Recombinant Human IL-18 R beta/IL-1 R7 Fc Avi Protein, CF Summary
|Human IL-18 R beta /IL-1 R7|
Accession # O95256.1
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 μg/lane of Biotinylated Recombinant Human IL‑18 R beta /IL‑1 R7 Fc Chimera Avi-tag Protein (Catalog # AVI118) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 87-97 kDa and 175-195 kDa, respectively.
Background: IL-18 R beta/IL-1 R7
IL-18, originally described as an interferon-gamma inducing factor (IGIF), is a member of the IL-1 family of cytokines that has multiple immunoregulatory functions. It has potent IFN-gamma inducing activities and plays a key role in the activation of T helper type 1 (Th1) responses. The functional IL-18 receptor complex consists of two components, the IL-18 R alpha (IL-1 R5) and IL-18 R beta (also termed IL-1 R7 and AcPL) subunits. Both subunits are members of the IL-1 receptor superfamily. Although IL-18 R alpha by itself binds IL-18 with low-affinity and IL-18 R beta does not bind IL-18 in vitro, co-expression of IL-18 R alpha and IL-18 R beta is required for high-affinity binding and IL-18 responsiveness. Human IL-18 R beta cDNA encodes a 599 amino acid (aa) residue precursor type I membrane protein with a 14 aa signal peptide, a 342 aa extracellular region containing three immunoglobulin-like domains, a single transmembrane domain and a 222 aa cytoplasmic domain. Human and mouse IL-18 R beta share 65% aa sequence identity. The expression of IL-18 R beta parallels that of IL-18 R alpha and is detected in numerous tissues including lung, spleen, leukocytes and colon. Our Avi-tag Biotinylated IL-18 R beta /IL-1R7 Fc Chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
- Born, T.L. et al. (1998) J. Biol. Chem. 273:29445.
- Okamura, H. et al. (2000) in Cytokine Reference, Vol. 2:1605, Academic Press.
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