Recombinant Human IL-12 R beta 2 Fc Chimera Protein, CF Summary
R beta 2
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 (Catalog # 219-IL) is immobilized at 0.5 µg/mL, Recombinant Human IL-12 R beta 2 Fc Chimera (Catalog # 1959-B2B) binds with an ED50 of 0.015-0.09 µg/mL.
1 μg/lane of Recombinant Human IL‑12 R beta 2 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silverstaining, showing bands at 112-133 kDa and 220-260 kDa, respectively.
Background: IL-12 R beta 2
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 type I transmembrane proteins within the cytokine receptor superfamily (1, 2). Its ligand, IL-12, is a disulfide-linked dimer 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 862 amino acid (aa) human IL-12 R beta 2 includes a 23 aa signal peptide, a 599 aa extracellular domain (ECD) with five fibronectin type III (Fn III) domains, 8 potential N-glycosylation sites, and a WSXWS motif, a 21 aa transmembrane domain and a 219 aa cytoplasmic region with a Box 1 motif and a tyrosine phosphorylation site that both mediate intracellular signaling (3). Human IL-12 R beta 2 ECD shares 69%, 67%, 79%, 81% and 82% aa sequence identity with mouse, rat, canine, porcine and bovine IL-12 R beta 2, respectively. Human and mouse IL-12 R beta 2 do not bind cross-species IL-12 (2). A human alternatively spliced 659 aa form contains a shortened, altered cytoplasmic sequence (4). Unlike IL-12 R beta 1, 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 (5-7). 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, 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).
- Presky, D.H. et al. (1996) Proc. Natl. Acad. Sci. USA 93:14002.
- Pistoia, V. et al. (2009) J. Clin. Oncol. 27:4809.
- Zou, J. et al. (1997) J. Biol. Chem. 272:6073.
- SwissProt accession # Q99665
- Rogge, L. et al. (1997) J. Exp. Med. 185:825.
- Becskei, A. and M.J. Grusby (2007) FEBS Lett. 581:5199.
- Szabo, S.J. et al. (1997) J. Exp. Med. 185:817.
- Zhao, Z. et al. (2008) J. Immunol. 181:3870.
- Gran, B. et al. (2010) Exp. Mol. Pathol. 89:126.
- Airoldi, I. et al. (2005) Blood 106:3846.
- Bossini-Castillo, L. et al. (2012) Hum. Mol. Genet. 21: 926
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