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Mouse anti stat1

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Mouse anti-STAT1 is a laboratory reagent used for the detection and analysis of STAT1 (Signal Transducer and Activator of Transcription 1) protein. STAT1 is a key transcription factor involved in cellular signaling pathways and plays a role in various biological processes. This antibody can be used in techniques such as Western blotting, immunoprecipitation, and immunohistochemistry to study the expression and localization of STAT1 in biological samples.

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Lab products found in correlation

Rabbit anti stat3, by Cell Signaling Technology (3 mentions) Ecl system, by Thermo Fisher Scientific (2 mentions) Rabbit anti phosphorylated stat3, by Cell Signaling Technology (1 mentions) Rabbit anti stat4, by Cell Signaling Technology (1 mentions) Mouse anti α tubulin, by Santa Cruz Biotechnology (1 mentions) Proteinase inhibitor cocktail mix, by Roche (1 mentions) Mouse anti v5, by Thermo Fisher Scientific (1 mentions) Rabbit anti gapdh, by Santa Cruz Biotechnology (1 mentions) Mouse anti gapdh, by Santa Cruz Biotechnology (1 mentions) Nitrocellulose membrane, by Bio-Rad (1 mentions) Dithiothreitol (dtt), by Thermo Fisher Scientific (1 mentions) Sodium chloride (nacl), by Avantor (1 mentions) Phenyl methyl sulfonyl fluoride (pmsf), by Merck Group (1 mentions) Phosstop, by Roche (1 mentions) Orthovanadate, by Merck Group (1 mentions) Ethylene diamine tetraacetic acid (edta), by MP Biomedicals (1 mentions) Rabbit anti phosphorylated stat3 y705, by Cell Signaling Technology (1 mentions) Rabbit anti erk, by Merck Group (1 mentions) Rabbit anti p65, by Santa Cruz Biotechnology (1 mentions) Protein assay kit, by Bio-Rad (1 mentions)

Spelling variants of this product

STAT1 (19 citations) Anti-STAT1 (15 citations) Mouse anti (2 citations) Mouse anti-human/mouse STAT1 phosphorylated at tyrosine 701 (2 citations)

4 protocols using mouse anti stat1

1

Immunoblotting Analysis of STAT Proteins

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Total protein was extracted from the cells with a lysis buffer containing 1% NP-40, 20 mM Tris-HCl, pH 7.4, 140 mM NaCl, 2 mM EDTA, and 50 mM NaF, supplemented with 100 mM orthovanadate, 200 mM PMSF, 1% aprotinin, 1 mg/ml pepstatin, 1 mg/ml leupeptin, and 1 mg/ml antipain. Protein fractions were separated by SDS-PAGE and electrotransferred onto PVDF membranes. The following primary Abs were used: mouse anti–phosphorylated STAT1 (BD), mouse anti-STAT1 (BD), rabbit anti–phosphorylated STAT3 (Cell Signaling Technology), rabbit anti-STAT3 (Cell Signaling Technology), rabbit anti–phosphorylated STAT4 (Abazyme), rabbit anti-STAT4 (Cell Signaling Technology), mouse anti–α-tubulin (Santa Cruz Biotechnology, Inc.), rabbit anti-TYK2 (C-ter1; Santa Cruz Biotechnology, Inc.), mouse anti-TYK2 (C-ter2; Santa Cruz Biotechnology, Inc.), and mouse anti-TYK2 Abs (N-ter1 [BD] and N-ter2 [a gift from S. Pellegrini, Institut Pasteur, CNRS URA 1961, Paris, France]). Ab binding was detected by incubation with HRP-conjugated anti–mouse or anti–rabbit secondary Abs (GE Healthcare), with the ECL system (Thermo Fisher Scientific).
Kreins A.Y., Ciancanelli M.J., Okada S., Kong X.F., Ramírez-Alejo N., Kilic S.S., El Baghdadi J., Nonoyama S., Mahdaviani S.A., Ailal F., Bousfiha A., Mansouri D., Nievas E., Ma C.S., Rao G., Bernasconi A., Sun Kuehn H., Niemela J., Stoddard J., Deveau P., Cobat A., El Azbaoui S., Sabri A., Lim C.K., Sundin M., Avery D.T., Halwani R., Grant A.V., Boisson B., Bogunovic D., Itan Y., Moncada-Velez M., Martinez-Barricarte R., Migaud M., Deswarte C., Alsina L., Kotlarz D., Klein C., Muller-Fleckenstein I., Fleckenstein B., Cormier-Daire V., Rose-John S., Picard C., Hammarstrom L., Puel A., Al-Muhsen S., Abel L., Chaussabel D., Rosenzweig S.D., Minegishi Y., Tangye S.G., Bustamante J., Casanova J.L, & Boisson-Dupuis S. (2015). Human TYK2 deficiency: Mycobacterial and viral infections without hyper-IgE syndrome. The Journal of Experimental Medicine, 212(10), 1641-1662.
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2

