Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. When Recombinant Mouse (rm) IL‑12 R beta 2 Fc Chimera is immobilized at 0.5 μg/mL (100 μL/well), the concentration of rmIL-12 that produces 50% of the optimal binding response is found to be approximately 4 ‑ 20 ng/mL. |
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Source | Mouse myeloma cell line, NS0-derived mouse IL-12 R beta 2 protein
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Accession # | |||||||
N-terminal Sequence | Asn24 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | Il12rb2 |
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Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 95.7 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 125-145 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in PBS. |
The high‑affinity IL‑12 receptor complex includes the 100 kDa IL‑12 receptor beta 1 (IL‑12 R beta 1) and the 130 kDa IL‑12 Receptor beta 2 (IL‑12 R beta 2) subunits, both of which are type I transmembrane proteins that belong to the cytokine receptor superfamily (1, 2). The complex's ligand, IL‑12, is a disulfide‑linked heterodimer composed of 35 kDa (IL‑12 alpha p35) and 40 kDa (IL‑12 beta p40) subunits. IL‑12 R beta 2 binds IL‑12 alpha and signals through Jak2, while IL‑12 R beta 1 binds IL‑12 beta and signals through Tyk2 (3). IL‑12 R beta 1 is also a subunit of the IL‑23 receptor complex (3). The 874 amino acid (aa) mouse IL‑12 R beta 2 precursor includes a 23 aa signal peptide, a 614 aa extracellular domain (ECD), a 21 aa transmembrane segment and a 216 aa cytoplasmic region. The ECD possesses one C2‑type Ig‑like domain, five fibronectin type III (Fn III) repeats, 14 potential N‑glycosylation sites, and a WSXWS motif, while the cytoplasmic region contains a Box 1 motif and three tyrosine phosphorylation sites that presumably mediate intracellular signaling (3). The mouse IL‑12 R beta 2 ECD shares 91% aa sequence identity with rat IL‑12 R beta 2, and 68% with human, porcine and bovine IL‑12 R beta 2. Human and mouse IL‑12 R beta 2 do not bind cross‑species IL‑12 (2). A 734 aa mouse isoform that lacks aa 363‑503 within the Fn III domains is reported (4). Unlike IL‑12 R beta 1, which is constitutively expressed on T cells, NK cells and B cells, IL‑12 R beta 2 expression is more restricted (2). On naïve T cells, IL‑12 R beta 2 is expressed following STAT1 activation by IFN‑ gamma , IL‑27 and/or T cell receptor ligation. This up‑regulation allows IL‑12 to promote Th1, but not Th2, differentiation (5‑7). Among B cells, surface expression is limited to naïve germinal center and memory B cells, and myeloma cells (2). Deletion of IL‑12 R beta 2 causes systemic over-expression of IL‑6, accelerated maturation of thymocytes, deficient regulatory T cell maturation and function, and reduced splenic T cell apoptosis (2, 8-10). These mice are susceptible to autoimmune diseases such as experimental autoimmune encephalitis and spontaneous B cell malignancies (2, 8-10). In humans, polymorphism of the IL‑12 R beta 2 gene is associated with systemic sclerosis (11).
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