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  4. Recombinant Mouse 5'-AMP-activated protein kinase catalytic subunit alpha-2 (Prkaa2)

Recombinant Mouse 5'-AMP-activated protein kinase catalytic subunit alpha-2 (Prkaa2)

  • 中文名稱：
    小鼠Prkaa2重組蛋白
  • 貨號(hào)：
    CSB-YP805325MO
  • 規(guī)格：
  • 來源：
    Yeast
  • 其他：
  • 中文名稱：
    小鼠Prkaa2重組蛋白
  • 貨號(hào)：
    CSB-EP805325MO
  • 規(guī)格：
  • 來源：
    E.coli
  • 其他：
  • 中文名稱：
    小鼠Prkaa2重組蛋白
  • 貨號(hào)：
    CSB-EP805325MO-B
  • 規(guī)格：
  • 來源：
    E.coli
  • 共軛：
    Avi-tag Biotinylated

    E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.

  • 其他：
  • 中文名稱：
    小鼠Prkaa2重組蛋白
  • 貨號(hào)：
    CSB-BP805325MO
  • 規(guī)格：
  • 來源：
    Baculovirus
  • 其他：
  • 中文名稱：
    小鼠Prkaa2重組蛋白
  • 貨號(hào)：
    CSB-MP805325MO
  • 規(guī)格：
  • 來源：
    Mammalian cell
  • 其他：

產(chǎn)品詳情

  • 純度：
    >85% (SDS-PAGE)
  • 基因名：
  • Uniprot No.：
  • 別名：
    Prkaa25'-AMP-activated protein kinase catalytic subunit alpha-2; AMPK subunit alpha-2; EC 2.7.11.1; Acetyl-CoA carboxylase kinase; ACACA kinase; EC 2.7.11.27; Hydroxymethylglutaryl-CoA reductase kinase; HMGCR kinase; EC 2.7.11.31
  • 種屬：
    Mus musculus (Mouse)
  • 蛋白長度：
    full length protein
  • 表達(dá)區(qū)域：
    1-552
  • 氨基酸序列
    MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ KIRSLDVVGK IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE LFDYICKHGR VEEVEARRLF QQILSAVDYC HRHMVVHRDL KPENVLLDAQ MNAKIADFGL SNMMSDGEFL RTSCGSPNYA APEVISGRLY AGPEVDIWSC GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPDYLNRS VATLLMHMLQ VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIDD EAVKEVCEKF ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPSGS FMDDSAMHIP PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA KWHLGIRSQS KACDIMAEVY RAMKQLGFEW KVVNAYHLRV RRKNPVTGNY VKMSLQLYLV DSRSYLLDFK SIDDEVVEQR SGSSTPQRSC SAAGLHRARS SFDSSTAENH SLSGSLTGSL TGSTLSSASP RLGSHTMDFF EMCASLITAL AR
  • 蛋白標(biāo)簽：
    Tag?type?will?be?determined?during?the?manufacturing?process.
    The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
  • 產(chǎn)品提供形式：
    Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 復(fù)溶：
    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • 儲(chǔ)存條件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保質(zhì)期：
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 貨期：
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事項(xiàng)：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet ：
    Please contact us to get it.

產(chǎn)品評(píng)價(jià)

