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Tyr 705 stat3

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Tyr-705)-STAT3 is a primary antibody product developed by Cell Signaling Technology. It recognizes the phosphorylated form of STAT3 at tyrosine 705. STAT3 is a transcription factor that plays a key role in cellular signaling pathways.

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Lab products found in correlation

Tyr 204 erk1 2, by Santa Cruz Biotechnology (2 mentions) Anti erk2, by Proteintech (2 mentions) Anti stat3, by Cell Signaling Technology (2 mentions) Anti flag tag, by Merck Group (2 mentions) Anti ha tag, by Cell Signaling Technology (2 mentions) Odyssey infrared imaging system, by LI COR (2 mentions) Mmp 9, by Cell Signaling Technology (1 mentions) β catenin, by Cell Signaling Technology (1 mentions) E cadherin, by Cell Signaling Technology (1 mentions) Interleukin 6 (il 6), by Thermo Fisher Scientific (1 mentions) Bovine serum albumin (bsa), by Roche (1 mentions) Total stat3, by Santa Cruz Biotechnology (1 mentions) α sma, by Merck Group (1 mentions) β actin, by Santa Cruz Biotechnology (1 mentions) Il 10, by R&D Systems (1 mentions)

Close spelling variants of this product

STAT3 (1075 citations) Anti-p-STAT3 (tyr-705) antibody (6 citations) Anti-phospho-STAT1 (Tyr-701) anti-phospho-STAT3 (Tyr-705) (3 citations) Rabbit anti-phospho-STAT3 (Tyr 705) antibody (3 citations) Antibodies against phospho-STAT3 (Tyr-705) (2 citations) Anti-phopho-STAT3 (Tyr 705; (2 citations)

4 protocols using tyr 705 stat3

1

Analyzing Stem Cell Signaling

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The PE-conjugated mouse anti-human monoclonal antibody CD 133 was purchased from Miltenyi Biotechnology Corporation (Bergisch Gladbach, DE). Bovine serum albumin (BSA) was acquired from Roche Corporation. Epidermal growth factor (EGF), β-FGF, and IL-6 were obtained from PeproTech (Rocky Hill, NJ, USA). Monoclonal antibodies against phosphorylated Stat3 (Tyr705), Stat3, MMP-9, β-catenin, and E-cadherin were obtained from Cell Signaling Technologies (Cambridge, MA). DHA was dissolved in dimethyl sulfoxide (DMSO) at a concentration of 200 mmol/L and stored at −20°C.
Wang W., Sun Y., Li X., Shi X., Li Z, & Lu X. (2020). Dihydroartemisinin Prevents Distant Metastasis of Laryngeal Carcinoma by Inactivating STAT3 in Cancer Stem Cells. Medical Science Monitor : International Medical Journal of Experimental and Clinical Research, 26, e922348-1-e922348-14.
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2

Extracellular LepR Subdomains Isolation

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The sequences and protocols to prepare extracellular sub-domains of LepR have been described previously 86 (link). Cell lysates (in Laemmli buffer with 30mM DTT, 2mM orthovanadate and 10mM NaF) were separated by SDS/PAGE, transferred to nitrocellulose membranes and immunoblotted with the following antibodies: anti-phospho-tyrosine (Tyr-705)-STAT3 (Cell Signaling Technology Cat#9145, RRID:AB_2491009), anti-STAT3 (Cell Signaling Technology Cat#9139, RRID:AB_331757), anti-phospho-tyrosine (Tyr-204)-ERK1/2 (Santa Cruz Biotechnology Cat#sc-1 6982, RRID:AB_2139990), anti-ERK2 (Proteintech Cat#51068-1-AP, RRID:AB_2250380), anti-FLAG tag (Sigma-Aldrich Cat#SAB4301135, RRID:AB_2811010), anti-HA tag (Cell Signaling Technology Cat#3724) or XPA (Xoma Laboratories). Western blots were scanned on an Odyssey infrared Imaging System (Licor).
Duquenne M., Folgueira C., Bourouh C., Millet M., Silva A., Clasadonte J., Imbernon M., Fernandois D., Martinez-Corral I., Kusumakshi S., Caron E., Rasika S., Deliglia E., Jouy N., Oishi A., Mazzone M., Trinquet E., Tavernier J., Kim Y.B., Ory S., Jockers R., Schwaninger M., Boehm U., Nogueiras R., Annicotte J.S., Gasman S., Dam J, & Prévot V. (2021). Leptin brain entry via a tanycytic LepR:EGFR shuttle controls lipid metabolism and pancreas function. Nature metabolism, 3(8), 1071-1090.
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3

Extracellular LepR Subdomains Isolation

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The sequences and protocols to prepare extracellular sub-domains of LepR have been described previously 86 (link). Cell lysates (in Laemmli buffer with 30mM DTT, 2mM orthovanadate and 10mM NaF) were separated by SDS/PAGE, transferred to nitrocellulose membranes and immunoblotted with the following antibodies: anti-phospho-tyrosine (Tyr-705)-STAT3 (Cell Signaling Technology Cat#9145, RRID:AB_2491009), anti-STAT3 (Cell Signaling Technology Cat#9139, RRID:AB_331757), anti-phospho-tyrosine (Tyr-204)-ERK1/2 (Santa Cruz Biotechnology Cat#sc-1 6982, RRID:AB_2139990), anti-ERK2 (Proteintech Cat#51068-1-AP, RRID:AB_2250380), anti-FLAG tag (Sigma-Aldrich Cat#SAB4301135, RRID:AB_2811010), anti-HA tag (Cell Signaling Technology Cat#3724) or XPA (Xoma Laboratories). Western blots were scanned on an Odyssey infrared Imaging System (Licor).
Duquenne M., Folgueira C., Bourouh C., Millet M., Silva A., Clasadonte J., Imbernon M., Fernandois D., Martinez-Corral I., Kusumakshi S., Caron E., Rasika S., Deliglia E., Jouy N., Oishi A., Mazzone M., Trinquet E., Tavernier J., Kim Y.B., Ory S., Jockers R., Schwaninger M., Boehm U., Nogueiras R., Annicotte J.S., Gasman S., Dam J, & Prévot V. (2021). Leptin brain entry via a tanycytic LepR:EGFR shuttle controls lipid metabolism and pancreas function. Nature metabolism, 3(8), 1071-1090.
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4

Molecular Markers in Myocardial Infarction

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Samples were obtained from either the border zone at day 3 or from the remote zone (>2 mm within the infarct) at day 28. Antibodies to phosphor (Tyr705)‐STAT3 (Cell Signaling Technology), total STAT3 (Santa Cruz Biotechnology), iNOS (Cell Signaling Technology), IL‐10 (R& D systems), α‐SMA (Clone 1A4, Sigma) and β‐actin (Santa Cruz Biotechnology) were used. Western blotting procedures were described previously.16 Experiments were replicated three times and results expressed as the mean value.
Lin C., Chen S., Lien H., Lin S, & Lee T. (2019). Targeting the PI3K/STAT3 axis modulates age‐related differences in macrophage phenotype in rats with myocardial infarction. Journal of Cellular and Molecular Medicine, 23(9), 6378-6392.
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