Rabbit anti ampkβ1 2

Manufactured by Cell Signaling Technology

Sourced in United States

Rabbit anti-AMPKβ1/2 is a primary antibody that specifically recognizes the AMPKβ1 and AMPKβ2 subunits of the AMP-activated protein kinase (AMPK) complex. AMPK is a key cellular energy sensor that plays a crucial role in regulating cellular metabolism.

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Lab products found in correlation

Rabbit anti ampkα, by Cell Signaling Technology (1 mentions) Rabbit anti p ampkα, by Cell Signaling Technology (1 mentions) Rabbit anti acc, by Cell Signaling Technology (1 mentions) Rabbit anti lkb1, by Cell Signaling Technology (1 mentions) Rabbit anti pthr172, by Cell Signaling Technology (1 mentions) Rabbit anti ampkα2, by Cell Signaling Technology (1 mentions) Rabbit anti pacc, by Cell Signaling Technology (1 mentions) Rabbit anti ampkα1, by Cell Signaling Technology (1 mentions) Mouse anti vinculin, by Merck Group (1 mentions)

2 protocols using rabbit anti ampkβ1 2

AMPK Signaling Pathway Characterization

Cited 1 time

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OFs were lysed and processed as described previously.²⁰ (link) Antibodies targeting p-AMPKα (rabbit anti-p-AMPKα), AMPKα (rabbit anti-AMPKα), p-AMPKβ (rabbit anti-p-AMPKβ), AMPKβ1/2 (rabbit anti-AMPKβ1/2), p-ACC (rabbit anti-p-ACC), ACC (rabbit anti-ACC), and β-tubulin (rabbit anti-β-tubulin) were all obtained from Cell Signaling Technology (Danvers, MA, USA), and AMPKβ (mouse anti-AMPKβ) was obtained from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

Hammond C.L., Roztocil E., Gonzalez M.O., Feldon S.E, & Woeller C.F. (2021). MicroRNA-130a Is Elevated in Thyroid Eye Disease and Increases Lipid Accumulation in Fibroblasts Through the Suppression of AMPK. Investigative Ophthalmology & Visual Science, 62(1), 29.

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AMPK Purification and Phosphorylation

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Recombinant His-tagged AMPK complexes were expressed in Escherichia coli and purified by chromatography on nickel-Sepharose [9 (link)]. AMPK was phosphorylated on Thr¹⁷² by overnight incubation with MgATP and CaMKKβ, and repurified as previously described [9 (link)]. Subsequent incubation with MgATP and CaMKKβ did not increase Thr¹⁷² phosphorylation, demonstrating that Thr¹⁷² is maximally phosphorylated using these conditions. The following antibodies were from Cell Signaling: rabbit anti-AMPKα1 (#2795), rabbit anti-AMPKα2 (#2757), mouse anti-AMPKα1/2 (#2793), rabbit anti-AMPKβ1/2 (#4150), rabbit anti-ACC (#3676), rabbit anti-pACC (#3661), rabbit anti-AMPKγ1 (#4187), rabbit anti-LKB1 (#3050) and rabbit anti-pThr¹⁷² (#2535). Mouse anti-vinculin was from Sigma–Aldrich (V9131). Mouse monoclonal anti-CaMKKβ antibody was a generous gift from Prof. Grahame Hardie (Dundee University).

Willows R., Sanders M.J., Xiao B., Patel B.R., Martin S.R., Read J., Wilson J.R., Hubbard J., Gamblin S.J, & Carling D. (2017). Phosphorylation of AMPK by upstream kinases is required for activity in mammalian cells. Biochemical Journal, 474(17), 3059-3073.

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