Recombinant Human STING/TMEM173 His-tag Protein, CF Summary
| Details of Functionality |
Measured by its binding ability in a functional ELISA. Recombinant
Human STING/TMEM173 His-tag (Catalog # 11821-ST) binds Human STING/TMEM173 Antibody
(Catalog #
MAB7169) with an ED50 of <50.0 ng/mL. |
| Source |
E. coli-derived human STING/TMEM173 protein Leu139 - Ser379, with an N-terminal Met-His6 tag |
| N-terminal Sequence |
Met-His |
| Protein/Peptide Type |
Recombinant Proteins |
| Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
28 kDa. 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. |
| SDS-PAGE |
28-35 kDa, under reducing conditions. |
Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 6 months from date of receipt, -20 to -70 °C as supplied.
- 3 months, -20 to -70 °C under sterile conditions after opening.
|
| Buffer |
Supplied as a 0.2 μm filtered solution in Tris, NaCl, DTT and Glycerol with Trehalose. |
| Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human STING/TMEM173 His-tag Protein, CF
Background
Stimulator of interferon genes (STING) is a critical innate immune adaptor protein that mediates cellular responses to cytosolic DNA and cyclic dinucleotide signaling, playing a central role in host defense, inflammation, and immune surveillance. STING is encoded by the TMEM173 gene and is primarily localized to the endoplasmic reticulum membrane, where it functions as a key signaling hub downstream of DNA sensors such as cyclic GMP–AMP synthase (cGAS) (1). Under basal conditions, STING remains in an inactive state; however, detection of cytosolic double-stranded DNA leads to production of cyclic GMP–AMP (cGAMP), which directly binds and activates STING (2). Human STING is a ~42 kDa transmembrane protein composed of four N-terminal transmembrane helices, a cytosolic ligand-binding domain, and a C-terminal tail required for downstream signaling (3). Upon ligand binding, STING undergoes conformational changes and translocates from the endoplasmic reticulum to the Golgi apparatus, where it recruits and activates TANK-binding kinase 1 (TBK1) and interferon regulatory factor 3 (IRF3) (2, 4). This results in robust induction of type I interferons and other inflammatory cytokines, establishing an antiviral state and promoting innate and adaptive immune responses (1, 3). In addition to its canonical role in antiviral immunity, STING has broader functions in cancer biology, autophagy, and cellular stress responses. STING signaling can promote antitumor immunity by enhancing dendritic cell activation and T cell priming, but chronic or dysregulated activation may contribute to inflammatory diseases and autoimmunity (4, 5). STING has also been implicated in noncanonical processes, including regulation of apoptosis, senescence, and metabolic pathways, highlighting its role as a multifunctional signaling regulator (3, 5). Genetic and pharmacological studies have demonstrated that altered STING activity is associated with a range of human diseases, including autoinflammatory disorders such as STING-associated vasculopathy with onset in infancy (SAVI), as well as cancer and infectious diseases (2, 6). Consequently, STING has emerged as a major therapeutic target, with agonists being developed for cancer immunotherapy and vaccine adjuvants, and antagonists for treatment of autoimmune and inflammatory conditions (6, 7). Recombinant human STING is therefore an essential research reagent for studies of innate immune signaling, protein–ligand interactions, cyclic dinucleotide recognition, inflammation biology, and therapeutic discovery targeting immune modulation and host defense pathways.
- Ishikawa, H. and Barber, G.N. (2008) Nature 455:674.
- Chen, Q. et al. (2016) Nat. Immunol. 17:1142.
- Shang, G. et al. (2019) Nat. Struct. Mol. Biol. 26:103.
- Hopfner, K.P. and Hornung, V. (2020) Nat. Rev. Mol. Cell Biol. 21:501.
- Decout, A. et al. (2021) Nat. Rev. Immunol. 21:548.
- Liu, Y. et al. (2014) N. Engl. J. Med. 371:507.
- Corrales, L. and Gajewski, T.F. (2015) Immunity 42:561.
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