Phosphor akt thr308

Manufactured by Cell Signaling Technology

Sourced in United States

Phosphor-Akt (Thr308) is a laboratory equipment product from Cell Signaling Technology. It is a specific antibody that recognizes Akt phosphorylated at threonine 308. This antibody can be used to detect the phosphorylation state of Akt, a key protein involved in cellular signaling pathways.

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4 protocols using phosphor akt thr308

Western Blot Analysis of Signaling Pathways

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The cells were lysed in NP40 lysis buffer containing 1mM PMSF, 1‰ protease inhibitor and 1% phosphorylase inhibitor on ice for 30 min. After centrifuged, the supernatant was acquired and separated by 12% SDS-PAGE, and then transferred to nitrocellulose membrane. The nitrocellulose membrane was blocked with 4% skim milk powder in PBST for 1 h, and incubated with anti-tilapia IFN-γ mAb or 1:1000 diluted primary antibody against S6, 4EBP1, phospho-S6 (Ser240/244), phospho-4EBP1 (Thr37/46), phosphor-STAT5 (Tyr694), phosphor-Erk1/2 (Thr202/Tyr204), phosphor-Akt (Thr308), phosphor-Akt (Ser473), and β-actin from Cell Signaling Technology at 4°C overnight, and further incubated with goat anti-rabbit or mouse IgG H&L 800 or 680 (Abcam). To detect the overexpressed IFN-γ in 293T cells, the nitrocellulose membrane was incubated with anti-tilapia IFN-γ mAb, followed by Ap-conjugated goat anti-mouse IgG secondary antibody (Southern Biotech), and visualized with freshly prepared substrate solution (100 mM NaCl, 100 mM Tris, and 5 mM MgCl₂; pH 9.5) containing nitroblue tetrazolium (Sigma) and 5-bromo-4-chloro-3-indolylphosphate (Sigma). Images were acquired by Odyssey CLx Image Studio.

Ai K., Li K., Jiao X., Zhang Y., Li J., Zhang Q., Wei X, & Yang J. (2022). IL-2–mTORC1 signaling coordinates the STAT1/T-bet axis to ensure Th1 cell differentiation and anti-bacterial immune response in fish. PLOS Pathogens, 18(10), e1010913.

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Insulin Signaling Pathway Regulation

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Antibodies against TXNIP (#14715), Akt (#2920), phosphor-Akt (Thr308) (#4056), AS160 (#2670), phosphor-AS160 (Ser588) (#8730), PDK1 (#13037), GLUT4 (#2213), PERK (#3192), IRE1α (#3294), CHOP (#5554), ATF6 (#65880), Histone H3 (#9715), IRS-1 (#2382), phosphor-IRS-1 (Ser307), JNK (#9252), phosphor-JNK (Thr183/Tyr185) (#4668), NF-κB p65 (#4764), phosphor-NF-κB p65 (Ser536) (#3033), and IκBα (#9242) were from Cell Signaling TECHNOLOGY (Beverly, MA, United States). Anti-PERK (phosphor T982) (ab192591), STAT3 (ab119352), STAT3 (phosphor Y705) (ab76315), and SOCS3 (ab16030) antibodies were obtained from Abcam, Inc. (Cambridge, MA, United States). Anti-IL-6 mouse monoclonal antibody (sc-57315) and normal mouse IgG (sc-2025) were purchased from Santa Cruz Biotechnology (Shanghai) Co., Ltd. (Shanghai, China). Insulin (91077C), palmitic acid (P5585), and icariin (I1286) were acquired from Sigma-Aldrich, Corp. (St. Louis, MO, United States). 2-Deoxy-D-2-[3H] glucose was obtained from HTA, Co. Ltd. (Beijing, China).

Li M., Zhang Y., Cao Y., Zhang D., Liu L., Guo Y, & Wang C. (2018). Icariin Ameliorates Palmitate-Induced Insulin Resistance Through Reducing Thioredoxin-Interacting Protein (TXNIP) and Suppressing ER Stress in C2C12 Myotubes. Frontiers in Pharmacology, 9, 1180.

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Insulin Signaling Pathway Regulation

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Immunoblotting Analysis of Cell Lysates

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Cell lysates after various treatments were prepared and subjected to IB analysis as described (Gu et al., 2007 (link)). The sources of primary antibodies were as follows: Cullin-1 (Santa Cruz, CA), phospho-AKT-Ser473, phosphor-AKT-Thr308, pan-AKT, AKT1, AKT2, AKT3, Aurora A, VHL, Phospho-Aurora A (Thr288)/Aurora B (Thr232)/Aurora C (Thr198) (D13A11), PDK1, phospho-PDK1-Ser²⁴¹ and Rictor (53A2) (Cell Signaling, Denver, CO), γ-tubulin, α-tubulin Clone AA13, acetylated tubulin Clone 6-11B-1, β-actin (Sigma, St. Louis, MO), CP110, NDE1, Cep97, Arl13B (Proteintech, Wuhan, P.R.C). UBA3 (Abcam, Shanghai, P.R.C). EGFR and phospho-EGFR-Tyr845 were gifts from Dr. Wanhong Xu,

Mao H., Tang Z., Li H., Sun B., Tan M., Fan S., Zhu Y, & Sun Y. (2019). Neddylation inhibitor MLN4924 suppresses cilia formation by modulating AKT1. Protein & Cell, 10(10), 726-744.

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