Stat3 79d7

Manufactured by Cell Signaling Technology

Sourced in United States

STAT3 (79D7) is a monoclonal antibody product developed by Cell Signaling Technology. The antibody targets the STAT3 protein, which is a transcription factor involved in cellular processes such as cell growth, differentiation, and survival. This product is intended for research use only.

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11 protocols using stat3 79d7

Western Blot Analysis of Cellular Proteins

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Whole cell lysates were prepared from 7 x 10⁵ cells in 2 x SDS-DTT sample buffer. Lysates were run on SDS-PAGE gels and transferred to PVDF membranes (Millipore) using standard protocols. Membranes were probed with the following primary antibodies at 1:1000 dilution unless otherwise stated: Acetyl-p53 Lys379 (1:500) (2570; Cell Signalling), total p53 (1C12; Cell Signalling), Phospho-p44/42 MAPK (Erk1/2) Thr202/Tyr204 (9101; Cell Signalling), p44/42 MAPK (Erk1/2) (9102; Cell Signalling), Phospho-Stat3 (Tyr705) (9131; Cell Signaling), Stat3 (79D7) (4904; Cell Signalling), Histone H3 (acetyl K27) (ab4729, Abcam), Histone H3 (ab1791, Abcam), Beta Actin (ab8227, Abcam). Membranes were probed with secondary antibodies conjugated to horseradish peroxidase (HRP) (GE Healthcare; 1:5000) and proteins detected using SuperSignal West Femto kit (Thermo Scientific).

Horton S.J., Giotopoulos G., Yun H., Vohra S., Sheppard O., Bashford-Rogers R., Rashid M., Clipson A., Chan W.I., Sasca D., Yiangou L., Osaki H., Basheer F., Gallipoli P., Burrows N., Erdem A., Sybirna A., Foerster S., Zhao W., Sustic T., Harrison A.P., Laurenti E., Okosun J., Hodson D., Wright P., Smith K.G., Maxwell P., Fitzgibbon J., Du M.Q., Adams D.J, & Huntly B.J. (2017). Early loss of Crebbp confers malignant stem cell properties on lymphoid progenitors. Nature cell biology, 19(9), 1093-1104.

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Hepatocyte Stress Signaling Analysis

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Total liver lysates were analyzed by immunoblotting using antibodies against HBsAg (20-HR20, Fitzgerald), GADD153 (F-168, Santa Cruz), phospho-PERK (16F8, Cell Signaling), PERK (H-300, Santa Cruz), phospho-eIF2α (119A11, Cell Signaling), eIF2α (L57A5, Cell Signaling), β-actin (13E5, Cell Signaling), JNK2 (N-18, Santa Cruz), c-Jun (60A8, Cell Signaling), phospho-c-Jun (D47G9, Cell Signaling), phospho-SAPK/JNK (81E11, Cell Signaling), STAT3 (79D7, Cell Signaling), phospho-STAT3 (D3A7, Cell Signaling).

Churin Y., Roderfeld M., Stiefel J., Würger T., Schröder D., Matono T., Mollenkopf H.J., Montalbano R., Pompaiah M., Reifenberg K., Zahner D., Ocker M., Gerlich W., Glebe D, & Roeb E. (2014). Pathological Impact of Hepatitis B Virus Surface Proteins on the Liver Is Associated with the Host Genetic Background. PLoS ONE, 9(3), e90608.

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Immunoblotting of pStat3-Ser727 in GBM

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Total protein from GBM cells were separated on 8% polyacrylamide gels and transferred to nitrocellulose. Blots were incubated with antibodies against pStat3-Ser727 (D8C2Z, Cell Signaling, Danvers, MA, USA), Stat3 (79D7, Cell Signaling) and GAPDH (sc-25778, Santa Cruz Biotechnology. Santa Cruz, CA, USA), followed by secondary anti-rabbit antibodies conjugated to horseradish peroxidase (sc-2357, Santa Cruz Biotechnology).

Vidal V., Gutierrez O., Talamillo A., Velasquez C, & Fernandez-Luna J.L. (2021). Glioblastoma invasion factor ODZ1 is induced by microenvironmental signals through activation of a Stat3-dependent transcriptional pathway. Scientific Reports, 11, 16196.

