Sting

Manufactured by Proteintech

Sourced in United States

The STING protein is a key component of the innate immune system, responsible for detecting the presence of cytosolic DNA and triggering an antiviral immune response. It serves as a critical sensor of foreign or aberrant DNA, playing a crucial role in the activation of the type I interferon signaling pathway.

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Lab products found in correlation

β actin, by Merck Group (6 mentions) Vinculin, by Cell Signaling Technology (4 mentions) Gapdh, by Proteintech (4 mentions) P tbk1, by Cell Signaling Technology (4 mentions) P irf3, by Cell Signaling Technology (3 mentions) Ifi204, by LifeSpan BioSciences (2 mentions) Phospho irf3, by Santa Cruz Biotechnology (2 mentions) Control shrna, by Merck Group (2 mentions) Sting, by Merck Group (2 mentions) Sting, by Cell Signaling Technology (2 mentions) Puromycin, by Merck Group (2 mentions) Hp mlkl, by Abcam (2 mentions) Flag tag (flag), by ABclonal (2 mentions) Western lightening chemiluminescent substrate, by PerkinElmer (2 mentions) Chemidoc imager, by Bio-Rad (2 mentions) Pvdf membrane, by Merck Group (2 mentions) Phosphostop, by Roche (2 mentions) β actin, by Cell Signaling Technology (2 mentions) Ly 6g ly 6c, by BioLegend (1 mentions) Alexa fluor 488 conjugated secondary antibody, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Anti-STING (9 citations) STING (19851-1-AP, (3 citations) STING antibody (2 citations) Anti-STING rabbit antibody (2 citations) Rabbit anti-STING pAb (2 citations) Anti-STING (19851-1-AP) (2 citations)

19 protocols using sting

Immunoprecipitation and Western Blot Analysis

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Cells were treated with cell lysis buffer for Western and IP (Beyotime). The indicated antibodies were added to cell lysates or supernatant, followed by incubation with gentle rocking overnight at 4°C. Then, protein G agarose beads were added to cell lysates, which was incubated with gentle rocking for 4 h at 4°C. Next, samples were eluted in SDS‐PAGE sample loading buffer and boiled. For immunoprecipitation, anti‐FLAG (AE005; ABclonal), STING (19851‐1‐AP; Proteintech) and MLKL (PA5‐102810; Invitrogen) antibodies were used.
The primary antibodies were used including STING (19851‐1‐AP; Proteintech), hp‐STING (S366, 50907; CST), mp‐STING (S365, 72971; CST), p‐TBK1 (S172; CST), TBK1 (38066; CST), IRF3 (4302; Cell Signaling), p‐IRF3 (S396, 29047; CST), mp‐RIPK3 (T231+S232, ab222320; Abcam), mp‐MLKL(S345, ab196436; Abcam), hp‐RIPK3 (S227, ab209384; Abcam), hp‐MLKL (S358, ab187091; Abcam), hMLKL (A19685; ABclonal), mMLKL (37705; CST), hRIPK3 (86671; CST), mRIPK3 (15828; CST), mp‐RIPK1 (S166, 31122; CST), RIPK1 (3493; CST), LC3 (12741; CST), P62 (A7758; ABclonal), β‐actin (4970; CST), β‐Tubulin (AC021; ABclonal), GAPDH (60004‐1‐Ig; Proteintech), FLAG‐tag (AE063; ABclonal), HA‐tag (ab236632; Abcam), MYC‐tag (AE070; ABclonal) and GFP‐tag (AE012; ABclonal).

Zhang X., Wu J., Liu Q., Li X., Yang Y., Wu L., Wu X., Zhao Y, & Ren J. (2023). RIPK3–MLKL necroptotic signalling amplifies STING pathway and exacerbates lethal sepsis. Clinical and Translational Medicine, 13(7), e1334.

