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Anti ifit1

Manufactured by Thermo Fisher Scientific
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Sourced in Japan

Anti-IFIT1 is a laboratory product that detects the presence of IFIT1 protein. IFIT1 is an interferon-stimulated gene that plays a role in the cellular immune response. The Anti-IFIT1 product is designed to identify and quantify IFIT1 expression levels in biological samples.

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Lab products found in correlation

Odyssey infrared imaging system, by LI COR (1 mentions) Irdye 800cw goat anti mouse, by LI COR (1 mentions) Irdye 680rd goat anti rabbit, by LI COR (1 mentions) Rabbit anti gapdh, by Cell Signaling Technology (1 mentions) Protease inhibitor cocktail, by Merck Group (1 mentions) Anti flag m2, by Merck Group (1 mentions) Immobilon psq pvdf membrane, by Merck Group (1 mentions) Mini protean tgx precast gel, by Bio-Rad (1 mentions) Anti hsp90, by Santa Cruz Biotechnology (1 mentions) Anti tbk1, by Cell Signaling Technology (1 mentions) Anti phospho tbk1s172, by Cell Signaling Technology (1 mentions) Anti ifit3, by Proteintech (1 mentions) Anti phospho stat1 y701, by Cell Signaling Technology (1 mentions)

3 protocols using anti ifit1

1

Western Blot Analysis of IFIT Proteins

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Cells were disrupted using Radioimmunoprecipitation assay (RIPA) lysis and extraction buffer (Sigma-Aldrich) supplemented with protease inhibitor cocktail (Sigma-Aldrich). Immunoblots were performed using a rabbit polyclonal anti-IFIT1 (Thermo Fisher), rabbit anti-GAPDH (Cell Signaling Technology), rabbit polyclonal anti-IFIT3 (Fensterl et al., 2008 (link)), or mouse monoclonal anti-FLAG M2 (Sigma-Aldrich), followed by IRDye 680RD goat anti-rabbit or IRDye 800CW goat anti-mouse (LiCor). Blots were imaged using a LiCor Odyssey infrared imaging system.
Johnson B., VanBlargan L.A., Xu W., White J.P., Shan C., Shi P.Y., Zhang R., Adhikari J., Gross M.L., Leung D.W., Diamond M.S, & Amarasinghe G.K. (2018). Binding of IFIT1 by IFIT3 modulates protein stability and RNA binding specificity. Immunity, 48(3), 487-499.e5.
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2

Immunoblotting Analysis of Innate Immune Signaling

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5′ppp-treated cells were lysed in RIPA buffer (50 mN Tris-Hcl PH 8, 1% sodium deoxycholate, 1% NP-40, 5 mM EDTA, 150 mM NaCl, 0.1% sodium dodecyl sulfate) and cleared by centrifugation at 17,000×g for 15 min at 4°C. Cleared lysates were subjected to SDS-PAGE analysis on 4–20% acrylamide Mini-Protean TGX precast gels (Biorad, Hercules, USA). Proteins were electrophoretically transferred to Immobilon-PSQ PVDF membranes (Millipore, Billerica, USA) and then subjected to immunoblotting using indicated antibodies. Anti-pIRF3 Ser 396 and anti-RIG-I antibodies were purchased from EMD Millipore, anti-IRF3 from IBL, Japan, anti-IFIT1 from Thermo Fisher Scientific, anti pSTAT1 Tyr701 and anti-STAT1 from Cell Signaling, and anti-β-actin from Odyssey.
Feng Q., Langereis M.A., Olagnier D., Chiang C., van de Winkel R., van Essen P., Zoll J., Hiscott J, & van Kuppeveld F.J. (2014). Coxsackievirus Cloverleaf RNA Containing a 5′ Triphosphate Triggers an Antiviral Response via RIG-I Activation. PLoS ONE, 9(4), e95927.
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3

Protein Extraction and Western Blot Analysis

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Total liver protein extracts were prepared using a lysis buffer containing 50 mM Tris–HCl (pH = 7.5), 137 mM NaCl, 1 mM EDTA, 1% Triton X-100, 10% glycerol, 10 mM NaF, 10 mM Na4P2O7, 1 mM Na3VO4, and protease inhibitor cocktail. The lysates were separated by SDS-PAGE and transferred to a PVDF membrane, followed by immunoblotting with primary antibodies and secondary antibodies. The following antibodies were used: anti-TBK1 (Cell Signaling Technology, 3013); anti-phospho-TBK1S172 (Cell Signaling Technology, 5483); anti-IFIT1 (Thermo Fisher, PA3-846); anti-IFIT3 (ProteinTech, 15201-1-AP); anti-ZBP1; anti-STAT1 (Cell Signaling Technology, 9172); anti-phospho-STAT1Y701 (Cell Signaling Technology, 9171); anti-HSP90 (Santa Cruz BioTech, sc-7947). TSK antibody was generated in rabbits with a synthetic peptide corresponding to mouse TSK (amino acids 317-335; CRRLVREGAYHRQPGSSPK) and affinity purified.
Xiong X., Wang Q., Wang S., Zhang J., Liu T., Guo L., Yu Y, & Lin J.D. (2018). Mapping the molecular signatures of diet-induced NASH and its regulation by the hepatokine Tsukushi. Molecular Metabolism, 20, 128-137.
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