免疫原
Synthesized phosho peptide around human CaMKK2 (Ser511)
特异性
This antibody detects endogenous levels of Human Mouse Rat CaMKK2 (phospho-Ser511)
组成（Formulation）
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
纯化工艺（Immunogen）
The antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
背景（Background）
The product of this gene belongs to the Serine/Threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. The major isoform of this gene plays a role in the calcium/calmodulin-dependent (CaM) kinase cascade by phosphorylating the downstream kinases CaMK1 and CaMK4. Protein products of this gene also phosphorylate AMP-activated protein kinase (AMPK). This gene has its strongest expression in the brain and influences signalling cascades involved with learning and memory, neuronal differentiation and migration, neurite outgrowth, and synapse formation. Alternative splicing results in multiple transcript variants encoding distinct isoforms. The identified isoforms differ in their ability to undergo autophosphorylation and to phosphorylate downstream kinases. [provided by RefSeq, Jul 2012],
功能
catalytic activity:ATP + a protein = ADP + a phosphoprotein.,domain:The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.,domain:The RP domain (arginine/proline-rich) is involved in the recognition of CAMKI and CAMK4 as substrates.,enzyme regulation:Activated by Ca(2+)/calmodulin. Binding of calmodulin may releave intrasteric autoinhibition. Autophosphorylation does not alter activity or regulation by Ca(2+)/calmodulin. In part, activity is independent on Ca(2+)/calmodulin.,function:Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. See
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