Analytical Data
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Gene name
CAMK2a
- Application
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Alternative Names
CAMKA
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
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Expression Region
Met1~Pro477
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Molecular Weight
58kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
CAMK2A, or calcium/calmodulin-dependent protein kinase II alpha, is a key enzyme involved in various cellular processes, particularly in neurons where it plays a critical role in synaptic plasticity and memory formation. Research on CAMK2A has gained momentum due to its implications in neurodegenerative diseases and psychiatric disorders, such as schizophrenia and Alzheimer’s disease. The protein functions as a multifunctional serine/threonine kinase and is activated by calcium-bound calmodulin, allowing it to phosphorylate target proteins in response to calcium signaling. Its unique structure, comprising a regulatory and a catalytic domain, enables it to form oligomers, which is essential for its persistent activity during neuronal signaling. Scientists utilize recombinant CAMK2A to gain insights into its biochemical properties, allosteric regulation, and interaction with various substrates and pathways. Studies often involve the production of the protein through recombinant DNA technology, allowing for detailed analysis of its activity, phosphorylation sites, and the effects of mutations. By exploring CAMK2A's role in signaling cascades and its function in synaptic adjustments, researchers hope to elucidate the mechanisms underlying learning and memory while also identifying potential therapeutic targets for associated pathologies. Understanding CAMK2A's dynamics at both molecular and cellular levels is imperative for developing strategies to mitigate its dysregulation in disease contexts. Overall, CAMK2A remains a focal point in neurobiology research, representing a crucial integrator of calcium signaling in the brain.
