Overview

Description

  • Nature
    Synthetic
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      C-LINGESG QAKRN
    • Amino acids
      864 to 875

Associated products

Specifications

Our Abpromise guarantee covers the use of ab45684 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Blocking - Blocking peptide for Anti-PDE5A antibody (ab28761)

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

General Info

  • Alternative names
    • 5''-cyclic phosphodiesterase
    • CGB PDE
    • CGB-PDE
    • CGBPDE
    • cGMP binding cGMP specific 3' 5' cyclic nucleotide phosphodiesterase
    • cGMP binding cGMP specific 35 cyclic nucleotide phosphodiesterase
    • cGMP binding cGMP specific phosphodiesterase
    • cGMP binding/cGMP specific phosphodiesterase
    • cGMP specific 3'5' cyclic phosphodiesterase
    • cGMP specific phosphodiesterase PDE5A2
    • cGMP specific phosphodiesterase type 5A
    • cGMP-binding cGMP-specific phosphodiesterase
    • cGMP-specific 3''
    • CN5A
    • CN5N
    • PDE 5
    • PDE 5A
    • PDE5
    • Pde5a
    • PDE5A_HUMAN
    • PDE5A1
    • Phosphodiesterase 5A
    • Phosphodiesterase 5A cGMP specific
    • Phosphodiesterase isozyme 5
    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
    modifications
    Phosphorylation is regulated by binding of cGMP to the two allosteric sites.
  • Information by UniProt

References

ab45684 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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