Recombinant Mouse 5-Amp-Activated Protein Kinase Catalytic Subunit Alpha-1 (PRKAA1) Protein (His)

Name: Recombinant Mouse 5-Amp-Activated Protein Kinase Catalytic Subunit Alpha-1 (PRKAA1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07878P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Mouse 5-Amp-Activated Protein Kinase Catalytic Subunit Alpha-1 (PRKAA1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q5EG47
Target Symbol	PRKAA1
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRAAIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFE
Expression Range	1-312aa
Protein Length	Partial
Mol. Weight	39.8 kDa
Research Area	Metabolism
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	Catalytic 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. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. In that process also activates WDR45. In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.
Subcellular Location	Cytoplasm. Nucleus. Note=In response to stress, recruited by p53/TP53 to specific promoters.
Protein Families	Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
Database References	KEGG: mmu:105787 STRING: 10090.ENSMUSP00000063166 UniGene: PMID: 28739141 these findings identify a previously uncharacterized role of folate/DHFR/AMPKalpha axis in regulating oligodendrocyte survival and myelination. PMID: 28496133 CNR1 modulates AMPKalpha to influence insulin resistance and endoplasmic reticulum stress induced by palmitate. PMID: 29909009 Inhibiting the LTB4/BLT1 signaling pathway via AMPK activation is a potential treatment strategy for septic cardiac dysfunction because it efficiently attenuates cardiac apoptosis, which may occur via the inhibition of inflammation and mitochondrial dysfunction. PMID: 28290498 Thus, these findings suggest that AMPKalpha1 and AMPKalpha2 activity in chondrocytes is important in maintaining joint homeostasis and osteoarthritis development. PMID: 28225087 At molecular analysis, there was a time-dependent nuclear translocation of the active phosphorylated catalytic subunits AMPKalpha1/alpha2 and PGC-1alpha in young, but not in mature, mice after sepsis. PMID: 28974562 Low AMPK expression is associated with Acute respiratory distress syndrome. PMID: 30171880 AMPK stabilizes FOXO3 and suggest a role in the first initiation step of mitochondrial segregation in muscle cells. PMID: 29580989 these results demonstrate that AMPK downregulation is not a triggering factor in fatty liver development but in contrast, establish the therapeutic impact of pharmacological AMPK re-activation in the treatment of fatty liver disease. PMID: 29343420 Prkaa1 deletion activates skeletal muscle mTOR signalling, which has a central role in lipid metabolism and mitochondrial oxidation. Collectively, our study provides new insights into the role of Prkaa1 in skeletal muscle PMID: 29288408 our findings suggest that the role of Cx43 in response to H2O2 stress is dependent on the activation of AMPK signaling pathways and regulates ROS production and cell necrosis. PMID: 29279848 activation of AMPK at early stage of adipogenesis is involved in the anti-adipogenesis effect of Red Pepper Seed extract. PMID: 29316805 Study indicate that the alpha 2 and alpha 1 subunits of AMPK have several functional differences, with alpha 2 conferring stronger osteogenic potential and a weaker ability to induce osteoblasts-associated osteoclastogenesis in MC3T3-E1 cells as well as conferring a lower adipogenic potential to 3T3-L1 cells. PMID: 27600021 Over-expression of AMP-activated protein kinase (AMPK) promoted the apoptosis of mesangial cells from the systemic lupus erythematosus (SLE) mice. PMID: 29268850 AMPK-PGC-1a control of mitochondrial reactive oxygen species regulates Warburg metabolism. PMID: 28978464 AMPKalpha1 has a critical role in maintaining the anticontractile actions of perivascular adipose tissue; an effect independent of the endothelium but likely mediated through altered adiponectin secretion or sensitivity. PMID: 27668984 Ampk-/- mice displayed retardation of postnatal bone development, although bone deformity was not observed at birth. PMID: 29126229 Cardiac SUR2A levels were significantly increased while Kir6.2 levels were not affected. Hypoxia did not induce phosphorylation of extracellular signal-regulated kinases (ERK1/2) or protein kinase B (Akt), but triggered phosphorylation of AMP activated protein kinase (AMPK). AICAR, an activator of AMPK, increased the level of SUR2A in H9c2 cells. We conclude that oxygen increases SUR2A level by activating AMPK. PMID: 28121062 This study provides new insights into the control of eEF2K by AMPK. PMID: 28502587 These data indicate that a reduction in AMPK disrupts cellular metabolism in both progenitors and differentiated placental trophoblasts. PMID: 28335680 Targeted activation of AMPK by GSK621 ameliorates H2O2-induced osteoblast cell injuries. PMID: 28060740 Sestrin 1 targets at the AMPK/mTORC1/autophagy pathway to inhibit cardiac hypertrophy by interaction with AMPK which is responsible for autophagy regulation. Taken together, our data indicate that Sestrin 1 regulates AMPK/mTORC1/autophagy axis to attenuate cardiac hypertrophy. PMID: 28181410 AMPK enhances intestinal barrier function and epithelial differentiation via promoting CDX2 expression, which is partially mediated by altered histone modifications in the Cdx2 promoter. PMID: 28234358 our