Analytical Data
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Gene name
CAMKK2
- Application
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Alternative Names
CAMKK; CAMKKB; Calcium/calmodulin-dependent protein kinase kinase beta
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Species
Human
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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
Q96RR4
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Expression Region
Met1~Gly332
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Molecular Weight
43kDa
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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
CAMKK2 (Calcium/Calmodulin-dependent protein kinase kinase 2) is a key enzyme involved in the regulation of cellular responses to calcium signaling and is critically implicated in various physiological processes, including metabolism, neuronal function, and muscle contraction. Its role in cellular signaling pathways, particularly in the activation of AMP-activated protein kinase (AMPK), makes CAMKK2 a significant focus in the study of metabolic disorders, diabetes, and neurodegenerative diseases. The recombinant expression of CAMKK2 protein has become vital for understanding its biochemical properties, substrate interactions, and regulatory mechanisms. In research, producing a functional recombinant CAMKK2 protein enables scientists to investigate its structure-function relationships and to develop potential therapeutic strategies targeting diseases linked to dysfunctional calcium signaling. Furthermore, the ability to manipulate CAMKK2 activity through precise biochemical assays can lead to insights into its potential role as a drug target, facilitating the discovery of novel pharmacological agents aimed at modulating its activity in various pathological conditions. Overall, the study of recombinant CAMKK2 not only advances our understanding of calcium-mediated signaling pathways but also holds promise for innovative therapeutic interventions in health and disease.











