Phospho-STING (Ser366) Antibody (YA9809)
(Synonyms: endoplasmic reticulum IFN stimulator; Endoplasmic reticulum interferon stimulator; ERIS; FLJ38577; hMITA; hSTING; Mediator of IRF3 activation; MITA; Mitochondrial mediator of IRF3 activation; MPYS)
Based on 1 Customer Validation
Phospho-STING (Ser366) Antibody (YA9809) is a Rabbit-derived and non-conjugated IgG Recombinant, Monoclonal antibody, targeting to Phospho-STING (Ser366).
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, Dot Blot, IP
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Reactivity :
Human
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Formulation:
Supplied in PBS (pH7.4), 0.1% BSA, 40% Glycerol, 0.05% Sodium Azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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Dot Blot
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IP
IP: Immunoprecipitation
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|---|---|---|---|
| Dilution Ratio | 1:2000 | 1:2000 | 1-2μg per 100-500μg Total protein |
Product Details
Phospho-STING (Ser366) Antibody (YA9809) is a Rabbit-derived and non-conjugated IgG Recombinant, Monoclonal antibody, targeting to Phospho-STING (Ser366).
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Host Rabbit
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Species ReactivityHuman
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Calculated Molecular Weight Predicted band size: 42 kDa
Synthetic phospho-peptide corresponding to residues surrounding Ser366 of Human STING.
Endogenous
affinity purified
Non-conjugated
Phosphorylated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH7.4), 0.1% BSA, 40% Glycerol, 0.05% Sodium Azide.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
STING is a Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, cyclic UMP-AMP (2',3'-cUAMP), and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol. Upon binding to c-di-GMP, cUAMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state. Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'-cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP. The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, which adopts an organized free-ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation. In addition to promote the production of type I interferons, plays a direct role in autophagy. Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome. Promotes autophagy by acting as a proton channel that directs proton efflux from the Golgi to facilitate MAP1LC3B/LC3B lipidation. The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation. Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (By similarity). May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons. May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (By similarity). Involved in intercellular immune signaling. Cross-activated by 2',3'-cGAMP previously generated in virus-infected cells, triggers type I interferon signaling in macrophages and uninfected neighboring cells to propagate and amplify the antiviral immune response[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33].
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Subcellular Localization
Endoplasmic reticulum membrane; Cytoplasm, perinuclear region; Endoplasmic reticulum-Golgi intermediate compartment membrane; Golgi apparatus membrane; Cytoplasmic vesicle, autophagosome membrane; Mitochondrion outer membrane; Cell membrane
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Expression
Tissue_Specificity: Ubiquitously expressed. Expressed in skin endothelial cells, alveolar type 2 pneumocytes, bronchial epithelium and alveolar macrophages. -
Isoforms & Post-Translational Modification
Phospho-STING has an amino acid length of 379, molecular weight is 42193 Da.
Phosphorylation by TBK1 leads to activation and production of IFN-beta. Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, STING1 is phosphorylated by TBK1 at Ser-366 in the pLxIS motif. The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines. Dephosphorylation by PPP6C leads to inactivation and decreased production of IFN-beta. Phosphorylation at Ser-358 is also required to activate IRF3. Phosphorylation at Ser-355 by MAP3K7/TAK1 facilitates its interaction with STEEP1, promoting STING1 translocation to COPII vesicles. -
Subunit
Homodimer; forms a homodimer in absence of cyclic nucleotide (c-di-GMP or cGAMP); 'Lys-63'-linked ubiquitination at Lys-150 is required for homodimerization.