靶點(diǎn)詳情

  • 功能：
    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. Involved in insulin receptor/INSR internalization. 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. 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 phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation. Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1.
  • 基因功能參考文獻(xiàn)：
    1. AMPK mediates the progress of atrophy during unloading and regrowth of atrophied muscles following reloading, but it does not influence the transition of myosin heavy chain isoforms. PMID: 30262782
    2. Those findings provide new insight into the mechanisms responsible for AMPKalpha2-dependent regulation of GLUT4 transcription after exercise. PMID: 28688716
    3. data suggest that AMPK is an intermediate effector in endocannabinoid-mediated exercise-induced antinociception. PMID: 28479394
    4. The rs2746342 polymorphism is significantly associated with susceptibility to type 2 diabetes mellitus (T2DM) and seems to interact with the rs2143754 polymorphism in the modulation of fasting plasma glucose (FPG) in the Han Chinese population. PMID: 27427333
    5. AMPKalpha2 activation prevents cardiac hypertrophy predominantly by inhibiting O-GlcNAcylation. PMID: 29371602
    6. Ampk is required for exercise-induced mitophagy in muscle. PMID: 28916822
    7. This novel mechanism explains how CDK4 promotes anabolism by blocking catabolic processes (FAO) that are activated by AMPK. PMID: 29053957
    8. High AMPKalpha2 phosphorylation is associated with abdominal aortic aneurysm. PMID: 28179583
    9. TNF-alpha treatment of colonic rho(0) cells augmented IL-8 expression by 9-fold (P < 0.01) via NF-kappaB compared to TNF-alpha-treated control. Moreover, reduced mitochondrial function facilitated TNF-alpha-mediated NF-kappaB luciferase promoter activity as a result of lowered inhibitory IkappaBalpha (nuclear factor of kappa light polypeptide gene enhancer in B-cell inhibitor, alpha), leading to elevated NF-kappaB. ... PMID: 28183804
    10. Rac1 and AMPK together account for almost the entire ex vivo contraction response in muscle glucose transport, whereas only Rac1, but not alpha2 AMPK, regulates muscle glucose uptake during submaximal exercise in vivo. PMID: 28389470
    11. we used the Cre-loxP system to knock down AMPKalpha2 expression in renal epithelial cells. Combining this approach with the systemic deletion of AMPKalpha1 we achieved reduced renal AMPK activity, accompanied by a shift to a moderate water- and salt-wasting phenotype. Thus we confirm the physiologically relevant role of AMPK in the kidney. PMID: 28179232
    12. AMPK phosphorylation of cortactin followed by SIRT1 deacetylation modulates the interaction of cortactin and cortical-actin in response to shear stress. Functionally, this AMPK/SIRT1 coregulated cortactin-F-actin dynamics is required for endothelial nitric oxide synthase subcellular translocation/activation and is atheroprotective. PMID: 27758765
    13. Findings show that decreased AMPK activity in muscle leads to decreased voluntary activity which is not due to secondary abnormalities in dopamine levels in the ventral striatum or sensitivity to cocaine. Thus, decreased voluntary activity in AMPK muscle deficient mice is most likely unrelated to regulation of brain dopamine content and metabolism. PMID: 27306083
    14. Hypoxia reduces HNF4alpha/MODY1 protein expression in pancreatic beta-cells by activating AMP-activated protein kinase. PMID: 28364040
    15. These studies reveal a novel mechanism in which CYP2J2 and epoxyeicosatrienoic acids enhanced Akt1 nuclear translocation through interaction with AMPKalpha2beta2gamma1 and protect against cardiac hypertrophy. PMID: 27416746
    16. Loss of AMPKalpha2 is associated with impaired control of vesicular stomatitis virus infection. PMID: 27879319
    17. AMPK-mediated HSPB1 expression enhanced insulin sensitivity in the skeletal muscle. PMID: 27928820
    18. Collectively, our data support the notion that the activation of AMPKalpha2 contributes to the atrophic effects of denervation. PMID: 27136709
    19. The activation of AMPKalpha2 in neutrophils is a decisive event in the initiation of vascular repair after ischemia. PMID: 27777247
    20. AMPKalpha2 deletion induces vascular smooth muscle cell phenotype switching and promotes features of atherosclerotic plaque. PMID: 27439892
    21. Suggest that E2 treatment ameliorates estrogen deficiency-induced changes in cardiac contractile function possibly through an AMPK-dependent mechanism. PMID: 25448287
    22. AMPKalpha2 deletion and high-fat feeding adverse effects are not additive on heart function and myocardial ischemic tolerance. PMID: 26596312
    23. AMPKalpha2 isoform plays a fundamental role in anti-oxidant stress and anti-senescence PMID: 26718972
    24. AMPKalpha2 is involved in post-transcriptional and not transcriptional regulation of PDK4 in muscle. PMID: 26359931
    25. PKD1 phosphorylates AMPKalpha2 at Ser485/491, thus diminishing AMPK activity. PMID: 26797128
