Rabbit anti akt1 2 3

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Rabbit anti-Akt1/2/3 is a primary antibody that recognizes the Akt1, Akt2, and Akt3 isoforms of the serine/threonine-protein kinase Akt. It is a research-use-only product intended for Western blotting, immunoprecipitation, and other immunodetection applications.

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Lab products found in correlation

Sds page gel, by Bio-Rad (1 mentions) Mouse anti β actin, by Abcam (1 mentions) Odyssey clx infrared imaging system, by LI COR (1 mentions) Mouse anti β actin, by Merck Group (1 mentions) Mouse anti bax, by Merck Group (1 mentions) Mouse anti bcl 2, by Merck Group (1 mentions) Rabbit anti jak2, by Cell Signaling Technology (1 mentions) Quantity one software, by Bio-Rad (1 mentions) Gs 800, by Bio-Rad (1 mentions) Rabbit anti rps6, by Cell Signaling Technology (1 mentions) Rabbit anti phospho 4ebp1, by Cell Signaling Technology (1 mentions)

Close spelling variants of this product

Akt1/2/3 (24 citations) Anti-Akt1 (15 citations) Anti-AKT1/2/3 (9 citations) Akt1/2 (8 citations) Rabbit anti-TM (2 citations) Rabbit anti-p-AKT1/2/3 (Ser473) polyclonal antibody (sc-101629) (2 citations)

3 protocols using rabbit anti akt1 2 3

Phospho-Akt and Histone Acetylation Assay

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Cell lysates were prepared by harvesting in lysis buffer (2% SDS, 20% glycerol, 50 mM Tris-HCl, 150 mM DTT, pH 7.4), separated on 4–20% SDS PAGE gels (Bio-Rad) and transferred to nitrocellulose membranes by electroblotting, probed with the primary antibodies: mouse anti-phospho-Akt (Ser473), clone 6F5 (Millipore), rabbit anti-acetyl lysine (Millipore), rabbit anti-Akt1/2/3 (Santa Cruz Biotechnology, Dallas, TX, U.S.A.), mouse anti-β-actin (abcam, Cambridge, U.K.) followed by secondary antibodies conjugated with infrared probes, and scanned on an Odyssey CLx Infrared Imaging System (Li-COR Biosciences, Lincoln, NE, U.S.A.). For histone acetylation Westerns, the cells were treated with 10 mM sodium butyrate to increase the background levels of acetylation, co-treated with SS at the listed concentrations, and harvested after 8 h.

Fernandez H.R, & Lindén S.K. (2017). The aspirin metabolite salicylate inhibits lysine acetyltransferases and MUC1 induced epithelial to mesenchymal transition. Scientific Reports, 7, 5626.

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Evaluation of Apoptosis and Signaling

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Western blotting was performed using a standard method described previously [12 (link)]. The nitrocellulose membranes were incubated with following antibodies: mouse anti-BAX (Sigma-Aldrich, St. Louis, MO, USA, Cat# WH0000581M1, RRID:AB_1840183,), mouse anti-BCL-2 (Sigma-Aldrich Cat# B3170, RRID:AB_258541), rabbit anti-phospho Akt1/2/3 (Santa Cruz Biotechnology, Dallas, TX, USA, Cat# sc-7985 also sc-7985-R, RRID:AB_667741), rabbit anti-Akt1/2/3 (Santa Cruz Biotechnology, Cat# sc-8312, RRID:AB_671714), rabbit anti-phospho-MAPK (Thermo Fisher Scientific, Waltham, MA, USA, Cat# PA1-14302, RRID:AB_1086514), rabbit anti-MAPK (Thermo Fisher Scientific Cat# PA5-14425, RRID:AB_2141578), rabbit anti-pospho JAK2 (Cell Signaling Technology, Leiden, The Netherlands, Cat# 3771S, RRID:AB_330403), rabbit anti-JAK2 (Cell Signaling Technology Cat# 4040S, RRID:AB_10691469), and mouse anti- β-Actin (Sigma-Aldrich Cat# A5316, RRID:AB_476743).

Tankiewicz-Kwedlo A., Hermanowicz J.M., Pawlak K., Czarnomysy R., Bielawski K., Prokop I, & Pawlak D. (2018). Erythropoietin Intensifies the Proapoptotic Activity of LFM-A13 in Cells and in a Mouse Model of Colorectal Cancer. International Journal of Molecular Sciences, 19(4), 1262.

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Western Blot Analysis of Muscle Proteins

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Protein was extracted from the gastrocnemius muscle, and Western blotting was performed as previously described (Smith et al. 2014) (link). Membranes were incubated with rabbit anti-AKT1/2/3 (1:10,000, #8312, Santa Cruz Biotechnology), rabbit anti-phospho AKT S473 (1:500, #7985, Santa Cruz Biotechnology), rabbit anti-4EBP1 (1:500, #R113, Santa Cruz Biotechnology), rabbit anti-phospho-4EBP1 (1:2000, Thr37/46, #236B4, Cell Signaling Technology), rabbit anti-rpS6 (1:1000, #2217, 5G10, Cell Signaling Technology) andrabbit antiphospho-rpS6 (1:1000, Ser235/236, #2211, Cell Signaling Technology), and the abundance of each protein was detected with enhanced chemiluminescence. GAPDH was used as a loading control (mouse anti-rabbit GAPDH (1:10,000, #RDI-TRK5G4-6C5, Research Diagnostics, Inc., NJ, USA). The optical densities of each immunoreactive band were captured with a densitometer (GS 800, Bio-Rad Laboratories (NZ) Pty Ltd) and analysed using Quantity One software (Bio-Rad Laboratories (NZ) Pty Ltd).

Hennebry A., Oldham J., Shavlakadze T., Grounds M.D., Sheard P., Fiorotto M.L., Falconer S., Smith H.K., Berry C., Jeanplong F., Bracegirdle J., Matthews K., Nicholas G., Senna-Salerno M., Watson T, & McMahon C.D. (2017). IGF1 stimulates greater muscle hypertrophy in the absence of myostatin in male mice. The Journal of endocrinology, 234(2).

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