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Histological and Immunological Analysis of Lung and Kidney Tissues

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Tissue samples of lung and kidney were fixed in buffered formalin solution (4%) and embedded in paraffin. Tissue sections (5 μm) were deparaffinized, rehydrated, and stained with hematoxylin-eosin. For immunohistochemistry, sections were subjected to an antigen retrieval step, followed by blocking for 1 h at room temperature, then stained with IFI204 (Lifespan), Ly-6G/Ly-6c (BioLegend), and F4/80 (BioLegend) antibodies. Subsequently, specific staining was detected using the UltraSensitive S-P Kit and DAB Detection Kit (Maixin-Bio) according to the manufacturer's directions. For immunofluorescence, cells were stained with phospho-IRF3 (Santa Cruz), IFI204 (Lifespan), STING (Proteintech) primary antibodies, and Alexa Fluor® 488-conjugated secondary antibodies (Invitrogen). Kidney cell apoptosis was analyzed by TUNEL staining using a commercial kit (KeyGEN Biotech). DAPI (1 μg/mL) was used to stain nuclei.

Chen W., Yu S.X., Zhou F.H., Zhang X.J., Gao W.Y., Li K.Y., Liu Z.Z., Han W.Y, & Yang Y.J. (2019). DNA Sensor IFI204 Contributes to Host Defense Against Staphylococcus aureus Infection in Mice. Frontiers in Immunology, 10, 474.

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Assessing the Role of MAVS and STING in HIV-1 Replication

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MDMs (1.2 × 10⁷) were infected with retroviruses encoding shRNAs directed against MAVS, STING, or a control shRNA (Sigma) and a puromycin‐resistance gene in the presence of Vpx. Infected cells were selected by culture in the presence of puromycin for 5 days, and either used in HIV‐1 replication assays or lysed for immunoblot analysis to measure MAVS and STING expression using antibodies to MAVS (Cell Signaling Technology), STING (ProteinTech), vinculin (Cell Signaling Technology), or β‐actin (Sigma).

Dickey L.L., Martins L.J., Planelles V, & Hanley T.M. (2022). HIV‐1‐induced type I IFNs promote viral latency in macrophages. Journal of Leukocyte Biology, 112(5), 1343-1356.

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Western Blot Analysis of STING and IRF3

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Briefly, polyacrylamide gel electrophoresis was used to separate proteins which extracted from tissues or cells, and transferred onto polyvinylidene fluoride membranes. Membranes were incubated with primary antibodies including: STING (1:1000; Proteintech, Chicago, IL, USA), IRF3 (1:1000; Proteintech), p-IRF3 (1:1000; Cell Signaling, Boston, MA, USA), GAPDH (1:3000; Proteintech), and then with HRP-conjugated secondary antibody. At last, enhanced chemiluminescence assay was used to detect the reactions.

Song S., Peng P., Tang Z., Zhao J., Wu W., Li H., Shao M., Li L., Yang C., Duan F., Zhang M., Zhang J., Wu H., Li C., Wang X., Wang H., Ruan Y, & Gu J. (2017). Decreased expression of STING predicts poor prognosis in patients with gastric cancer. Scientific Reports, 7, 39858.

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Western Blot Analysis of Innate Immune Signaling

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Whole-cell extracts were generated by direct lysis with 1× Cell Lysis Buffer (Cell Signaling Technology, #9873) with 1 mM phenylmethylsulphonyl fluoride (PMSF) added immediately before use. Samples with 6× SDS sample buffer added were heated at 100°C for 10 min and resolved by SDS-PAGE and then transferred to a PVDF membrane. The membranes were then examined with primary antibodies, followed by the corresponding HRP-conjugated anti-mouse or anti-rabbit (Proteintech) secondary antibodies. The following antibodies were used: α-tubulin (1 : 1000, Proteintech), cGAS (1 : 1000, Abcepta), TBK1 (1 : 1000, Proteintech), phospho-TBK1 (1 : 1000, CST), STING (1 : 1000, Proteintech), phospho-STING (1 : 1000,CST), IRF3 (1 : 1000, Proteintech), and phospho-IRF3 (1 : 1000, CST).

He X., Xiao Y., Liu S., Deng R., Li Z, & Zhu X. (2022). Predicting the Immune Microenvironment and Prognosis with a NETosis-Related lncRNA Signature in Head and Neck Squamous Cell Carcinoma. BioMed Research International, 2022, 3191474.

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Molecular Markers of Cell Death Pathways

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Histology, immunohistochemistry and immunofluorescence for tissue or cell were performed as previously described.¹³ Primary antibodies were used including hp‐RIPK3 (S227, ab209384; Abcam), hp‐MLKL (S358, ab187091; Abcam), STING (19851‐1‐AP; Proteintech), LC3 (12741; CST) and FLAG‐tag (AE063; ABclonal). Nucleus was stained with DAPI.

