• NatureRecombinant
  • SourceBaculovirus infected Sf9 cells
  • Amino Acid Sequence
    • SpeciesHuman


Our Abpromise guarantee covers the use of ab80375 in the following tested applications.

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

  • Biological activitySpecific Activity: 0.85 pmoles/min/µg. Enzyme reaction is conducted in a buffer containing 50 mM HEPES (pH7.5), 10 mM MgCl2, 1 mM EGTA, 200 µM ATP, 0.01% Brij-35, and 2 µM substrate (SER/THR 14) at room temperature for 1 hour.
  • Applications

    Functional Studies


  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.

    Preservative: None
    Constituents: 20% Glycerol, 0.05% Tween 20, 3mM DTT, 25mM Tris HCl, 100mM Sodium chloride, pH 7.5

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • cGK 1
    • cGK1
    • cGKI
    • cGKI alpha
    • cGKI beta
    • cGMP-dependent protein kinase 1
    • cGMP-dependent protein kinase I
    • DKFZp686K042
    • FLJ36117
    • KGP1_HUMAN
    • KGPB
    • MGC71944
    • pkg
    • PRKG1
    • PRKG1B
    • PRKGR1A
    • PRKGR1B
    see all
  • FunctionSerine/threonine protein kinasethat acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smoth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca(2+) release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca(2+) levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle.
  • Tissue specificityPrimarily expressed in lung and placenta.
  • Sequence similaritiesBelongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cGMP subfamily.
    Contains 1 AGC-kinase C-terminal domain.
    Contains 2 cyclic nucleotide-binding domains.
    Contains 1 protein kinase domain.
  • DomainComposed of an N-terminal leucine-zipper domain followed by an autoinhibitory domain, which mediate homodimer formation and inhibit kinase activity, respectively. Next, two cGMP-binding domains are followed by the catalytic domain at the C-terminus. Binding of cGMP to cGMP-binding domains results in a conformational change that activates kinase activity by removing the autoinhibitory domain from the catalytic cleft leaving the catalytic domain free to phosphorylate downstream substrates. Isoforms alpha and beta have identical cGMP-binding and catalytic domains but differ in their leucine zipper and autoinhibitory sequences and therefore differ in their dimerization substrates and kinase enzyme activity.
    Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase.
  • Post-translational
    Autophosphorylation increases kinase activity.
    65 kDa monomer is produced by proteolytic cleavage.
  • Cellular localizationCytoplasm. Colocalized with TRPC7 in the plasma membrane.
  • Information by UniProt

Recombinant human cGKI protein images

  • Image showing specific activity of ab80375.
  • 0% SDS-PAGE showing ab80375 at approximately 78kDa (3µg).

References for Recombinant human cGKI protein (ab80375)

ab80375 has not yet been referenced specifically in any publications.

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