Recombinant Human IL-12 R beta 2 Fc Avi-tag Protein, CF
Recombinant Human IL-12 R beta 2 Fc Avi-tag Protein, CF SummaryLearn more about Avi-tag Biotinylated Proteins
|Human IL-12 RB2|
Accession # Q99665.1
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.
When Recombinant Human IL-12 Protein (Catalog# 219-IL) is immobilized at 1.0 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human IL‑12R beta 2 Fc Chimera Avi-tag (Catalog # AVI10930) that produces 50% of the optimal binding response is 0.15‑1.50 μg/mL.
1 μg/lane of Biotinylated Recombinant Human IL‑12 R beta 2 Fc Chimera Avi-tag Protein (Catalog # AVI10930) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized bysilver staining, showing bands at 115-130 kDa and 230-260 kDa, respectively.
Background: IL-12 R beta 2
IL-12 Receptor beta 2 (IL-12 R beta 2) is a member of the cytokine receptor superfamily and when combined with the highly homologous IL-12 R beta 1, forms the heterodimeric high affinity IL-12 receptor complex. Both receptors are type I transmembrane glycoproteins with homology to gp130, the common receptor beta -chain of the IL-6-like cytokine superfamily (ref). Mature human IL-12 R beta 2 consists of an extracellular domain (ECD) with five fibronectin type III (FnIII) domains and a WSXWS motif, a single transmembrane domain and a cytoplasmic region with a Box 1 motif and a tyrosine phosphorylation site that both mediate intracellular signaling (1). The ECD of human IL-12 R beta 2 shares 69% and 67% amino acid sequence identity with mouse and rat IL-12 R beta 2, respectively. Human and mouse IL-12 R beta 2 do not bind cross-species IL-12 (2). Alternative splicing creates a IL-12 R beta 2 with a shortened and altered cytoplasmic sequence (3). IL-12 R beta 1 and IL-12 R beta 2 are receptors for the IL-12 family, which includes IL-12, IL-23, IL-27 and IL-35 and they activate the Janus kinase (JAK)–STAT (signal transducer and activator of transcription) pathway of signal transduction (4). The receptor chains are utilized by the cytokines in different combinations, with IL-12RB2 binding to IL-12 and IL-35 (5). Unlike IL-12RB1, which is constitutive in T cells, NK cells and B cells, IL-12 R beta 2 expression is more limited (2). IL-12 R beta 2 is expressed following STAT1 activation by IFN-gamma, IL-27 and/or T cell receptor stimulation of naïve T cells, allowing IL-12 to promote Th1, but not Th2, differentiation (6-8). Among B cells, surface expression is limited to naïve germinal center and memory B cells, and myeloma cells (2). Deletion of mouse IL-12 R beta 2 causes systemic overexpression of IL-6, accelerated maturation of thymocytes, deficient regulatory T cell maturation and function, and reduced splenic T cell apoptosis (2, 9-11). These mice are susceptible to autoimmune diseases such as experimental autoimmune encephalitis and spontaneous B cell malignancies (2, 9-11). In humans, polymorphism of the IL-12 R beta 2 gene is associated with systemic sclerosis (12). Our Avi-tag Biotinylated IL-12 R beta 2 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.
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