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Anti rig 1

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Anti-RIG-I is a monoclonal antibody that recognizes the RIG-I (Retinoic Acid-Inducible Gene I) protein. RIG-I is a cytoplasmic pattern recognition receptor that plays a crucial role in the innate immune response to viral infections by detecting the presence of viral RNA in the cytoplasm.

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Lab products found in correlation

Anti flag, by Merck Group (4 mentions) Peroxidase conjugated secondary antibody, by GE Healthcare (2 mentions) Anti gst, by Merck Group (2 mentions) Amersham imager, by GE Healthcare (2 mentions) Anti trim25, by BD (2 mentions) Glutathione conjugated sepharose beads, by GE Healthcare (2 mentions) Pvdf membrane, by Bio-Rad (2 mentions) Anti actin, by Merck Group (2 mentions) Protease inhibitor cocktail, by Roche (2 mentions) Anti ha, by Merck Group (2 mentions) Anti v5, by Merck Group (2 mentions) Anti phospho stat1 y701, by Cell Signaling Technology (2 mentions) Anti phospho irf3 s386, by GeneTex (2 mentions) Ag 20b 0009 c100, by Merck Group (2 mentions) Anti phospho rig 1 ser8, by Abnova (2 mentions) Anti khsrp, by Cell Signaling Technology (2 mentions) Anti cox 4, by Cell Signaling Technology (2 mentions) Anti rig 1, by Merck Group (2 mentions) Anti β actin, by Cell Signaling Technology (2 mentions) Anti flag m2, by Merck Group (2 mentions)

Spelling variants of this product

Mouse anti-RIG-I (2 citations)

6 protocols using anti rig 1

1

Immunoblotting of Interferon Signaling

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Cells were lysed in RIPA buffer (20 mM Tris pH 7.5, 2 mM EDTA, 150 mM NaCl, 1 % NP40, 1 % SDS, 0.1 % TritonX100, 0.25 % Na-Deoxychalate, plus protease inhibitor) and the samples were incubated at 95 °C for 5 min. Protein lysates were separated on 10 % SDS-PAGE gels and transferred onto polyvinylidene difluoride (PVDF) membranes. As primary antibodies we used anti-Mx (mouse, M143 [31 (link)]), anti-RIG-I (mouse, AdipoGen), and anti-beta-actin (mouse, AC-15, Sigma-Aldrich). Primary antibodies were detected with peroxidase-conjugated secondary antibodies (GE Healthcare).
Schilling M., Vaughan-Jackson A., James W, & McKeating J.A. (2023). Hypoxia dampens innate immune signalling at early time points and increases Zika virus RNA levels in iPSC-derived macrophages. The Journal of General Virology, 104(8), 001885.
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2

Western Blot Analysis of Innate Immune Proteins

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Cells were lysed in YG-lysis buffer (10 mM Trizma, 50 mM NaCl, 30 mM sodium pyrophosphate, 5 mM sodium fluoride, 5 μM ZnCl2, 10% NP40, plus protease inhibitor) and the samples were incubated at 95 °C for 5 min. Protein lysates were separated on 10% SDS-PAGE gels and transferred onto polyvinylidene difluoride (PVDF) membranes. As primary antibodies we used anti-MDA5 (mouse, [13 (link)]), anti-Mx (mouse; M143 [32 (link)]), anti-PARP (rabbit, cell signaling), anti-RIG-I (mouse, AdipoGen), anti-IRF3 (D6I4C, rabbit, cell signaling), anti-p-IRF3-S396 (4D4G, rabbit, cell signaling), anti-ZIKV NS3 and anti-ZIKV NS5 sera (kind gift from A. Merits, Tartu) and anti-beta-actin-HRP (clone AC-15, Sigma-Aldrich). Detection of the primary antibodies was performed by the use of peroxidase-conjugated secondary antibodies (GE Healthcare).
Schilling M., Bridgeman A., Gray N., Hertzog J., Hublitz P., Kohl A, & Rehwinkel J. (2020). RIG-I Plays a Dominant Role in the Induction of Transcriptional Changes in Zika Virus-Infected Cells, which Protect from Virus-Induced Cell Death. Cells, 9(6), 1476.
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3

Immunoblotting Analysis of Ubiquitination

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Pelleted cells were lysed in NP-40 buffer (50 mM HEPES [pH 7.4], 150 mM NaCl, 1% [v/v] NP-40, and protease inhibitor cocktail [Roche]), followed by centrifugation at 13,000 rpm for 25 min. Lysates were mixed with a 50% slurry of glutathione-conjugated Sepharose beads (GE Healthcare), and the binding reaction was incubated for 3 hr at 4°C. Precipitates were washed extensively with lysis buffer. Proteins bound to the beads were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane (Bio-Rad). Immunoblots were performed with anti-Ub (1:5,000; P4D1; Santa Cruz), anti-FLAG (1:2,000; Sigma), anti-GST (1:2,000; Sigma), anti-RIG-I (1:1,000; Adipogen), anti-TRIM25 (1:2,000; BD Biosciences), anti-actin (1:5,000–1:15,000; Sigma), or anti-NS1 (polyclonal rabbit; 1:3,000; kindly provided by Adolfo García-Sastre, Mount Sinai). The proteins were visualized by a chemiluminescence reagent (Pierce) and detected with a GE Healthcare Amersham Imager.
Sanchez J.G., Chiang J.J., Sparrer K.M., Alam S.L., Chi M., Roganowicz M.D., Sankaran B., Gack M.U, & Pornillos O. (2016). Mechanism of TRIM25 Catalytic Activation in the Antiviral RIG-I Pathway. Cell reports, 16(5), 1315-1325.
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4

