Recombinant Human IL-27 Ra/WSX-1/TCCR Fc Avi-tag Protein, CF

Recombinant Human IL-27 Ra/WSX-1/TCCR Fc Avi-tag Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

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.

Background: IL-27 R alpha/WSX-1/TCCR

IL‑27 R alpha (also known as WSX‑1 and TCCR) is a 96 ‑ 100 kDa member of the type I, group 2 cytokine receptor family (1, 2, 3, 4, 5, 6). Mature IL‑27 R alpha  is a type I transmembrane glycoprotein that contains a 484 amino acid (aa) extracellular region, a 21 aa transmembrane segment and a 99 aa cytoplasmic domain. Consistent with type I cytokine receptors, the extracellular region contains four positionally conserved cysteine residues, a WSxWS motif (for receptor folding and ligand binding), and three fibronectin type III repeats. The intracellular domain contains a "box‑1" motif that may be involved with Janus kinases (3). One potential alternate splice form has been hypothesized that involves a 58 aa addition to the cytoplasmic domain and, based on mouse, a soluble 33 kDa splice form that shows a 20 aa substitution for aa 257 ‑ 636 may also occur in human (3, 7). The human IL‑27 R alpha extracellular region shares 63% amino acid identity with the mouse IL‑27 R alpha extracellular domain (2, 3). IL‑27 R alpha is expressed in mast cells, endothelial cells, NK cells, macrophages, monocytes, B cells, dendritic cells, and naïve T cells (1, 2, 4, 8). Typical of other class I cytokine receptor chains, the ligand binding IL‑27 R alpha molecule is known to heterodimerize with a signal‑transducing subunit (gp130) to form a functional IL‑27 receptor (9, 10). In addition, IL‑27 R alpha is reported to complex with CNTFR alpha and gp130 form a humanin receptor on neurons (7, 11), and to complex with gp130 and IL‑6 R to form a receptor for a p28:CLF heterodimeric cytokine on lymphocytes (12). Studies using IL‑27 R alpha /WSX‑1^‑/‑ mice reveal that IL‑27 has the ability to suppress T cell activity during infection, and to mediate an inhibition of both type 1 and type 2 T cell immunity (4, 13, 14). In particular, IL‑27 is known to act on naïve T cells, blocking their differentiation into a Th17 phenotype. Notably, cells committed to a Th17 phenotype, although they express a functional IL‑27 receptor, are unresponsive to the effects of IL‑27 (15). Activated T cells that are CD4⁺ and CD8⁺, and which express the IL‑27 receptor, can be induced by IL‑27 to form a double‑positive CD25⁺ FoxP3^‑ IFN‑ gamma plus IL‑10 secreting phenotype that both promotes and suppresses the inflammatory response (16). Our Avi-tag Biotinylated human IL-27 R alpha  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.

Related Research Areas

• B Cell Activation
• B Cell Development and Differentiation
• B Cell Markers
• Dendritic Cell Activation
• IL-12 Family
• Isolation, Culture, and Identification of Natural Killer Cells
• Mast Cells
• Monocyte Markers
• Receptors in the Jak/STAT Pathway
• T Cell Cytokine Signaling
• Th1 Cells