BACKGROUND Calcium/Calmodulin-dependent kinases (CaMK) are a family of serine/threonine kinases that mediate many of the second messenger effects of Ca2+. At basal Ca2+ levels, CaMKs are maintained in a dormant state through autoinhibition. An increase in Ca2+ levels allows calmodulin to relieve this autoinhibition and activate the kinase activity. There are two main classes of CaMKs; mulitfunctional CaMKs (CaMKK, CaMKI, CaMKII and CaMKIV) which have multiple downstream targets and substrate-specific CaMKs (CaMKIII) which have only one known downstream target. All CaMKs, with the exception of CaMKII, exist as monomers and most are expressed ubiquitously. Some subtypes display specific distributions, for example, CaMKIVbeta is expressed exclusively in cerebellar granule cells. CaMKs have numerous cellular functions and they influence processes as diverse as gene transcription, cell survival, apoptosis, cytoskeletal re-organization and learning and memory.1
CaMKI is a monomeric enzyme of ∼42 kDa that has widespread tissue distribution and that can phosphorylate a number of substrates including synapsin I, synapsin II, and CREB, the cAMP-response element-binding protein.2 CaMKI exhibits complex regulation by Ca2+-CaM. On the one hand, Ca2+-CaM directly activates CaMKI through relief of intrasteric autoinhibition. In addition, CaMKI is strongly dependent for its activity upon its Ca2+-CaM –dependent phosphorylation by a kinase kinase, CaMKI kinase (CaMKIK). Activation results from the phosphorylation by CaMKIK of a single residue, Thr-177 located in the “activation loop” of CaMKI.3
1. Lisman, J. et al:Nature Rev. Neurosci. 3:175-189, 2002
2. Matsushita, M. & Nairn, A.C.: J. Biol. Chem. 273:21473-81, 1998
3. Aletta, J. M. et al: J. Biol. Chem. 271:20930-34, 1996
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|Anti-CaMK 1: Anti-CaMK I||Size: 100 ul||CAT.#: CG1060||Price: $325.00|