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Immunoblot Analysis of STAT3 Phosphorylation

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Cells were lysed in cell lysis buffer (20 mM Tris, 150 mM NaCl, 1 mM Na₂EDTA, 1mM EGTA, 1% Triton X-100) supplemented with protease and phosphatase inhibitors. Whole cell lysates were resolved by SDS-PAGE and immunoblotted with the following antibodies from Cell Signaling Technology (Danvers, MA): Actin (13E5) 1:1000, GAPDH (14C10) 1:1000, STAT3 (79D7) 1:1000, phospho-Stat3 Tyr705 (D3A7) 1:250, phospho-Stat3 Ser727 (9134) 1:250.

DeVaux R.S., Ropri A.S., Grimm S.L., Hall P.A., Herrera E.O., Chittur S.V., Smith W.P., Coarfa C., Behbod F, & Herschkowitz J.I. (2020). Long noncoding RNA BHLHE40-AS1 promotes early breast cancer progression through modulating IL6 / STAT3 signaling. Journal of cellular biochemistry, 121(7), 3465-3478.

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Western Blot Analysis of Cellular Proteins

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Immunoblotting of PD-1, STAT3, and p-STAT3

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BMDCs in respective experiments were lysed in lysis buffer A (150 mM NaCl, 20 mM Tris Cl (pH7.4), 5 mM EDTA, 1 mM CaCl₂, 10 mM NaF, 1% Triton X 100, 5% glycerol, HALT protease/phosphatase inhibitor (Thermo Scientific). 10 μgs protein were loaded and separated by SDS-PAGE and analyzed by immunoblotting for PD-1 (Novus Biologicals, AF1021), STAT3 (79D7) and p-STAT3 (D3A7) (Cell Signaling Technology), and β-actin (LI-COR, Lincoln NE). Corresponding anti-goat, anti-mouse, and anti-rabbit secondary antibodies conjugated to IRDyes were purchased from LI-COR. Signal was detected using LI-COR Odyssey Imaging System.

Lamichhane P., Karyampudi L., Shreeder B., Krempski J., Bahr D., Daum J., Kalli K.R., Goode E.L., Block M.S., Cannon M.J, & Knutson K.L. (2017). IL-10 release upon PD-1 blockade sustains immunosuppression in ovarian cancer. Cancer research, 77(23), 6667-6678.

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SDS-PAGE Immunoblotting for Protein Quantification

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Extracts were run on an 8% to 12% SDS-PAGE gel, transferred to Immobilon-P transfer membranes (Milipore Corp.), and visualized with antibodies specific for phospho-STAT3 (Tyr705 and 3E2; Cell Signaling), STAT3 (79D7; Cell Signaling), phospho-ERK1/2 (Thr202 and Tyr204; Cell Signaling Technology), ERK1 (C16; Santa Cruz), mouse monoclonal UL99 (pp28) and HA (HA-7; Sigma), rabbit UL7, and actin (C4; Millipore).

MacManiman J.D., Meuser A., Botto S., Smith P.P., Liu F., Jarvis M.A., Nelson J.A, & Caposio P. (2014). Human Cytomegalovirus-Encoded pUL7 Is a Novel CEACAM1-Like Molecule Responsible for Promotion of Angiogenesis. mBio, 5(6), e02035-14.

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Western Blot Analysis of JAK-STAT Signaling

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Cell pellets were lysed with RIPA buffer (Sigma-Aldrich) following the manufacturer’s instruction. SDS–polyacrylamide gel electrophoresis was performed using 4–20% Criterion TGX Stain Free Protein Gel (Bio-Rad, Hercules, CA), and proteins were transferred to poly-vinylidene difluoride (PVDF) Immobilion-p membrane (Merck-Millipore, Billerica, MA, USA) using wet/tank Bio-Rad blotting system. Membranes were blocked in I-block 2% (Invitrogen, Waltham, MA, USA), incubated overnight at 4 °C with primary antibodies and 1 h with the HRP- conjugated secondary antibody (PerkinElmer, Waltham, MA, USA). Bands were detected using Invitrogen™ iBright™ FL1500 Imaging System. The following primary antibodies were used: JAK1 Y1022/1023 (Cell Signaling Technologies, #3331), JAK2 Y1007 (MBS128333, MyBioSource, San Diego, CA, USA), STAT6 Y641 (Millipore, 06-937), STAT3 Y705 (Cell Signaling Technologies, #9145), STAT5 Y694 (Cell Signaling Technologies, #9351), STAT6 (#11290, Becton Dickinson, Franklin Lakes, NJ, USA), STAT3 (79D7) (Cell Signaling Technologies, #4904), STAT5 (Becton Dickinson #611834), GAPDH (GTX 8627408, Genetex, Irvine, CA, USA).

