CAMK2A/CAMK2D (Phospho-Thr286) ELISA Kit (DEIA-XYA332)

Regulatory status: For research use only, not for use in diagnostic procedures.

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Size
2 x 96T
Sample
cultured cells
Species Reactivity
Human, Mouse, Rat
Intended Use
The CAMK2 (Phospho-Thr286) Cell-Based ELISA Kit is a convenient, lysate-free, high throughput and sensitive assay kit that can monitor CAMK2 protein phosphorylation and expression profile in cells. The kit can be used for measuring the relative amounts of phosphorylated CAMK2 in cultured cells as well as screening for the effects that various treatments, inhibitors (ie. siRNA or chemicals), or activators have on CAMK2 phosphorylation.
Contents of Kit
1. 96-Well Cell Culture Clear-Bottom Microplate: 2 plates
2. 10x TBS: 24 mL (10x)
3. Quenching Buffer: 24 mL (1x)
4. Blocking Buffer: 50 mL (1x)
5. 10x Wash Buffer: 50 mL (10x)
6. 100x Anti-CAMK2 (Phospho-Thr286) Antibody (Rabbit Polyclonal): 60 μL (100x), Red
7. 100x Anti-CAMK2 Antibody (Rabbit Polyclonal): 60 μL (100x), Purple
8. 100x Anti-GAPDH Antibody (Mouse Monoclonal): 60 μL (100x), Green
9. HRP-Conjugated Anti-Rabbit IgG Antibody: 12 mL (1x), Glass
10. HRP-Conjugated Anti-Mouse IgG Antibody: 12 mL (1x), Glass
11. Primary Antibody Diluent: 12 mL (1x)
12. Ready-to-Use Substrate: 12 mL (1x), Brown
13. Stop Solution: 12 mL (1x)
14. Crystal Violet Solution: 12 mL (1x), Glass
15. SDS Solution: 24 mL (1x)
16. Adhesive Plate Seals: 4 seals
Storage
4°C/6 Months

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References


Lack of Neuronal Glycogen Impairs Memory Formation and Learning-Dependent Synaptic Plasticity in Mice

FRONTIERS IN CELLULAR NEUROSCIENCE

Authors: Duran, Jordi; Gruart, Agnes; Varea, Olga; Lopez-Soldado, Iliana; Delgado-Garcia, Jose M.; Guinovart, Joan J.

Since brain glycogen is stored mainly in astrocytes, the role of this polysaccharide in neurons has been largely overlooked. To study the existence and relevance of an active neuronal glycogen metabolism in vivo, we generated a mouse model lacking glycogen synthase specifically in the Camk2a-expressing postnatal forebrain pyramidal neurons (GYS1(Camk2a-KO)), which include the prefrontal cortex and the CA3 and CA1 cell layers of the hippocampus. The latter are involved in memory and learning processes and participate in the hippocampal CA3-CA1 synapse, the function of which can be analyzed electrophysiologically. Long-term potentiation evoked in the hippocampal CA3-CA1 synapse was decreased in alert behaving GYS1(Camk2a-KO) mice. They also showed a significant deficiency in the acquisition of an instrumental learning task - a type of associative learning involving prefrontal and hippocampal circuits. Interestingly, GyS1(Camk2a-KO) animals did not show the greater susceptibility to hippocampal seizures and myoclonus observed in animals completely depleted of glycogen in the whole CNS. These results unequivocally demonstrate the presence of an active glycogen metabolism in neurons in vivo and reveal a key role of neuronal glycogen in the proper acquisition of new motor and cognitive abilities, and in the changes in synaptic strength underlying such acquisition.

Overexpression of type-1 adenylyl cyclase in mouse forebrain enhances recognition memory and LTP

NATURE NEUROSCIENCE

Authors: Wang, HB; Ferguson, GD; Pineda, VV; Cundiff, PE; Storm, DR

Cyclic AMP is a positive regulator of synaptic plasticity and is required for several forms of hippocampus-dependent memory including recognition memory. The type I adenylyl cyclase, Adcy1 (also known as AC1), is crucial in memory formation because it couples Ca2+ to cyclic AMP increases in the hippocampus. Because Adcy1 is neurospecific, it is a potential pharmacological target for increasing cAMP specifically in the brain and for improving memory. We have generated transgenic mice that overexpress Adcy1 in the forebrain using the Camk2a (also known as alpha-CaMKII) promoter. These mice showed elevated long-term potentiation (LTP), increased memory for object recognition and slower rates of extinction for contextual memory. The increase in recognition memory and lower rates of contextual memory extinction may be due to enhanced extracellular signal-related kinase (ERK)/mitogen-activated protein kinase (MAPK) signaling, which is elevated in mice that overexpress Adcy1.

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