Recombinant Human 5'-Amp-Activated Protein Kinase Subunit Gamma-2 (PRKAG2) Protein (His)

Name: Recombinant Human 5'-Amp-Activated Protein Kinase Subunit Gamma-2 (PRKAG2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08670P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human 5'-Amp-Activated Protein Kinase Subunit Gamma-2 (PRKAG2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9UGJ0
Target Symbol	PRKAG2
Synonyms	PRKAG25'-AMP-activated protein kinase subunit gamma-2; AMPK gamma2; AMPK subunit gamma-2; H91620p
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MLEKLEFEDEAVEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETWRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQNLDELGIGTYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALILTPAGAKQKETETE
Expression Range	1-328aa
Protein Length	Full Length of Isoform B
Mol. Weight	41.5kDa
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	AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.
Protein Families	5'-AMP-activated protein kinase gamma subunit family
Database References	HGNC: 9386 OMIM: 194200 KEGG: hsa:51422 STRING: 9606.ENSP00000287878 UniGene: PMID: 28546535 PRKAG2-mutated iPSC-CMs displayed functional and structural abnormalities, which were abolished by correcting the mutation in the patient's iPSCs using CRISPR technology. PMID: 28917552 gamma2 AMPK activation downregulates fundamental sinoatrial cell pacemaker mechanisms to lower heart rate, including sarcolemmal hyperpolarization-activated current (I f) and ryanodine receptor-derived diastolic local subsarcolemmal Ca(2+) release. In contrast, loss of gamma2 AMPK induces a reciprocal phenotype of increased heart rate, and prevents the adaptive intrinsic bradycardia of endurance training. PMID: 29097735 Case Report: PRKAG2 missense mutation causing glycogen storage disease and severe biventricular hypertrophy and high-grade atrio-ventricular block. PMID: 27496753 We highlight the potential for patients with PRKAG2 mutations. PMID: 28801758 This study of patients with PRKAG2 mutations provides a more comprehensive view of the natural history of this disease and demonstrates a high risk of cardiac complications. Early recognition of this disease appears important to allow an appropriate management. PMID: 28431061 A novel missense genetic variant of unknown significance (GVUS) was detected in the PRKAG2 gene (c.869A>T, p.K290I). This novel GVUS has not been identified in any global population databases. PMID: 28690312 As in patients with PRKAG2 cardiomyopathy, iPS cell and mouse models are protected from cardiac fibrosis, and we define a crosstalk between AMPK and post-transcriptional regulation of TGFbeta isoform signaling that has implications in fibrotic forms of cardiomyopathy. PMID: 28009297 Identify a novel, de novo PRKAG2 mutation (K475E) in the cystathionine beta-synthase 3 repeat, a region critical for AMP binding, which affects AMP-activated protein kinase activity, activates cell growth pathways, and results in cardiac hypertrophy, which can be reversed with rapamycin. PMID: 28550180 PRKAG2 polymorphism maybe important factor treating hypertensive patients with hydrochlorothiazide. PMID: 27381900 Data suggest different gamma-isoforms in AMPK can have different effects on enzyme activation; here, activation of AMPK by compound 991 is greater if AMPK contains PRKAG2 versus PRKAG1 or PRKAG3. PMID: 28302767 mice with chronic AMPK activation, resulting from mutation of the AMPK gamma2 subunit, exhibit ghrelin signaling-dependent hyperphagia, obesity, and impaired pancreatic islet insulin secretion. Humans bearing the homologous mutation manifest a congruent phenotype. PMID: 27133129 PRKAG2 cardiac syndrome may present with eccentric distribution of LVH, involving focal mid-infero-lateral pattern in the early disease stage, and more diffuse pattern but focusing on interventricular septum in advanced cases. PMID: 26496977 Overexpression of G100S mutation in PRKAG2 causes Wolff-Parkinson-White syndrome in transgenic zebrafish. PMID: 23992123 Its mutation causes AMPK signaling abnormality which leads to cardiac syndrome. PMID: 23778007 The PRKAG2 autosomal dominant cardiac syndrome may be commonly characterized by Left Ventricular Hypertrophy, an accessory pathway, and progression to conduction disease requiring implantation of a pacemaker. PMID: 23810891 Data indicate that except AMPK-alpha1, expressions of the other five AMPK subunits -alpha2, -beta1, -beta2, -gamma1 and -gamma2 are significantly higher in ovarian carcinomas. PMID: 22897928 Single nucleotide polymorphisms in PRKAG2 is associated with drug response in breast cancer. PMID: 23034890 The authors found that the gene encoding the gamma2 subunit of AMP-activated protein kinase (AMPK) strongly correlated with Zaire Ebolavirus transduction in the tumor cell panel. PMID: 23115293 found a significant association between the -26C/T polymorphism and cognitive impairment. Moreover, this