    26. In conclusion, our findings reveal a new functional role of activating AMPK in the CNS to attenuate inflammatory responses and acute lung injury in sepsis. PMID: 26252187
    27. AMPKalpha signalling suppresses EMT and secretion of chemokines in renal tubular epithelia through interaction with CK2beta to attenuate renal injury. PMID: 26108355
    28. the current data suggests that activation of AMPK signaling is sufficient but not required for exercise-induced accumulation in mitochondrial FAT/CD36. PMID: 25965390
    29. The increase in nuclear PPARalpha protein by four-week exercise training under the intermittent hypoxia was dependent on AMPKalpha2 activation. PMID: 25923694
    30. Low AMPK-alpha2 signaling disrupts, in part, the exercise training-induced adaptations. PMID: 25103967
    31. provide evidence that high CO2 activates skeletal muscle atrophy via AMPKalpha2-FoxO3a-MuRF1, which is of biological and potentially clinical significance in patients with lung diseases and hypercapnia PMID: 25691571
    32. AMPKalpha2 is an essential mediator of nicotine-induced whole-body IR in spite of reductions in adiposity PMID: 25799226
    33. AMPKalpha2 ablation in muscle did not exacerbate high fat diet induce obesity in mice. On the contrary, it improved animal glucose tolerance and insulin sensitivity, with reduced triglyceride content in skeletal muscle. PMID: 25637528
    34. AMPKalpha2 translocates into the nucleus via phosphorylation, AMPKalpha2 interacts with and phosphorylates hnRNP H in the nucleus, and such a protein-protein interaction modulates metformin-mediated glucose uptake. PMID: 24686086
    35. activation of AMPKalpha2 seems crucial for maintaining skeletal muscle function, integrity and the ability to compensate chronic metabolic stress induced by SM mitochondrial uncoupling PMID: 24732703
    36. Dietary wolfberry elevated the xanthophyll concentrations and enhanced expression of BCO2 and heat shock protein 60, activated AMPKalpha2, potentiated mitophagy and mitochondrial biogenesis and enhanced lipid oxidation and secretion in the liver of mice. PMID: 24449471
    37. Data (including data from Prkaa2 knockout mice) suggest leptin is involved in regulation of cardiomyocyte contraction (or dysfunction) via Prkaa2 phosphorylation/activation and autophagy. PMID: 23688013
    38. AMPK alpha2 might represent an important therapeutic target for colon cancer metastasis-induced liver injury PMID: 24515110
    39. AMPKalpha2 significantly contributed to stabilization and activation of E2F1 by doxorubicin, forming a positive signal amplification loop. PMID: 24398673
    40. Deletion of AMPKalpha2 causes aberrant VSMC migration with accelerated neointima formation via Skp2 up-regulation and E-cadherin down-regulation. PMID: 24115035
    41. The impact of ageing and high fat diet on insulin action is not worsened in mice lacking functional alpha2AMPK in skeletal muscle. PMID: 23671593
    42. AMPK is the first identified physiological substrate for CHIP chaperone activity, establishing a link between cardiac proteolytic and metabolic pathways. PMID: 23863712
    43. A functionally active AMPKalpha2 subunit is required for insulin-stimulated muscle glycogen synthesis. PMID: 23224579
    44. Suggest that AMPKalpha(2) is involved in the regulation of substrate uptake in a time-dependent manner in contracting muscle but is not necessary for regulation of fatty acid uptake and oxidation during caffeine treatment. PMID: 21551008
    45. AMPKalpha2 controls cardiac p70S6K under normoxia and regulates eEF-2 but not the mTOR-p70S6K pathway during ischemia. PMID: 23466593
    46. Data from knockout mice suggest that LKB1 (liver kinase B1) acts independent of AMPKa2 in regulation of oxidation of free fatty acids in skeletal muscle during physical activity/exercise. Knockdown of LKB1 leads to decrease in muscle AMPKa2. PMID: 23349504
    47. AMPKalpha suppression or knockdown produces the opposite effects. The results demonstrate an anti-infamatory pathway linking AMPK, PARP-1, and Bcl-6 in endothelial cells PMID: 23382195
    48. Our data identify the microtubule cytoskeleton as a sensitive target of AMPK activity, and the data suggest a novel role for AMPK in limiting accumulation and densification of microtubules that occurs in response to hypertrophic stress. PMID: 23316058
    49. Endoplasmic reticulum stress increases vascular smooth muscle contractility resulting in high blood pressure, and AMP-activated protein kinase activation mitigates high blood pressure through the suppression of ER stress in vivo. PMID: 23288166
    50. p70S6 kinase forms a complex with the alpha-2 catalytic subunit of AMPK, resulting in phosphorylation on serine(491). PMID: 22727014

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  • 亞細(xì)胞定位：
    Cytoplasm. Nucleus. Note=In response to stress, recruited by p53/TP53 to specific promoters.
  • 蛋白家族：
    Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
  • 數(shù)據(jù)庫鏈接：