Recombinant human cGKI protein (ab96403)
Key features and details
- Expression system: Baculovirus infected insect cells
- Purity: > 95% Densitometry
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE
Description
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Product name
Recombinant human cGKI protein
See all cGKI proteins and peptides -
Biological activity
The specific activity of ab96403 was determined to be 780 nmol/min/mg. The specific activity was determined to be 780 nmol/min/mg.
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Purity
> 95 % Densitometry.
Affinity purified. -
Expression system
Baculovirus infected insect cells -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Predicted molecular weight
100 kDa including tags -
Amino acids
2 to 686
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Specifications
Our Abpromise guarantee covers the use of ab96403 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
SDS-PAGE
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Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
pH: 7.50
Constituents: 0.307% Glutathione, 0.00174% PMSF, 0.00385% DTT, 0.79% Tris HCl, 0.00292% EDTA, 25% Glycerol (glycerin, glycerine), 0.87% 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
- cGK 1
- cGK1
- cGKI
see all -
Function
Serine/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 specificity
Primarily expressed in lung and placenta. -
Sequence similarities
Belongs 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. -
Domain
Composed 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
modificationsAutophosphorylation increases kinase activity.
65 kDa monomer is produced by proteolytic cleavage. -
Cellular localization
Cytoplasm. Colocalized with TRPC7 in the plasma membrane. - Information by UniProt
Images
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)
ab96403 has not yet been referenced specifically in any publications.