IL-12 R beta 2 Antibody (918102) [Unconjugated] Summary
| Immunogen |
Mouse myeloma cell line NS0-derived recombinant mouse IL-12 R beta 2
Met1-Asn637 Accession # P97378 |
| Specificity |
Detects mouse IL-12 R beta 2 in direct ELISAs.
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| Source |
N/A
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| Isotype |
IgG2b
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| Clonality |
Monoclonal
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| Host |
Rat
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| Gene |
Il12rb2
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| Endotoxin Note |
<0.10 EU per 1 μg of the antibody by the LAL method.
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Applications/Dilutions
| Dilutions |
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Packaging, Storage & Formulations
| 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 with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
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| Preservative |
No Preservative
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| Reconstitution Instructions |
Reconstitute at 0.5 mg/mL in sterile PBS.
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Notes
Alternate Names for IL-12 R beta 2 Antibody (918102) [Unconjugated]
- IL-12 R beta 2
- IL-12 receptor beta 2
- IL-12 receptor subunit beta-2
- IL12R beta 2
- IL-12R subunit beta-2
- IL12RB2
- IL-12Rb2
- IL-12R-beta-2
- interleukin 12 receptor, beta 2
- interleukin-12 receptor beta-2 chain
- interleukin-12 receptor subunit beta-2
Background
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 complexs 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 overexpression 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).