50 of biotinylated human IL1B-His (Cat:10139-H07E) is 0.11-0.25 μg/mL.
Protein Construction
A DNA sequence encoding the human IL1R3 (NP_002173.1) extracellular domain (Met 1-Glu 359) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Ser 21
Molecule Mass
The recombinant human IL1R3/Fc is a disulfide-linked homodimer. The reduced monomer consists of 586 amino acids and has a predicted molecular mass of 67.3 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh IL1R3/Fc monomer is approximately 75-85 kDa due to glycosylation.
Formulation
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -70℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

IL1RAP / IL-1RAcP Protein, Human, Recombinant (His & Fc Tag): Images

IL1RAP / IL-1RAcP Protein, Human, Recombinant (His & Fc Tag): Alternative Names

C3orf13 Protein, Human; IL-1RAcP Protein, Human; IL1R3 Protein, Human

IL1RAP / IL-1RAcP Background Information

Interleukin-1 receptor accessory protein (IL-1RAcP) also known as Interleukin-1 receptor member 3 (IL-1R3) is a a cytokine receptor which binds interleukin 1. The IL-1 receptor accessory protein (IL1RAP) is a transmembrane protein that interacts with IL-1R and is required for IL-1 signal transduction. Interleukin 1 induces synthesis of acute phase and proinflammatory proteins during infection, tissue damage, or stress, by forming a complex at the cell membrane with an interleukin 1 receptor and an accessory protein. IL-1RAcP/IL-1R3 is a necessary part of the interleukin 1 receptor complex which initiates signalling events that result in the activation of interleukin 1-responsive genes. Alternative splicing of this gene results in two transcript variants encoding two different isoforms, one membrane-bound and one soluble. The ratio of soluble to membrane-bound forms increases during acute-phase induction or stress. IL-1RAcP/IL-1R3 mediates interleukin-1-dependent activation of NF-kappa-B. Isoform 1 is part of the membrane-bound form of the IL-1 receptor. Signaling involves formation of a ternary complex containing IL1R1, TOLLIP, MYD88, and IRAK1 or IRAK2. Isoform 2 modulates the response to interleukins by associating with soluble IL1R1 and enhancing interleukin-binding to the decoy receptor.
Full Name
interleukin 1 receptor accessory protein
References
  • Goldbach-Mansky R, et al. (2009) Autoinflammation: the prominent role of IL-1 in monogenic autoinflammatory diseases and implications for common illnesses. J Allergy Clin Immunol. 124(6): 1141-9.
  • Johnston A, et al. (2011) IL-1F5, -F6, -F8, and -F9: a novel IL-1 family signaling system that is active in psoriasis and promotes keratinocyte antimicrobial peptide expression. J Immunol. 186(4): 2613-22.
  • Ozaki K, et al. (2001) Effect of tumor weight and tube feeding on TNF-alpha and IL-1beta mRNA expression in the brain of mice. JPEN J Parenter Enteral Nutr. 25(6): 317-22.
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