Preparation And Storage
Recommended Assay Procedures
The biotinylated 114 antibody (Cat. No. 551973) can be used for the immunofluorescent staining (≤ 1 µg antibody/10e6 cells) and flow cytometric analysis of mouse T cells and NK cells to measure their expressed levels of surface IL-12Rβ1. An appropriate purified immunoglobulin isotype control is clone G155-179 (Cat. No. 553455).
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
The 114 monoclonal antibody specifically binds to mouse CD212 (the β1 subunit of IL-12Rβ1), originally termed IL-12Rβ, of the mouse IL-12 receptor complex. The IL-12Rβ1 subunit associates with a β2 subunit to form a heterodimeric IL-12 receptor complex. Each one of the IL-12R subunits exhibits low affinity for IL-12, but in combination, they bind IL-12 with high affinity. The IL-12Rβ1 subunit interacts primarily with IL-12 p40 whereas the IL-12Rβ2 binds both to IL-12 p40 and IL-12 p35. IL-12Rβ1 is required for high affinity binding of IL-12 but IL-12Rβ2 is required for signaling. IL-12Rβ1 has more recently been described to bind IL-23, a heterodimer formed of the p40 subunit from IL-12, and p19. The cytoplasmic regions of the β1 and β2 subunits contain the box1 and box2 motifs found in other cytokine receptors such as gp130, LIFR and G-CSFR. IL-12Rβ1 are primarily expressed by activated T cells and NK cells. Experiments with IL-12Rβ1 deficient mice have shown that IL-12Rβ1 is necessary for mouse T and NK cell responsiveness to IL-12 p75. The 114 antibody was generated by immunizing IL-12Rβ1 deficient mice of (129 x BALB/c)F1 background with mouse Ba/F3 cells that were stably transfected with IL-12Rβ1.
Development References (8)
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Chua AO, Wilkinson VL, Presky DH, Gubler U. Cloning and characterization of a mouse IL-12 receptor-beta component. J Immunol. 1995; 155(9):4286-4294. (Clone-specific). View Reference
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Gately MK, Renzetti LM, Magram J, et al. The interleukin-12/interleukin-12-receptor system: role in normal and pathologic immune responses. Annu Rev Immunol. 1998; 16:495-521. (Biology). View Reference
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Presky DH, Minetti LJ, Gillessen S, et al. Analysis of the multiple interactions between IL-12 and the high affinity IL-12 receptor complex. J Immunol. 1998; 160(5):2174-2179. (Biology). View Reference
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Presky DH, Yang H, Minetti LJ, et al. A functional interleukin 12 receptor complex is composed of two beta-type cytokine receptor subunits. Proc Natl Acad Sci U S A. 1996; 93(4):14002-14007. (Clone-specific). View Reference
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Stahl N, Yancopoulos GD. The alphas, betas, and kinases of cytokine receptor complexes. Cell. 1993; 74(4):587-590. (Biology). View Reference
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Wang X, Wilkinson VL, Podlaski FJ, et al. Characterization of mouse interleukin-12 p40 homodimer binding to the interleukin-12 receptor subunits. Eur J Immunol. 1999; 29(6):2007-2013. (Biology). View Reference
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Wu C, Ferrante J, Gately MK, Magram J. Characterization of IL-12 receptor beta1 chain (IL-12Rbeta1)-deficient mice: IL-12Rbeta1 is an essential component of the functional mouse IL-12 receptor. J Immunol. 1997; 159(4):1658-1665. (Biology). View Reference
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Wu C, Wang X, Gadina M, O'Shea JJ, Presky DH, Magram J. IL-12 receptor beta 2 (IL-12R beta 2)-deficient mice are defective in IL-12-mediated signaling despite the presence of high affinity IL-12 binding sites. J Immunol. 2000; 165(11):6221-6228. (Biology). View Reference
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.
