Ampkβ

Manufactured by Cell Signaling Technology

Sourced in United States

AMPKβ is a subunit of the AMP-activated protein kinase (AMPK) complex. AMPK is a critical cellular energy sensor that plays a key role in regulating metabolism and cellular homeostasis. The AMPKβ subunit is responsible for binding to the AMPK complex and regulating its activity.

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P-AMPKβ (3 citations) Anti-human AMPKβ−1 (2 citations)

4 protocols using ampkβ

Protein Isolation and Western Blot Analysis

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Protein isolation and western blot analysis were performed as described in literature (Wu et al., 2010 (link)). Briefly, protein samples were placed in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and blotted onto polyvinylidene difluoride membranes. The membranes were blocking with non-fat dry milk for 1 h and incubated at room temperature for 2 h with p-LKB1, LKB1, p-AMPKα, AMPKα, p-AMPKβ, AMPKβ, p-ACC, ACC (Cell Signaling Technology, Boston, MA, USA) or SREBP-1, CYP2E1, GAPDH, Sirt1, PPARγ (Abcam, Cambridge, MA, USA) or caspase-1, β-actin, PPARα (Santa Cruz, CA, USA) or IL-1β (R&D Systems Europe Ltd., Abingdon, UK). Then the membranes were followed by incubated with HRP-conjugated secondary antibody for 1 h at room temperature and visualized by ECL Prime Western Blotting Detection Reagent (Bio-Rad, USA).

Yao Y.L., Han X., Li Z.M., Lian L.H., Nan J.X, & Wu Y.L. (2017). Acanthoic Acid Can Partially Prevent Alcohol Exposure-Induced Liver Lipid Deposition and Inflammation. Frontiers in Pharmacology, 8, 134.

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Western Blot Analysis of Metabolic Proteins

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Proteins were resolved on 10–12% (w/v) NuPAGE BisTris gels in 3‐(N‐morpholino)propanesulfonic acid buffer (Life Technologies) and transferred to polyvinylidene fluoride membrane. Proteins were analysed by western blot using the following antibodies: phospho‐acetyl‐CoA carboxylase, AMPKα (pT172) and AMPKβ (all at 1 : 1000; Cell Signaling Technology, Beverly, MA, USA).

Rousset C.I., Leiper F.C., Kichev A., Gressens P., Carling D., Hagberg H, & Thornton C. (2015). A dual role for AMP‐activated protein kinase (AMPK) during neonatal hypoxic–ischaemic brain injury in mice. Journal of Neurochemistry, 133(2), 242-252.

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Liver Protein Expression Analysis

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Western blots (WBs) were performed in liver samples homogenized in buffer A. Homogenates were centrifuged at 16 000 g for 15 min at 4 °C. Proteins were resolved in 10% or 15% acrylamide gels for SDS/PAGE and transferred to Immobilon membranes (Millipore, Sigma-Aldrich). The following antibodies were used: PEPCK (a kind gift from Dr. E. Beale); p-FoxO1 Thr24 (9464, Cell Signaling, Danvers, MA, USA); FoxO1 (9454, Cell Signaling); GK (peptide 414–428 raised by Sigma Genosys (Cambridge, UK)); p-AMPKβ Ser108 (4181, Cell Signaling); AMPKβ (4150, Cell Signaling); p-AMPKα Thr172 (2531, Cell Signaling); AMPKα (2532, Cell Signaling); p-AKT Thr308 (4056, Cell Signaling); p-AKT Ser473 (9271, Cell Signaling); AKT (9272, Cell Signaling); p-GSK3β Ser9 (9336, Cell Signaling); and GSK3β (sc7291, Santa Cruz, Dallas, TX, USA). Proteins were detected by the ECL method (Immobilon Western Chemiluminescent HRP Substrate, Millipore, Sigma-Aldrich). Loading control of the WB membrane was performed using the REVERT total protein stain.

López-Soldado I., Bertini A., Adrover A., Duran J, & Guinovart J.J. (2020). Maintenance of liver glycogen during long-term fasting preserves energy state in mice. FEBS letters, 594(11), 1698-1710.

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Comprehensive Protein Profiling in Mouse Liver

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Total protein lysates from mouse livers were prepared in a radioimmunoprecipitation assay buffer, fractionated on 8–12% SDS-PAGE, and transferred to a PVDF membrane. Membranes were blocked in Tris-buffered saline, 0.1% Tween buffer containing 5% non-fat dry milk, and then incubated with an indicated primary antibody followed by incubation with a secondary antibody conjugated to horseradish peroxidase. Membrane-bound immune complexes were detected with an enhanced chemiluminescence kit (Thermo Fisher). The antibodies used in this study are as follows: GS, phospho-GS (p-GS), insulin receptor substrate 1 (IRS1), insulin receptor β (IRβ), p-IRβ, AKT serine/threonine kinase (AKT), p-AKT, extracellular signal-regulated kinase (ERK), p-ERK, AMPKα, p-APMKα, and AMPKβ from Cell Signaling; calcium/calmodulin-dependent protein kinase kinase 2 (CaMKK2) from BD Biosciences; TUBULIN from Sana Cruz Biotechnology; β-ACTIN from Sigma.

Tran M., Gilling S., Wu J., Wang L, & Shin D.J. (2024). miR-141/200c contributes to ethanol-mediated hepatic glycogen metabolism. Molecular Metabolism, 84, 101942.

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