Analytical Data
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Gene name
cia
- Application
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Species
Escherichia coli
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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
P06716
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Expression Region
282-385aa
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Molecular Weight
15.7 kDa
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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
Cyclic AMP (cAMP) is a critical second messenger that plays a pivotal role in various cellular processes, including energy metabolism, gene expression, and cell signaling. The regulation of cAMP levels is essential for maintaining cellular homeostasis and is often disrupted in various diseases, including cancer and heart conditions. One of the key enzymes involved in cAMP metabolism is phosphodiesterase (PDE), which hydrolyzes cAMP to AMP, thereby terminating its signaling effects. The study of cyclic AMP signal transduction has led to significant advancements in understanding how cells communicate and respond to external stimuli. Researchers have focused on the development and characterization of cyclic AMP-related proteins, such as cAMP-dependent protein kinases (PKA) and exchange proteins activated by cAMP (Epac), as these proteins mediate the diverse physiological effects of cAMP. The reconstitution of these proteins in vitro allows scientists to dissect their structural and functional properties, elucidating how cAMP modulates various signaling pathways. Additionally, investigating the interactions between cAMP and its effector proteins has implications for therapeutic interventions, particularly in targeting diseases associated with aberrant cAMP signaling. Therefore, the study of cAMP-related proteins is not only fundamental to basic biological research but also holds great promise for developing novel drug therapies aimed at restoring proper cellular function.