Immunoblotting Analysis of Ubiquitination

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Pelleted cells were lysed in NP-40 buffer (50 mM HEPES [pH 7.4], 150 mM NaCl, 1% [v/v] NP-40, and protease inhibitor cocktail [Roche]), followed by centrifugation at 13,000 rpm for 25 min. Lysates were mixed with a 50% slurry of glutathione-conjugated Sepharose beads (GE Healthcare), and the binding reaction was incubated for 3 hr at 4°C. Precipitates were washed extensively with lysis buffer. Proteins bound to the beads were separated by SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane (Bio-Rad). Immunoblots were performed with anti-Ub (1:5,000; P4D1; Santa Cruz), anti-FLAG (1:2,000; Sigma), anti-GST (1:2,000; Sigma), anti-RIG-I (1:1,000; Adipogen), anti-TRIM25 (1:2,000; BD Biosciences), anti-actin (1:5,000–1:15,000; Sigma), or anti-NS1 (polyclonal rabbit; 1:3,000; kindly provided by Adolfo García-Sastre, Mount Sinai). The proteins were visualized by a chemiluminescence reagent (Pierce) and detected with a GE Healthcare Amersham Imager.
Sanchez J.G., Chiang J.J., Sparrer K.M., Alam S.L., Chi M., Roganowicz M.D., Sankaran B., Gack M.U, & Pornillos O. (2016). Mechanism of TRIM25 Catalytic Activation in the Antiviral RIG-I Pathway. Cell reports, 16(5), 1315-1325.
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5

Antibody Panel for IFN Signaling Pathway

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The anti-IRF3 antibody was a gift from Michael David62 (link). The following antibodies were used in this study: anti-phospho-IRF3 (S386) (Genetex; GTX130422), anti-STAT1 (BD; 610115), anti-phospho-STAT1 (Y701) (Cell Signaling; 9171), anti-COX-IV (Cell Signaling; 4850), anti-β-Actin (Cell Signaling; 4970), anti-KHSRP (Cell Signaling; 13398), anti-RIG-I (EMD Millipore; MABF297), anti-RIG-I (Adipogen; AG-20B-0009-C100), anti-RIG-I (Sigma-Aldrich; SAB2104315), anti-Flag (M2) (Sigma; F3165), anti-Flag (Sigma; F7425), anti-V5 (Sigma; V8137), anti-HA (Sigma; H6908), HA-probe (Santa Cruz Bio; sc-7392), and anti-phospho-RIG-I (Ser8) (Abnova; PAB15905).
Soonthornvacharin S., Rodriguez-Frandsen A., Zhou Y., Galvez F., Huffmaster N.J., Tripathi S., Balasubramaniam V.R., Inoue A., de Castro E., Moulton H., Stein D.A., Sánchez-Aparicio M.T., De Jesus P.D., Nguyen Q., König R., Krogan N.J., García-Sastre A., Yoh S.M, & Chanda S.K. (2017). Systems-based Analysis of RIG-I-dependent Signaling Identifies KHSRP as an Inhibitor of RIG-I Receptor Activation. Nature microbiology, 2, 17022.
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6

Antibody Panel for IFN Signaling Pathway

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The anti-IRF3 antibody was a gift from Michael David62 (link). The following antibodies were used in this study: anti-phospho-IRF3 (S386) (Genetex; GTX130422), anti-STAT1 (BD; 610115), anti-phospho-STAT1 (Y701) (Cell Signaling; 9171), anti-COX-IV (Cell Signaling; 4850), anti-β-Actin (Cell Signaling; 4970), anti-KHSRP (Cell Signaling; 13398), anti-RIG-I (EMD Millipore; MABF297), anti-RIG-I (Adipogen; AG-20B-0009-C100), anti-RIG-I (Sigma-Aldrich; SAB2104315), anti-Flag (M2) (Sigma; F3165), anti-Flag (Sigma; F7425), anti-V5 (Sigma; V8137), anti-HA (Sigma; H6908), HA-probe (Santa Cruz Bio; sc-7392), and anti-phospho-RIG-I (Ser8) (Abnova; PAB15905).
Soonthornvacharin S., Rodriguez-Frandsen A., Zhou Y., Galvez F., Huffmaster N.J., Tripathi S., Balasubramaniam V.R., Inoue A., de Castro E., Moulton H., Stein D.A., Sánchez-Aparicio M.T., De Jesus P.D., Nguyen Q., König R., Krogan N.J., García-Sastre A., Yoh S.M, & Chanda S.K. (2017). Systems-based Analysis of RIG-I-dependent Signaling Identifies KHSRP as an Inhibitor of RIG-I Receptor Activation. Nature microbiology, 2, 17022.
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