Analytical Data
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Gene name
PDE1A
- Application
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Alternative Names
hCam-1; 61 kDa Cam-PDE; Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
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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
P54750
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Expression Region
Gly2~Asp318
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Molecular Weight
40kDa
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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
Related Products
Protein Description
PDE1A, or phosphodiesterase 1A, is an enzyme that plays a critical role in the hydrolysis of cyclic nucleotides, specifically cAMP and cGMP, thereby regulating various physiological processes, including cellular signaling, muscle contraction, and neuronal communication. Research into PDE1A has gained traction due to its involvement in several pathological conditions, such as cardiovascular diseases, neurodegenerative disorders, and certain types of cancer. Its dual substrate specificity has made it a candidate for therapeutic targeting, prompting the development of selective inhibitors that may offer benefits over broader PDE inhibitors by minimizing side effects. Additionally, the understanding of its structural dynamics and regulatory mechanisms is crucial for the design of such inhibitors. Recent advancements in recombinant protein technology have facilitated the expression and purification of PDE1A, allowing for detailed biochemical studies and the exploration of its interactions with other cellular molecules. Consequently, PDE1A serves not only as a valuable biomarker for disease states but also as a potential therapeutic target, making its research pivotal in the fields of pharmacology and molecular medicine.
