< 1.0 EU per μg of the protein as determined by the LAL method
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.
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.
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.
Lyophilized from sterile PBS, pH 7.4 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
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.
安定性 & 保存条件
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ 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.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Measured by its ability to bind with biotinylated human IL1R2-His (Cat: 10111-H08H)in a functional ELISA. Immobilized human IL1R3-Fch at 10 μg/mL (100μl/well) can bind biotinylated human IL1B-His (Cat: 10139-H07E). The EC50of biotinylated human IL1B-His (Cat: 10139-H07E) is 0.11-0.25 μg/mL.
C3orf13 Protein, Human; IL-1RAcP Protein, Human; IL1R3 Protein, Human
Interleukin-1 receptor accessory protein (IL-1RAcP) also known as Interleukin-1 receptor member 3 (IL-1R3) is a cytokine receptor that 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 the synthesis of the 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 signaling 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 the 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.
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.