Recombinant Mouse Cgmp-Dependent Protein Kinase 1 (PRKG1) Protein (His&Myc)

Name: Recombinant Mouse Cgmp-Dependent Protein Kinase 1 (PRKG1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07043P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Cgmp-Dependent Protein Kinase 1 (PRKG1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P0C605
Target Symbol	PRKG1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	SELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPDEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGQVNVTREDSPSEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDSFPEDSDEPPPDDNSGWDIDF
Expression Range	2-671aa
Protein Length	Full Length of Mature Protein
Mol. Weight	83.7 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Serine/threonine protein kinase that 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. Smooth 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 IRAG1 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.
Subcellular Location	Cytoplasm.
Protein Families	Protein kinase superfamily, AGC Ser/Thr protein kinase family, cGMP subfamily
Database References	KEGG: mmu:19091 UniGene: PMID: 30152261 This study demonstrates that H- ras deletion protects against AngII-induced cardiac remodeling, possibly via a mechanism in which PKG-Ibeta overexpression could play a partial role, and points to H-Ras and/or downstream proteins as potential therapeutic targets in cardiovascular disease. PMID: 29054855 that PKG-I expressed in nociceptors is not only a key determinant of dorsal root ganglion hyperexcitability and spinal synaptic plasticity but also an important modulator of cortical neuronal activity in pathological pain states PMID: 28326941 analysis of the role of binding interface with protein kinase G-Ialpha leucine zipper in vascular function PMID: 28280239 Brown adipose tissue, via Nox4-derived hydrogen peroxide, induces cyclic GMP-dependent protein kinase G type-1alpha activation, resulting in reduced vascular contractility. PMID: 28062507 disulfide formation at Cys(43) does not directly activate PKGIalpha, and the C43S-mutant PKGIalpha has a higher Ka for cGMP. Results highlight that mutant enzymes should be carefully biochemically characterized before making in vivo inferences. PMID: 28360102 PKG Ialpha disulfide formation triggers cardiac injury, and this initiation of maladaptive signaling can be blocked by pharmacological therapies that elevate cGMP, which binds kinase to limit its oxidation. PMID: 27342776 Cyclic GMP kinase deletion causes iron deficiency anemia, duodenal ulcers, and bleeding in the knockout mice. PMID: 26830212 Protein kinase G has a role in regulating production of H2S, which governs oxygen sensing PMID: 25900831 these results demonstrate that myocardial PKG1alpha oxidation prevents a beneficial response to pathological stress, may explain variable responses to PKG1alpha pathway stimulation in heart disease PMID: 25938783 Data show that cGMP-dependent kinase (cGK-Ialpha) knockdown partially rescued TNF-alpha-induced decrease in 42-kDa cGMP-dependent protein kinase-anchoring protein (GKAP42) and impairment of insulin signals. PMID: 25586176 miR-20a expression is up-regulated in response to hypoxia in both mouse and human pulmonary arterial smooth muscle cells PMID: 25447536 These findings characterize PKG as a novel regulator of AR-mediated transcription by enhancing AR cofactor p44/WDR77's function. PMID: 23755100 A functional leucine zipper domain in PKG-1alpha is essential for maintenance of a low pulmonary vascular tone in normoxia. PMID: 25128522 For the initial phase of angiotenin II-induced cardiac hypertrophy, lack of cardiomyocyte cGKI activity does not worsen hypertrophic growth. PMID: 25139994 the key role of PKG-I in transforming growth factor beta1 induction by like weak inducer of apoptosis in kidney cells PMID: 24872318 Results indicate that cGMP, acting primarily through cGKIalpha, is an important suppressor of kidney fibrosis. PMID: 23760283 cGKI and Trpc1,3,6 channels are not functionally coupled in vascular smooth cell. PMID: 23832809 Increasing PKG activity ameliorates renal fibrosis in part through regulation of macrophage and tubular cell function, leading to reduced TGF-beta-induced fibrosis. PMID: 24573388 cGMP, through activation of PKGI, inhibits c-Abl, leading to increased key antioxidant enzymes and resistance to lung endothelial oxidant injury. PMID: 24401847 In dystrophic hearts, excess contractility and arrhythmia are coupled to TRPC6 and are ameliorated by its targeted suppression or PKG activation. PMID: 24449818 PKG-1alpha dimerization is a major contributing factor to the vasodilator actions of DHEA. PMID: 24375799 mutation of the PKGIalpha LZ domain produces a clinically relevant