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Inhibition of Innate Immune Sensors in HIV-1 Infection

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MDMs (1.2 × 10⁷) were infected with retroviruses encoding shRNAs directed against MAVS, STING, or a control shRNA (Sigma) and a puromycin-resistance gene in the presence of Vpx. Infected cells were selected by culture in the presence of puromycin for five days, and either used in HIV-1 replication assays or lysed for immunoblot analysis to measure MAVS and STING expression using antibodies to MAVS (Cell Signaling Technology), STING (ProteinTech), vinculin (Cell Signaling Technology), or β-actin (Sigma).

Dickey L.L., Martins L.J., Planelles V, & Hanley T.M. (2022). HIV‐1‐induced type I IFNs promote viral latency in macrophages. Journal of Leukocyte Biology, 112(5), 1343-1356.

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MAVS and STING Protein Detection

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1 × 10⁶ MDMs were lysed in 100 μL of NETN buffer (100 mM NaCl, 20 mM Tris-Cl pH 8.0, 0.5 mM EDTA, 0.05% NP-40) with protease inhibitors (cOmplete, Roche) and phosphatase inhibitor (PhosphoStop, Roche), and protein concentration was determined using BCA protein assay kit (Pierce). Proteins were separated on SDS-PAGE gels and transferred to PVDF membranes (Millipore). Membranes were probed with antibodies to MAVS (Cell Signaling Technology), STING (ProteinTech), vinculin (Cell Signaling Technology), or β-actin (Sigma), developed using Western Lightening Chemiluminescent Substrate (Perkin Elmer), and analyzed in a ChemiDoc imager (Bio-Rad Laboratories).

Dickey L.L., Martins L.J., Planelles V, & Hanley T.M. (2022). HIV‐1‐induced type I IFNs promote viral latency in macrophages. Journal of Leukocyte Biology, 112(5), 1343-1356.

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Immunoblot and Immunoprecipitation Protocols

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For immunoblot assays, NPC or HEK293T cells were subjected to lysis in ice-cold low-salt lysis buffer (LSB, 150 mM NaCl, 50 mM Hepes pH 7.5, 1.5 mM MgCl₂,1 mM EDTA, 10% glycerol, 1% Triton X-100) supplemented with 5 mg/mL protease inhibitor cocktail (Roche, Basel, Switzerland). Aliquots of 20–25 μL extracts were subjected to SDS-PAGE. For IP assays, NPC or HEK293T cells were transfected with corresponding expression vectors for indicated times, then FLAG- or Myc-tagged proteins were pulled down using FLAG-beads (Sigma -Aldrich, St. Louis, MO, USA) or Myc-beads (Immuoway, Newark, DE, USA). The following antibodies were used which were directed to: FLAG (Sigma, A8592), β-actin (Sigma, A2228), HA (Roche Applied Science, clone 3F10), Myc (Roche Applied Science, 11814150001), STING (Proteintech, IL, USA, 19851-1-AP), TRIM29 (Proteintech, 17542-1-AP).

Zhang C.X., Huang D.J., Baloche V., Zhang L., Xu J.X., Li B.W., Zhao X.R., He J., Mai H.Q., Chen Q.Y., Zhang X.S., Busson P., Cui J, & Li J. (2020). Galectin-9 promotes a suppressive microenvironment in human cancer by enhancing STING degradation. Oncogenesis, 9(7), 65.

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Immunostaining Protocol for DNA Damage Pathway

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C-176, ethidium bromide (EtBr) and cyclosporin A (CsA) were obtained from Selleck (Houston, TX, USA). 8-OHDG was obtained from MCE (China). Benzalkonium chloride (BAC) was obtained from Sigma‒Aldrich (Louis, MO, USA). Primary antibodies against dsDNA, cGAS, STING, TBK1, p-TBK1, IRF3 and p-IRF3 were obtained from Proteintech (Chicago, IL, USA), Abcam (Cambridge, UK) or CST (Danvers, MA, USA). The HRP-conjugated secondary antibody was purchased from Invitrogen (Carlsbad, CA, USA) (Table S3).

Ouyang W., Wang S., Yan D., Wu J., Zhang Y., Li W., Hu J, & Liu Z. (2023). The cGAS-STING pathway-dependent sensing of mitochondrial DNA mediates ocular surface inflammation. Signal Transduction and Targeted Therapy, 8, 371.

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