results elucidate a previously unrecognized role of AMPKalpha1 deletion in loss of contact inhibition of cellular proliferation and angiogenesis PMID: 27449088 AMPK and Sirt2 control compensatory glucose uptake in metabolically arrested mitochondria. PMID: 27909079 results indicate that liver AMPKalpha1alpha2 is required for maintaining glucose homeostasis during an acute bout of exercise. PMID: 29038293 AMP-activated protein kinase (AMPK) regulates autophagy by phosphorylating BECN1 at Thr388 PMID: 27304906 activation of AMPK might be a stress response of host cells to restrict virus production through promotion of autophagic degradation PMID: 27305174 AMPK regulates T cell survival and function. Demonstrate AMPK-dependent and independent rolesof AICAR/Compound C in regulating T cell responses. PMID: 27177226 AMPK was sufficient to stimulate osteogenesis of MC3T3-E1 cells and inhibit adipogenesis of 3T3-L1 cells through the AMPK-Gfi1-OPN axis. PMID: 27283242 AMPK activation reduces the formation of atheromata-inducing macrophages in ApoE(-/-)-deficient mice by inhibiting expression of Ccr2, thereby preventing the Ccr2-mediated migration of Ly6C(hi) monocytes from the bone marrow. PMID: 28235712 AMPK activation inhibited IL-1beta-stimulated CXCL10 secretion, associated with reduced interleukin-1 receptor associated kinase-4 (IRAK4) phosphorylation. PMID: 27840174 Findings indicate that the energy-sensing LKB1-AMPK pathway regulates IGF1 secretion in mouse primary hepatocytes, which in turn regulates activation of the IGF1R-PKB pathway. PMID: 28500773 These data suggest that nutrient availability dictates the mode of division and that LKB1-AMPK mediates this nutrient-driven effect on intestinal epithelial stem cell proliferation. PMID: 28766983 Myeloid-Restricted AMPKalpha1 Promotes Host Immunity and Protects against IL-12/23p40-Dependent Lung Injury during Hookworm Infection PMID: 27183598 Data suggest that Il4 (usually released from helper T-cells) induces Cox1 in macrophages at post-transcriptional level; activation of Ampk (catalytic subunit Prkaa1) by metformin blocks Il4-dependent induction of Cox1 and blocks macrophage polarization/activation. (Il4 = interleukin-4; Cox1 = cyclooxygenase 1; Ampk = AMP-activated protein kinase) PMID: 28684424 The metformin-rescued P23H rhodopsin was still intrinsically unstable and led to increased structural instability of the rod outer segments. These data suggest that improving the traffic of misfolding rhodopsin mutants is unlikely to be a practical therapy, but also highlights the potential of altering translation through AMPK to improve protein function in other protein misfolding diseases PMID: 28065882 Mechanistically, miR-499 directly targets Fnip1, an AMP-activated protein kinase (AMPK)-interacting protein that negatively regulates AMPK, a known activator of PGC-1alpha. This miR-499/Fnip1/AMPK circuit can serve as a mechanism to couple muscle fiber type and mitochondrial function. PMID: 27506764 dopamine is coupled to AMPK activation, which provides a substantial anti-inflammatory and bioenergetic advantage and reduces the severity of endotoxin-induced acute lung injury. PMID: 27733575 AMPKalpha1 deficiency suppresses brown adipogenesis in favor of fibrogenesis during brown adipose tissue development. PMID: 28668388 AMPK-dependent metabolic repair mechanisms are important for mitigating lung injury. PMID: 28085510 these data demonstrated that LKB1/AMPK signaling pathway activation improved the survival of diabetic mice complicated with endotoxemia. Thus, LKB1/AMPK signaling pathway may serve as a potentially useful therapeutic target for severe infection in diabetic patients. PMID: 28628912 We confirmed that procyanidins suppressed acute hyperglycemia with an oral glucose tolerance test in a dose-dependent manner.procyanidins, especially cinnamtannin A2, significantly ameliorate postprandial hyperglycemia at least in part by promoting GLUT4 translocation to the plasma membrane by activating both insulin- and AMPK-signaling pathways. PMID: 27598258 These findings demonstrate that the AMPK-TBC1D1 signaling nexus interacts with the PKB-mTOR pathway via IGF1 secretion, which consequently controls expression of lipogenic genes in the adipose tissue PMID: 27307439 AMPKa1 deficiency impairs autophagy-mediated monocyte differentiation and decreases monocyte/macrophage survival PMID: 28330873 The authors identified lactate dehydrogenase (LDH) as a new functional target of AMPKalpha1. PMID: 28515121 AMPKalpha1 knockout (KO) mice exhibit normal renal sodium handling and a moderate antidiuretic state. This is accompanied by higher urinary aldosterone excretion rates and reduced blood pressure. Plasma volume, however, was found to be increased compared with wild-type mice. PMID: 28179232 AMPK in adipocytes is vital for maintaining mitochondrial integrity. PMID: 27411013 Study demonstrated that adenosine monophosphate-activated protein kinase alpha 1 (AMPKalpha1) is imperative for maintaining normal nociception, and mice deficient for AMPKalpha1 exhibit mechanical allodynia. PMID: 27058143 The data suggest that AMPK is not required for the regulation of the intermediate filament interaction with CPT-I during exercise. PMID: 27941154

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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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