Recombinant Human IL-10 R beta Fc Chimera Avi Protein, CF New

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-10 R beta

Interleukin-10 Receptor beta (IL-10 R beta ), also known as IL-10 R2 and CRF2-4, is a 60 kDa transmembrane glycoprotein that functions as a co-receptor for several class 2 cytokines including Interleukins-10, -22, -26, -28A/IFN-lambda 2, -28B/IFN-lambda 3, and -29/IFN-lambda (1, 2). IL-10 R beta associates with ligand‑specific receptor subunits to form signaling receptor complexes, e.g. IL-10 R alpha for IL-10 (3, 4), IL-20 R alpha for IL-26 (5, 6), IL-22 R alpha for IL-22 (7, 8), and IL-28 R alpha for IL-28A, IL-28B, and IL-29 (9, 10). IL‑10 R beta is widely expressed, while the associated receptor subunits exhibit differential expression patterns (1). The ligand‑specific subunits are responsible for the divergent functions of these cytokines, encompassing immune suppression, promotion or inhibition of inflammation, mucosal defense, antiviral immunity, and hematopoiesis (1). IL-10 R beta deficient mice lack responsiveness to each of those cytokines. IL-10 R beta contributes to ligand binding, but effective signaling is only triggered in the presence of the ligand‑specific subunit (8, 9, 11). In the case of IL-10, a cytokine dimer binds to two IL‑10 R alpha /IL-10R1 chains, resulting in recruitment of two IL-10 R beta /IL-10R2 chains (3, 12). Some members of the IL-10 family are monomeric cytokines and interact with single molecules of IL-10 R beta and their ligand‑specific subunit (1). Mature human IL-10 R beta consists of a 201 amino acid (aa) extracellular region with two fibronectin type-III domains, a 22 aa transmembrane segment and a 83 aa cytoplasmic domain (13). Within the ECD, human IL-10 R beta shares 75% and 78% aa sequence identity with mouse and rat IL-10 R beta, respectively. Our Avi-tag Biotinylated human IL-10 R beta 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 Development and Differentiation
• Cytokines and Receptors in Allergy and Asthma
• Cytokines and Receptors in Angiogenesis
• Cytokines and Receptors in Tfh Cell Differentiation and Function
• IL-10 Family
• Interferons
• Microglia Homeostasis
• Monocyte Markers
• Receptors in the Jak/STAT Pathway
• Regulatory T Cells (Tregs)