Protein Extraction and Immunoblotting Protocol

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Total protein was extracted from the cells in a lysis buffer containing 1% NP-40 (Fluka), 20 mM Tris–HCl pH 7.4 (Tris MP Biomedicals, HCl Sigma), 140 mM NaCl (VWR), and 2 mM EDTA (MP Biomedicals); supplemented with 100 mM orthovanadate (Sigma), 200 mM PMSF (Sigma), proteinase inhibitor cocktail mix (Roche), phosSTOP (Roche), and 0.1 mM DTT (Invitrogen). Protein fractions were separated by SDS-PAGE and electrotransferred onto nitrocellulose membranes (Biorad). The following primary Abs were used: mouse anti-phosphorylated Y701 STAT1 (BD), mouse anti-STAT1 (BD), rabbit anti-phosphorylated Y705 STAT3 (Cell Signaling Technology), rabbit anti-STAT3 (Cell Signaling Technology), goat anti-IL-10RB (Bio-Techne), mouse HRP-conjugated anti-His (Santa Cruz Biotechnology), mouse anti-V5 (Invitrogen), mouse anti-GAPDH (Santa Cruz Biotechnology) or rabbit anti-GAPDH (Santa Cruz Biotechnology), and mouse HRP-conjugated anti-DDK (Origene). Antibody binding was detected by incubation with HRP-conjugated anti-mouse, anti-goat, or anti-rabbit secondary Abs (GE Healthcare), with the ECL system (Thermo Fisher Scientific). Antibodies were also detected by fluorescence on the Licor system with secondary antibodies conjugated to IRDye800 or IRDye680 anti-mouse, anti-goat, or anti-rabbit antibodies (all from Licor Biosciences Proteomics).
Korol C.B., Belkaya S., Alsohime F., Lorenzo L., Boisson-Dupuis S., Brancale J., Neehus A.L., Vilarinho S., Zobaida A., Halwani R., Al-Muhsen S., Casanova J.L, & Jouanguy E. (2022). Fulminant Viral Hepatitis in Two Siblings with Inherited IL-10RB Deficiency. Journal of Clinical Immunology, 43(2), 406-420.
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3

Phosphorylated STAT1/3 Immunoblot Protocol

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The following primary antibodies were used throughout the experiments in 5 % BSA/TBS/0.1 % Tween-20: rabbit-anti-phosphorylated STAT1 (Y701) (Cell Signaling Technology, Danvers, MA, USA; 1:1000), mouse-anti-STAT1 (BD Biosciences, San Jose, CA, USA; 1:1000), rabbit-anti-phosphorylated STAT3 (Y705) (Cell Signaling Technology, 1:1000), rabbit-anti-STAT3 (Cell Signaling Technology, 1:1000), and rabbit-anti-SOCS3 (Immunobiological Laboratories Co. Ltd., Gunma, Japan; 1:200). Horseradish peroxidase (HRP)-conjugated donkey-anti-rabbit immunoglobulin (GE healthcare life sciences; Marlborough, MA, USA) secondary antibody was used at 1:5000 in 5 % BSA/TBS/0.1 % Tween-20. HRP-conjugated sheep-anti-mouse immunoglobulin (GE Healthcare Life Sciences) secondary antibody was used at 1:5000 in 5 % BSA/TBS/0.1 % Tween-20.
Swiderski K., Thakur S.S., Naim T., Trieu J., Chee A., Stapleton D.I., Koopman R, & Lynch G.S. (2016). Muscle-specific deletion of SOCS3 increases the early inflammatory response but does not affect regeneration after myotoxic injury. Skeletal Muscle, 6, 36.
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4

Microglial Protein Extraction and Analysis

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Microglial cells were plated into 25 cm2 flasks. Total proteins were extracted with RIPA buffer (Pierce) and 1% protease / phosphatase inhibitor cocktail (Pierce). Nuclear extracts were prepared using a nuclear extract kit according to the manufacturer’s instructions (Active Motif, CA). Protein content was determined using the Bio-Rad Protein Assay Kit according to the manufacturer’s protocol.
Total proteins (20 μg) or nuclear proteins (10 μg) were separated through SDS-PAGE on a 12% gel and transferred to nitrocellulose membrane. Blots were incubated with a mouse anti-Stat1 (1:500, BD Biosciences, Belgium), rabbit anti-phospho-Stat1 (1:1000, Bioke, The Netherlands), rabbit anti-p38 (1:1000, Calbiochem, Belgium), rabbit anti-phospho-p38 (1:1000, Bioke), rabbit anti-ERK (1:20000, Sigma), rabbit anti-phospho-ERK (1:2000, Bioke), mouse anti-α-tubulin (1:5000, AbCam, UK), rabbit anti-p65 (1:200, Santa Cruz Biotechnologies, Germany), rabbit anti-c-Fos (1:1000, Bioke), rabbit anti-Nrf2 (1:1000, Bioke) and mouse anti-HDAC1 (1:2000, AbCam) antibody. After washing, membranes were incubated with an anti-rabbit or anti-mouse IgG-HRP antibody (1:2000, Amersham Biosciences, UK). Antibody complexes were detected by using SuperSignal West Femto Maximum Sensitivity Substrate (Pierce) on a ChemiDoc™ XRS+ System (Bio-Rad).
Hoenen C., Gustin A., Birck C., Kirchmeyer M., Beaume N., Felten P., Grandbarbe L., Heuschling P, & Heurtaux T. (2016). Alpha-Synuclein Proteins Promote Pro-Inflammatory Cascades in Microglia: Stronger Effects of the A53T Mutant. PLoS ONE, 11(9), e0162717.
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