Recombinant Human IL-4R alpha Fc Chimera Avi-tag Protein, CF Summary
|Human IL-4R alpha|
Accession # P24394.1
Disulfide-linked homodimer, Biotinylated via Avi-tag
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 250 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-4R alpha Fc Chimera Avi-tag (Catalog # AVI7700) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 73-82 kDa and 145 -165 kDa, respectively.
Background: IL-4R alpha
Interleukin 4 Receptor alpha (IL-4R alpha ), also known as CD124 and BSF receptor, is a widely expressed 140 kDa transmembrane glycoprotein in the class I cytokine receptor family. IL-4R alpha plays an important role in Th2-biased immune responses, alternative macrophage activation, mucosal immunity, allergic inflammation, tumor progression, and atherogenesis (1-5). Mature human IL-4R alpha consists of a 207 amino acid (aa) extracellular domain (ECD) that contains a cytokine binding region and one fibronectin type III domain, a 24 aa transmembrane segment, and a 569 aa cytoplasmic domain that contains one Box 1 motif and one ITIM motif (6, 7). Within the ECD, human IL-4R alpha shares 51% aa sequence identity with mouse and rat IL-4R alpha. Soluble forms of IL-4R alpha, generated by alternate splicing or proteolysis, retain ligand binding properties and inhibit IL-4 bioactivity (8-11). IL-4R alpha is a component of two distinct receptor complexes and shows species selectivity between human and mouse (6). It can associate with the common gamma chain ( gamma c) to form the IL-4 responsive type I receptor in which gamma c increases the affinity for IL-4 and enables signaling (12, 13). It can alternatively associate with IL-13R alpha 1 to form the type II receptor which is responsive to both IL-4 and IL-13 (14, 15). The use of shared receptor components contributes to the overlapping biological effects of IL-4 and IL-13 as well as other cytokines that utilize gamma c (i.e. IL-2, IL-7, IL-9, IL-15, and IL-21) (16, 17).
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