Recombinant human PDE5A/PDE5 protein (ab56614)
Key features and details
- Expression system: Baculovirus infected Sf9 cells
- Purity: > 40% SDS-PAGE
- Active: Yes
- Tags: GST tag N-Terminus
- Suitable for: Functional Studies
Description
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Product name
Recombinant human PDE5A/PDE5 protein
See all PDE5A/PDE5 proteins and peptides -
Biological activity
Specific Activity: ≥ 3,100 pmole/min/µg
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Purity
> 40 % SDS-PAGE.
Affinity purified. -
Expression system
Baculovirus infected Sf9 cells -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Tags
GST tag N-Terminus
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab56614 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Functional Studies
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Form
Liquid -
Additional notes
This product was previously labelled as PDE5A
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
pH: 8.00
Constituents: 0.1535% Glutathione, 0.0462% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.395% Tris HCl, 0.05% Tween, 50% Glycerol (glycerin, glycerine), 0.58% Sodium chlorideThis product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
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Alternative names
- 5''-cyclic phosphodiesterase
- CGB PDE
- CGB-PDE
see all -
Function
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. -
Tissue specificity
Expressed in aortic smooth muscle cells, heart, placenta, skeletal muscle and pancreas and, to a much lesser extent, in brain, liver and lung. -
Pathway
Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1. -
Sequence similarities
Belongs to the cyclic nucleotide phosphodiesterase family.
Contains 2 GAF domains. -
Domain
Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain which contains two homologous allosteric cGMP-binding regions, A and B. -
Post-translational
modificationsPhosphorylation is regulated by binding of cGMP to the two allosteric sites. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (0)
ab56614 has not yet been referenced specifically in any publications.