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AB125581

Recombinant human PDE5A/PDE5 protein

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(1 Publication)

Recombinant human PDE5A/PDE5 protein is a Human Fragment protein, in the 537 to 875 aa range, expressed in Baculovirus infected Sf9 cells, with >90%, suitable for SDS-PAGE, FuncS.

View Alternative Names

PDE5, PDE5A, cGMP-binding cGMP-specific phosphodiesterase, CGB-PDE

4 Images
Functional Studies - Recombinant human PDE5A/PDE5 protein (AB125581)
  • FuncS

Unknown

Functional Studies - Recombinant human PDE5A/PDE5 protein (AB125581)

The specific activity of ab125581 was determined to be 2275 nmol/min/mg.

Functional Studies - Recombinant human PDE5A/PDE5 protein (AB125581)
  • FuncS

Unknown

Functional Studies - Recombinant human PDE5A/PDE5 protein (AB125581)

The specific activity of PDE5A/PDE5 (ab125581) was determined to be 1940 nmol/min/mg as per activity assay protocol

SDS-PAGE - Recombinant human PDE5A/PDE5 protein (AB125581)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PDE5A/PDE5 protein (AB125581)

SDS PAGE analysis of ab125581

SDS-PAGE - Recombinant human PDE5A/PDE5 protein (AB125581)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PDE5A/PDE5 protein (AB125581)

SDS Page analysis of ab125581

Key facts

Purity

>90% Densitometry

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

The specific activity of ab125581 was determined to be 2275 nmol/min/mg.

Accession

O76074

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.79% Tris HCl, 0.5% Magnesium chloride, 0.29% Sodium chloride, 0.003% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

This product was previously labelled as PDE5A

Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":"63 kDa","actualMolecularWeight":null,"aminoAcidEnd":875,"aminoAcidStart":537,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"O76074","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PDE5A also known as PDE5 or phosphodiesterase type 5 plays a critical role in hydrolyzing cyclic guanosine monophosphate (cGMP) to its inactive form. This enzyme is part of the phosphodiesterase family and has a molecular mass of approximately 100 kDa. PDE5A is expressed mainly in the smooth muscle cells of blood vessels and in the corpus cavernosum of the penis. Other expression sites include the lung heart and skeletal muscle.
Biological function summary

PDE5A regulates intracellular levels of cGMP an important secondary messenger in various signaling pathways. It is not part of a large protein complex but directly influences the contractility of smooth muscle tissues. By controlling cGMP levels PDE5A modulates vascular tone and influences processes such as vasodilation. This regulation is essential for maintaining a balance in the contractile state of muscles impacting blood flow and other vital functions.

Pathways

PDE5A contributes significantly to the nitric oxide (NO)-cGMP signaling pathway which is important for vascular relaxation. In this pathway nitric oxide stimulates guanylate cyclase to produce cGMP which then activates specific kinases and ion channels. Related proteins such as guanylate cyclase and cGMP-dependent protein kinases work alongside PDE5A to mediate smooth muscle relaxation and vasodilation particularly in penile erectile tissue.

PDE5A shows strong connections to erectile dysfunction and pulmonary hypertension. In the case of erectile dysfunction impaired regulation of cGMP by PDE5A affects the relaxation of smooth muscle leading to inadequate blood flow. Pulmonary hypertension involves elevated blood pressure in the lung arteries which PDE5A influences through its role in controlling vascular tone. The enzyme guanylate cyclase associates closely with PDE5A in these contexts as both influence cGMP pathways involved in these conditions.

Specifications

Form

Liquid

Additional notes

The purity was determined to be 95% by densitometry. Affinity purified.

General info

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 (PubMed : 15489334, PubMed : 9714779). Specifically regulates nitric-oxide-generated cGMP (PubMed : 15489334).

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Post-translational modifications

Phosphorylation is regulated by binding of cGMP to the two allosteric sites (By similarity). Phosphorylation by PRKG1 leads to its activation.

Product protocols

Target data

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 (PubMed : 15489334, PubMed : 9714779). Specifically regulates nitric-oxide-generated cGMP (PubMed : 15489334).
See full target information PDE5A

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

PloS one 14:e0222803 PubMed31539416

2019

Exploration of icariin analog structure space reveals key features driving potent inhibition of human phosphodiesterase-5.

Applications

Unspecified application

Species

Unspecified reactive species

Yasmin Chau,Fu-Shuang Li,Olesya Levsh,Jing-Ke Weng
View all publications

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