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SwissProt ID
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Synonyms
endoplasmic reticulum IFN stimulator; Endoplasmic reticulum interferon stimulator; ERIS; FLJ38577; hMITA; hSTING; Mediator of IRF3 activation; MITA; Mitochondrial mediator of IRF3 activation; MPYS
Documentation
References
[1]. Ishikawa H, et al. STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling. Nature. 2008 Oct 2;455(7213):674-8. [Content Brief]
[2]. Zhong B, et al. The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity. 2008 Oct 17;29(4):538-50. [Content Brief]
[3]. Sun W, et al. ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization. Proc Natl Acad Sci U S A. 2009 May 26;106(21):8653-8. [Content Brief]
[4]. Ishikawa H, et al. STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity. Nature. 2009 Oct 8;461(7265):788-92. [Content Brief]
[5]. Orzalli MH, et al. Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein. Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):E3008-17. [Content Brief]
[6]. Zhang X, et al. Cyclic GMP-AMP containing mixed phosphodiester linkages is an endogenous high-affinity ligand for STING. Mol Cell. 2013 Jul 25;51(2):226-35. [Content Brief]
[7]. Gao P, et al. Structure-function analysis of STING activation by c[G(2',5')pA(3',5')p] and targeting by antiviral DMXAA. Cell. 2013 Aug 15;154(4):748-62. [Content Brief]
[8]. Zhang M, et al. USP18 recruits USP20 to promote innate antiviral response through deubiquitinating STING/MITA. Cell Res. 2016 Dec;26(12):1302-1319. [Content Brief]
[9]. Haag SM, et al. Targeting STING with covalent small-molecule inhibitors. Nature. 2018 Jul;559(7713):269-273. [Content Brief]
[10]. Shang G, et al. Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP. Nature. 2019 Mar;567(7748):389-393. [Content Brief]
[11]. Domizio JD, et al. The cGAS-STING pathway drives type I IFN immunopathology in COVID-19. Nature. 2022 Mar;603(7899):145-151. [Content Brief]
[12]. Lu D, et al. Activation of STING by targeting a pocket in the transmembrane domain. Nature. 2022 Apr;604(7906):557-562. [Content Brief]
[13]. Lee GM, et al. Varicella-Zoster Virus ORF39 Transmembrane Protein Suppresses Interferon-Beta Promoter Activation by Interacting with STING. J Microbiol. 2023 Feb;61(2):259-270. [Content Brief]
[14]. Ma M, et al. TAK1 is an essential kinase for STING trafficking. Mol Cell. 2023 Nov 2;83(21):3885-3903.e5. [Content Brief]
[15]. Lee KG, et al. Bruton's tyrosine kinase phosphorylates DDX41 and activates its binding of dsDNA and STING to initiate type 1 interferon response. Cell Rep. 2015 Feb 24;10(7):1055-65. [Content Brief]
[16]. Wang W, et al. RNF39 facilitates antiviral immune responses by promoting K63-linked ubiquitination of STING. Int Immunopharmacol. 2024 Dec 5;142(Pt A):113091. [Content Brief]
[17]. Kranzusch PJ, et al. Ancient Origin of cGAS-STING Reveals Mechanism of Universal 2',3' cGAMP Signaling. Mol Cell. 2015 Sep 17;59(6):891-903. [Content Brief]
[18]. Burdette DL, et al. STING is a direct innate immune sensor of cyclic di-GMP. Nature. 2011 Sep 25;478(7370):515-8. [Content Brief]
[19]. Wu J, et al. Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA. Science. 2013 Feb 15;339(6121):826-30. [Content Brief]
[20]. Diner EJ, et al. The innate immune DNA sensor cGAS produces a noncanonical cyclic dinucleotide that activates human STING. Cell Rep. 2013 May 30;3(5):1355-61. [Content Brief]
[21]. Ablasser A, et al. cGAS produces a 2'-5'-linked cyclic dinucleotide second messenger that activates STING. Nature. 2013 Jun 20;498(7454):380-4. [Content Brief]
[22]. Bridgeman A, et al. Viruses transfer the antiviral second messenger cGAMP between cells. Science. 2015 Sep 11;349(6253):1228-32. [Content Brief]
[23]. Li Y, et al. cGLRs are a diverse family of pattern recognition receptors in innate immunity. Cell. 2023 Jul 20;186(15):3261-3276.e20. [Content Brief]
[24]. Tanaka Y, et al. STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway. Sci Signal. 2012 Mar 6;5(214):ra20. [Content Brief]
[25]. Liu S, et al. Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation. Science. 2015 Mar 13;347(6227):aaa2630. [Content Brief]
[26]. Zhang C, et al. Structural basis of STING binding with and phosphorylation by TBK1. Nature. 2019 Mar;567(7748):394-398. [Content Brief]
[27]. Srikanth S, et al. The Ca(2+) sensor STIM1 regulates the type I interferon response by retaining the signaling adaptor STING at the endoplasmic reticulum. Nat Immunol. 2019 Feb;20(2):152-162. [Content Brief]
[28]. Shi H, et al. Molecular basis for the specific recognition of the metazoan cyclic GMP-AMP by the innate immune adaptor protein STING. Proc Natl Acad Sci U S A. 2015 Jul 21;112(29):8947-52. [Content Brief]
[29]. Liu D, et al. STING directly activates autophagy to tune the innate immune response. Cell Death Differ. 2019 Sep;26(9):1735-1749. [Content Brief]
[30]. Gui X, et al. Autophagy induction via STING trafficking is a primordial function of the cGAS pathway. Nature. 2019 Mar;567(7747):262-266. [Content Brief]
[31]. Tan JX, et al. PtdIns(3,5)P(2) is an endogenous ligand of STING in innate immune signalling. Nature. 2026 Apr;652(8109):490-498. [Content Brief]
[32]. Li J, et al. Regulation of STING activation by phosphoinositide and cholesterol. Nature. 2026 Apr;652(8109):499-507. [Content Brief]
[33]. Liu B, et al. Human STING is a proton channel. Science. 2023 Aug 4;381(6657):508-514. [Content Brief]
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