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| AlternativeName: | Calcium/calmodulin-dependentproteinkinaseII |
| Clone: | 6G9 |
| Host: | Mouse |
| Isotype: | IgG1 |
| Immunogen: | RatCaMKII(partiallypurified). |
| UniProtID: | P15791 |
| GenBankID: | J05072 |
| Speciesreactivity: | Mouse,Rat |
| Applications: | IHC,WB invitroAssay |
| RecommendedDilutions/Conditions: | WesternBlot(Colorimetric,1:1,000) Suggesteddilutions/conditionsmaynotbeavailableforallapplications. Optimalconditionsmustbedeterminedindividuallyforeachapplication. |
| ApplicationNotes: | Detectsabandof~50-60kDabyWesternblot. |
| PurityDetail: | ProteinGaffinitypurified. |
| Formulation: | Liquid.InPBScontaining50%glyceroland0.09%sodiumazide. |
| Shipping: | ShippedonBlueIce |
| LongTermStorage: | -20°C |
| ScientificBackground: | CaMKIIa,thealphasubunitofCa<sup>2+</sup>calmodulin-dependentproteinkinaseIIispartofafamilyofmultifunctionalproteinkinases,whichplayamajorroleinCa<sup>2+</sup>-mediatedsignaltransduction. CaMKIIaisexpressedinmanydifferenttissuesbutisspecificallyfoundintheneuronsoftheforebrainanditsmRNAisfoundwithinthedendritesaswellasthesomaoftheneuron. TheneuronalCaMKIIconsistsoftwomajorsubunitsof52and60kDawhichareencodedbya-andb-CaMKIIgenes,respectively. Additionalisoformsaregeneratedbyalternativesplicingoftheseaswellasoftheubiquitiousg-andd-CaMKIIgenes. EachsubunithasanATP-bindingdomain(arginine-X-X-serune/threonine),consensusphosphorylationsite,catalyticdomain,andacentrallylocatedregulatorydomainwhichhascalmodulinbindingactivity.ActivationandautophosphorylationofCaMKIImayregulatenumerousneuronalprocesseswhichincludestwoformsofsynapticplasticity,longtermpotentiationandlongtermdepression. NeuronalCaMKIIsubunitsassembleaslargemultimericholoenzymes. TheC-terminalassociationdomainsof 6-12subunitsassembleintoacentralglobularstructurefromwhichtheN-terminalcatalytic/regulatorydomainsextendradiallylikepetalsofaflower.ThesubunitcompositionoftheratforebrainCaMKIIholoenzymeconsistsofheteromerscomposedofaandβsubunitsataratioof2:1andhomomerscomposedofonlyasubunits. TheassociationofCaMKIIsubunitsleadstothepositioningoftheircatalytic/regulatorydomainsincloseproximityandtheneighboringcalmodulin-boundsubunitscooperatetorapidlyphosphorylateeachother. AutophosphorylationalsoenablesCaMKIItoattainanenhancedaffinityforNMDAreceptorsinpostsynapticdensities. |