model for hypertensive heart disease of aging. PMID: 23657971 ANP attenuates the inflammatory actions of histamine via endothelial GC-A/cGMP/cGKI signaling and inhibitory phosphorylation of TRPC6 channels. PMID: 23814119 PKG positively regulates proteasome activities and proteasome-mediated degradation of misfolded proteins, likely through posttranslational modifications to proteasome subunits. PMID: 23770744 Data indicate that oxidative activation of PKG Ialpha is a key mediator of hypotension and consequential organ injury during sepsis. PMID: 23716652 RhoA is a PKGIalpha target and direct binding of activated PKGIalpha to RhoA is central to cGMP-mediated inhibition of the VSMC Rho kinase contractile pathway PMID: 23066013 Data indicate that the 2 mechanisms (cGMP binding and the disulfide homodimer) of activating PKG1alpha are intricately linked with the binding of cGMP preventing oxidation to the disulfide state. PMID: 23006734 PKG-I deficiency induces pulmonary hypertension through Rho A/Rho kinase activation-mediated vasoconstriction and pulmonary vascular remodeling. PMID: 22632818 PKG-I-mediated presynaptic facilitation and synaptic long-term potentiation in spinal projection neurons is functionally involved in activity-dependent centrally mediated nociceptive hypersensitivity. PMID: 22427743 these findings suggest that cGK-Ialpha interacts with and phosphorylates rhotekin, thereby contributing to neurite outgrowth regulation. PMID: 22503686 Data show that protection of the duodenum from acid injury requires neuronal cGMP kinase I. PMID: 22253479 Sodium depletion enhances renal expression of (pro)renin receptor via cyclic GMP-protein kinase G signaling pathway. PMID: 22203739 role in noise-induced hearing loss and endogenous signaling pathway and activation of poly (ADP-ribose) polymerase PMID: 22270721 different signaling pathways exist for each cGKI isoform in vivo in fundus muscles PMID: 21914444 There are sex differences in the effects of PKG-I activation on the regulation of adipose tissue function and diet-induced obesity. PMID: 20930715 Genetic deletion of cGKI in non-neuronal cells results in a complex metabolic phenotype, including liver inflammation and fasting hyperglycemia. PMID: 21464444 protein kinase G type-I is essential for promoting proliferation and cell survival of mouse bone marrow stromal cells PMID: 21328456 Basal/moderately elevated PKG activity protects against high/pathological-level nitric oxide-induced apoptosis and promotes DNA synthesis/proliferation in vascular smooth muscle cells. PMID: 20060325 cGKI modulates glucagon release by suppression of calcium in alpha cells in mice. PMID: 20978093 Ang II suppression by ANP was abolished in cardiomyocytes of mice deficient in GC-A, in cyclic GMP-dependent protein kinase I (PKG I) or in the regulator of G protein signalling (RGS) 2, a target of PKG I PMID: 20352235 cGMP/cGKI signaling differentially inhibits contraction: in jejunum, inhibition is performed without changing [Ca(2+)](i) and is dependent on phosphatase activity, whereas in colon, inhibition is mediated by inhibition of [Ca(2+)](i) signals. PMID: 19628652 Cyclis GMP, through PKGI, attenuated H(2)O(2)-induced cytotoxicity in lung microvascular endothelial cells by increasing catalase and Gpx-1 expression through an unknown posttranscriptional effect. PMID: 20453163 evidence for PKGIalpha-dependent phosphorylation and activation of neuronal AAAD in vitro, and introduce AAAD as a putative PKGIalpha substrate. PMID: 20456015 These data establish that glucose-mediated downregulation of PKG levels stimulates TSP1 expression and enhances TGF-beta activity and matrix protein expression, which can contribute to vascular remodeling in diabetes. PMID: 20164378 Activation and inhibition of protein kinase G (PKG) respectively upregulates and downregulates recombinant potassium channel subfamily K (TASK1) channels heterologously expressed in PKG-loaded human embryonic kidney cells in vitro. PMID: 20410120 cardiac myocyte cGKI does not affect the development of heart hypertrophy induced by pressure overload or chronic isoproterenol infusion PMID: 20212138 (D)-Amino acid analogues of DT-2 as highly selective and superior inhibitors of cGMP-dependent protein kinase Ialpha. PMID: 20018259 PKGI links NO and cGMP signaling with the RhoA-ROCK and the insulin pathways, thereby controlling induction of adipogenic and thermogenic programs during brown fat cell differentiation PMID: 19952371 Cytosolic cGKI can support fear memory consolidation and LTP in neurons of the lateral amygdala via activation of CREB and CRE-dependent transcription. PMID: 20171263

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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