Veltri G., Silvestri C., Gallingani I., Sandei M., Vencato S., Lovisa F., Cortese G., Pillon M., Carraro E., Bresolin S., Biffi A., Basso G., Accordi B., Mussolin L, & Serafin V. (2021). Ruxolitinib as a Novel Therapeutic Option for Poor Prognosis T-LBL Pediatric Patients. Cancers, 13(15), 3724.

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Immunoprecipitation of STAT3 in C2C12 cells

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C2C12 cells were subjected to cell lysis buffer containing 10 mM Tris-HCl (pH 8), 10 mM NaCl, 0,1 mM EDTA (pH 8), 0,1 mM EGTA, and phosphatase and protease inhibitors. Then, NP-40 was added at the final concentration of 0.5%. After the centrifugation, 200 μg of cytoplasmic extract was immunoprecipitated with 2 μl of anti-STAT3 antibody (#119352; Abcam) overnight at 4°C. After the addition of 20 μl of protein A/G magnetic beads (Thermo Fisher Scientific) for 120 min at 4°C, the immunoprecipitated proteins were washed with lysis buffer, containing 50 mM Tris-HCl (pH 8), 150 mM NaCl, 1 mM EDTA (pH 8), 1 mM EGTA, six times. Subsequently, immunoprecipitated samples were added to Laemmli buffer and subjected to immunoblotting analysis. Incubation with primary and secondary antibodies was performed. The following antibodies have been used: STAT3 (79D7) (1:1,000, #4904; Cell Signaling), PKR (1:1,000, #184257; Abcam).

Catarinella G., Bracaglia A., Skafida E., Procopio P., Ruggieri V., Parisi C., De Bardi M., Borsellino G., Madaro L., Puri P.L., Sacco A, & Latella L. (2024). STAT3 inhibition recovers regeneration of aged muscles by restoring autophagy in muscle stem cells. Life science alliance, 7(8).

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Immunohistochemical Analysis of Stem Cell Markers

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Sections (3 μm thick) from specimens were deparaffinized and rehydrated. The slides were heated to 95 °C for 35 min in citrate buffer pH 6.0 for antigen retrieval and incubated in methanol and in 6% hydrogen peroxide solution (1:1) for 30 min to quench endogenous peroxidase activity. The sections were incubated with 1% BSA (Bovine Serum Albumin; Sigma Aldrich) for 45 min to block nonspecific reactions. The slides were incubated with primary antibodies: Oct-4 (C52G3, Cell Signaling Technology, Danvers, MA) 1:25, Sox-2 (D6D9 XP, Cell Signaling Technology, Danvers, MA) 1:50, Nanog (1E6C4, Cell Signaling Technology, Danvers, Massachusetts) 1:60, Stat-3 (79D7, Cell SignalingTechnology, Danvers, Massachusetts) 1:50 and Sox-5 (AV33323, Sigma Aldrich, St Louis, Missouri) 1:50, overnight at 4 °C. The Advanced HRP system (Dako, Glostrup, Denmark) detected antibodies. The specimens were counterstained with Harris's hematoxylin (Sigma Aldrich, St Louis, Missouri) dehydrated and mounted for observation. Nonimmune serum was used as a negative control, bell stage of dental formation was used as a positive control for Oct-4, Sox-5 and Nanog, lung carcinoma for Sox-2 and colon adenocarcinoma for Stat-3. Immunohistochemistry was not evaluated by software, staining was analyzed by three researchers specialized in morphology. The assessment was carried out independently.

Pagni T.C., Cunha J.M., Saez D.M., Costa-Neves A.D., Kerkis I, & Silva M.C. (2023). Nanog, Stat-3, and Sox-5 involvement in human fetal temporomandibular joint late development. Journal of Oral Biology and Craniofacial Research, 13(5), 636-641.

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