polymorphism was also related to the presence of diabetes. PMID: 21813245 The mutation in the PRKAG2 gene was identified as responsible for the familial form of WPW syndrome in this Chinese family. PMID: 20381067 These two individuals may be considered to suffer from a combination of both a classical hypertrophic cardiomyopathy (due to the two mutations in MYBPC3) and a glycogen storage cardiomyopathy (due to the mutation in PRKAG2). PMID: 21409595 no mutations were detected within the coding region of PRKAG2 in Wolff-Parkinson-White syndrome patients PMID: 20561859 Newly identified polymorphisms (amino acid substitutions) are likely associated with cardiac disease in type 2 diabetic patients. PMID: 20022652 This protein, transfected into a transgenic mouse, activates and mediates cardiac hypertrphic signaling pathways. PMID: 20005292 PRKAG2 R302Q mutant induces AMPK activation and increases glycogen content in cardiomyocytes. PMID: 20031621 Identified a novel mutation (Arg531Gly) in the PRKAG2 of AMP-activated protein kinase (AMPK) to be responsible for a syndrome associated with ventricular preexcitation and early onset of atrial fibrillation and conduction disease. PMID: 11748095 The role of the causative gene, gamma-2 regulatory subunit (PRKAG2) of AMP-activated protein kinase, in the regulation of the glucose metabolic pathway in muscle suggests that genetic defects in PRKAG2 may induce a cardiac glycogenosis syndrome. PMID: 12015471 Three of the mutations studied occur within the cystathionine beta-synthase (CBS) domains of gamma(2). Two of these mutations lead to a marked decrease in AMP dependence, whereas the third reduces AMP sensitivity. PMID: 12397075 unlike familial WPW syndrome, constitutional mutation of PRKAG2 is not commonly associated with sporadic WPW syndrome PMID: 12716108 mutations affecting PRKAG2 are likely to confer a specific alteration of AMPK function of particular importance in the myocardium PMID: 14519435 Transgenic mice expressing human mutant(TG(R302Q)) PRKAG2 gene with the cardiac-specific promoter alpha-myosin heavy chain have ventricular pre-excitation, prolonged QRS, excess cardiac glycogen and a distinct AV accessory pathway. PMID: 15611370 The glycogen-storage cardiomyopathy produced by LAMP2 or PRKAG2 mutations resembles hypertrophic cardiomyopathy but is distinguished by electrophysiological abnormalities PMID: 15673802 The AMP kinase disease is uncommon in HCM and is characterized by progressive conduction disease and cardiac hypertrophy and includes extracardiac manifestations such as a skeletal myopathy. PMID: 15766830 Biochemical characterization of the recombinant R531Q mutant protein showed >100-fold reduction of binding affinities for the regulatory nucleotides AMP and ATP but an enhanced basal activity and increased phosphorylation of the alpha -subunit. PMID: 15877279 The PRKAG2 N488I mutation causes inappropriate AMPK activation, which leads to glycogen accumulation and heart conduction system disease when transfected into mice. PMID: 16275868 The study describe a 38-year-old man with a new heterozygous PRKAG2 mutation (Ser548Pro) manifesting by hypertrophic cardiomyopathy, severe conduction system abnormalities, and skeletal muscle glycogenosis. PMID: 16487706 AMP-activated protein kinase is regulated by a pseudosubstrate sequence on the gamma subunit. PMID: 17255938 Altered AMPK gamma 2 subunit activity under normal energetic status remodels the cardiac metabolic network to cause a unique form of glycogen storage disease in transgenic mice. PMID: 17431505 four members of the same family with a very similar ECG pattern characterized by conduction defects and mutations in PRKAG2 gene PMID: 17483151 Human mutations which disrupt the nucleotide-binding affinity of the gamma2 subunit lead to loss of inhibition by ATP and inappropriate activate AMP-Kinase under resting conditions. PMID: 17990392 Gene analysis identified a R302Q mutation of the gamma2 subunit producing AMP protein kinase, coded by the gene PRKAG2, and associated with a heart conduction defect. PMID: 18033003 data provide insight into mechanisms of cardiac PRKAG2 disease and suggest that glycogen-storage cardiomyopathy can be modulated by lowering glycogen content in the heart PMID: 18158359 REVIEW. Compelling evidence exists that Prkag2 mutations cause a "gain of function" in basal AMPK activity, leading to excessive cellular glucose uptake and pathological glycogen storage in the heart, resulting in a potentially fatal cardiac phenotype. PMID: 18195183 Mutational analysis of PRKAG2, LAMP2, and NKX2-5 genes in a cohort of 125 patients with accessory atrioventricular connection. PMID: 19533775 Preexcitation associated with the R302Q mutation in PRKAG2 is associated with Mahaim fibers. PMID: 19808419

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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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