Active • Host: E. coli • AA: 138-379 • Tag: N-terminal His • MW: 28.7 kDa
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STING R232 variant (N242A mutant; human, recombinant)

Item No. 40241

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Endoplasmic Reticulum Interferon Stimulator
  • ERIS
  • Mediator of IRF3 Activation
  • MITA
  • Mitochondrial Mediator of IRF3 Activation
  • MPYS
  • Stimulator of Interferon Genes
  • Stimulator of Interferon Response cGAMP Interactor 1
  • STING1
  • N-Terminal Methionine-Proline-Tyrosine-Serine Plasma Membrane Tetraspanner
  • TMEM173
  • Transmembrane Protein 173
Purity
≥80% estimated by SDS-PAGE
Source
Active recombinant human N-terminal His-tagged STING R232 variant (N242A mutant) expressed in E. coli
Amino Acids
138-379
MW
28.7 kDa
Formulation (Request formulation change)
50 mM HEPES, pH 8.0, with 100 mM sodium chloride, and 10% glycerol
UniProt Accession №
Q86WV6
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $649

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    Cayman Chemical
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    Product Description

    Stimulator of interferon genes (STING) is a component of the innate immune response that recognizes and binds to cyclic dinucleotides (CDNs), which either originate from bacteria or are signals of intracellular stress, leading to activation of NF-κB and transcription of immunomodulatory genes, including type I interferon (IFN).1,2,3,4,5 The R232 variant is the most common variant in the human population, found at a frequency of 57.9% in the 1000 Genome Project.6 STING is composed of four transmembrane domains at the N-terminus, a helix α1 domain involved in protein dimerization and ligand sensing, and a cytoplasmic C-terminal domain containing the cyclic dinucleotide-binding domain, as well as the TBK1/IRF1-binding site, TBK1 phosphorylation site, and IRF3 docking site.7 Various mutations in STING either reduce or increase its activity or binding affinity.6,8,9,10 The asparagine-to-alanine substitution at position 242 (N242A) reduces c-di-GMP and 2’3’-cGAMP binding to STING.11,12 Cayman’s STING R232 variant (N242A mutant; human, recombinant) protein can be used for ELISA, enzyme activity assay, and Western blot applications.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Burdette, D.L., Monroe, K.M., Sotelo-Troha, K., et al. STING is a direct innate immune sensor of cyclic-di-GMP. Nature 478(7370), 515-518 (2011).

    2. Sun, L., Wu, J., Du, F., et al. Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway. Science 339(6121), 786-791 (2013).

    3. Wu, J., Sun, L., Chen, X., et al. Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA. Science 339(6121), 826-830 (2013).

    4. Konno, H., Konno, K., and Barber, G.N. Cyclic dinucleotides trigger ULK1 (ATG1) phosphorylation of STING to prevent sustained innate immune signaling. Cell 155(3), 688-698 (2013).

    5. Hopfner, K.-P., and Hornung, V. Molecular mechanisms and cellular functions of cGAS-STING signalling. Nat. Rev. Mol. Cell. Biol. 21(9), 501-521 (2020).

    6. Yi, G., Brendel, V.P., Shu, C., et al. Single nucleotide polymorphisms of human STING can affect innate immune response to cyclic dinucleotides. PLoS One 8(10), e77846 (2013).

    7. Li, Y., Wilson, H.L., and Kiss-Toth, E. Regulating STING in health and disease. J. Inflamm. (Lond) 14, 11 (2017).

    8. Jeremiah, N., Neven, B., Gentili, M., et al. Inherited STING-activating mutation underlies a familial inflammatory syndrome with lupus-like manifestations. J. Clin. Invest. 124(12), 5516-5520 (2014).

    9. Ni, G., Konno, H., and Barber, G.N. Ubiquitination of STING at lysine 224 controls IRF3 activation. Sci. Immunol. 2(11), eaah7119 (2017).

    10. Sauer, J.D., Sotelo-Troha, K., von Moltke, J., et al. The N-ethyl-N-nitrosourea-induced Goldenticket mouse mutant reveals an essential function of Sting in the in vivo interferon response to Listeria monocytogenes and cyclic dinucleotides. Infect. Immun. 79(2), 688-694 (2011).

    11. Shu, C., Yi, G., Watts, T., et al. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Nat. Struct. Mol. Biol. 19(7), 722-724 (2012).

    12. Gao, P., Ascano, M., Zillinger, T., et al. Structure-function analysis of STING activation by c[G(2',5')pA(3',5')p] and targeting by antiviral DMXAA. Cell 154(4), 748-762 (2013).