CAMKK1 or CAMKKalpha is a Ca2+/calmodulin-dependent protein kinase that activates CAM-kinases I and IV via phosphorylation of their Thr(177) and Thr(196) residues, respectively. Recent studies have shown that the activity of CAMKK1 is decreased upon phosphorylation by cAMP-dependent protein kinase (PKA). The CAMKKalpha has been identified in intact cells as AMPKKs, predicting a significant role for this kinase in regulating AMPK activity in vivo. It has been shown that 2-deoxyglucose- and ionomycin-stimulated AMPK activity is substantially reduced in HeLa cells transfected with small interfering RNAs specific for CAMKKalpha.
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Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.2 5mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.
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The Journal of biological chemistry, 280(32), 29060-29066 (2005-06-28)
The AMP-activated protein kinase (AMPK) is an important regulator of cellular metabolism in response to metabolic stress and to other regulatory signals. AMPK activity is absolutely dependent upon phosphorylation of AMPKalphaThr-172 in its activation loop by one or more AMPK
Journal of biochemistry, 130(4), 503-513 (2001-09-28)
Ca(2+)/calmodulin-dependent protein kinases (CaM-kinases) I and IV are activated upon phosphorylation of their Thr(177) and Thr(196), respectively, by the upstream Ca(2+)/calmodulin-dependent protein kinases CaM-kinase kinase alpha and beta, and deactivated upon dephosphorylation by protein phosphatases such as CaM-kinase phosphatase. Recent
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