C9869
CAMK2α, active, GST tagged human
PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
CAMKA, KIAA0968
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
recombinant
expressed in baculovirus infected Sf9 cells
Quality Level
product line
PRECISIO® Kinase
Assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
218-294 nmol/min·mg
mol wt
~74 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... CAMK2A(815)
Biochem/physiol Actions
CAMK2α is a ser/thr protein kinase that is a member of the Ca2+/calmodulin-dependent protein kinase family. CAMK2α is abundant in the brain as a major constituent of the postsynaptic density and is required for hippocampal long-term potentiation (LTP) and spatial learning. In addition to its CaCa2+/calmodulin-dependent activity, CAMK2α can undergo autophosphorylation, resulting in Ca2+/calmodulin-independent activity. The protein level of CAMK2α fluctuates during neuronal activity in cultured rat pup hippocampal neurons. The levels of CAMK2α increased with heightened neuronal activity.
Physical form
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.
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Tara C Thiagarajan et al.
Neuron, 36(6), 1103-1114 (2002-12-24)
We show that alpha and betaCaMKII are inversely regulated by activity in hippocampal neurons in culture: the alpha/beta ratio shifts toward alpha during increased activity and beta during decreased activity. The swing in ratio is approximately 5-fold and may help
A J Silva et al.
Science (New York, N.Y.), 257(5067), 206-211 (1992-07-10)
Although long-term potentiation (LTP) has been studied as the mechanism for hippocampus-dependent learning and memory, evidence for this hypothesis is still incomplete. The mice with a mutation in the alpha-calcium-calmodulin-dependent kinase II (alpha-CaMKII), a synaptic protein enriched in the hippocampus
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