Analytical Data
-
Gene name
cGB-PDE
- Application
-
Alternative Names
cGMP-binding cGMP-specific phosphodiesterase (CGB-PDE) (Pde5)
-
Species
Mouse
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8CG03
-
Expression Region
154-320aa
-
Molecular Weight
26.1 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Cyclic guanosine monophosphate phosphodiesterase (cGB-PDE) is an enzyme that plays a crucial role in the regulation of intracellular levels of cyclic guanosine monophosphate (cGMP), a second messenger involved in various physiological processes, including vasodilation, neuronal signaling, and cell growth. The study of cGB-PDE has gained significant attention due to its potential implications in cardiovascular diseases, neurological disorders, and cancer. Abnormal cGMP signaling often indicates pathological conditions, making cGB-PDE a promising target for therapeutic interventions. Recent advancements in structural biology, particularly in recombinant protein technology, have enabled researchers to produce functional cGB-PDE proteins for detailed biochemical characterization and structure-function studies. This recombinant approach allows for the exploration of cGB-PDE's catalytic mechanisms, regulation, and interactions with other cellular components. Furthermore, understanding the molecular dynamics of cGB-PDE may provide insights into its role in drug development, enabling the design of selective inhibitors or activators for specific therapeutic applications. Ongoing research aims to elucidate the regulatory pathways involving cGB-PDE, thereby contributing to the development of innovative strategies for treating diseases associated with cGMP dysregulation. In summary, the investigation into recombinant cGB-PDE proteins offers a promising avenue for advancing our understanding of cGMP signaling and its therapeutic potential, highlighting the importance of this enzyme in both basic and applied biomedical research.
