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    Recombinant Rat RAC-beta serine/threonine-protein kinase(Akt2)

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    • 共轭:
      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.

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    • 来源:
      Mammalian cell
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    • 纯度:
      >85% (SDS-PAGE)
    • 基因名:
    • Uniprot No.:
    • 别名:
      Akt2RAC-beta serine/threonine-protein kinase; EC; Protein kinase Akt-2; Protein kinase B beta; PKB beta; RAC-PK-beta
    • 种属:
      Rattus norvegicus (Rat)
    • 蛋白长度:
      Full length protein
    • 表达区域:
    • 氨基酸序列
    • 蛋白标签:
      The following tags are available.
      N-terminal His-tagged
      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.
    • 产品提供形式:
      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.
    • 复溶:
      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.
    • 储存条件:
      Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
    • 保质期:
      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.
    • 货期:
      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.
    • 注意事项:
      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.



    • 功能:
      AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinases, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.; One of the few specific substrates of AKT2 identified so far is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 seems also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Phosphorylates CLK2 on 'Thr-343'.
    • 基因功能参考文献:
      1. Suggest that when cardiomyocytes incur oxidative stress under diabetic conditions, it subsequently activates the PI3Kgamma/Akt cell-signaling pathway and further increases HMGB1 expression. PMID: 27821807
      2. The results of this study suggest that phosphorylation of Akt2 mediates the beneficial effects of galanin on insulin-induced glucose uptake in the adipocytes of diabetic rats. PMID: 28365702
      3. Data suggest that caloric restriction in aging rats up-regulates insulin-stimulated glucose uptake in the predominantly slow-twitch soleus muscle; this up-regulation appears to rely on enhanced Akt2 phosphorylation. PMID: 27786542
      4. Evidence links greater Akt2 activation to the caloric restriction-induced elevation of insulin-stimulated glucose uptake by muscle from old animals. PMID: 26739650
      5. Nuclear translocation of Akt2 and synthesis of GLUT2 is increased in the hepatocytes of chard or/and insulin-treated hyperglycemic rats. PMID: 23746671
      6. PP2A inhibitors increased hepatic Akt phosphorylation and inhibited FoxO1in vitro and in vivo, and suppressed gluconeogenesis in hepatocytes PMID: 24150286
      7. In adult recuperated rats, Akt phosphorylation (P<0.01) and protein levels of Akt-2 (P<0.01) were also reduced. Messenger RNA expression levels of these proteins were not different, indicating a post-transcriptional effect. PMID: 23229735
      8. Hydrogen sulfide effects on cardiac relaxation involve KATP channels, the Akt/NOS-cGMP/PKG pathway, and S-sulfhydration of cardiac proteins. PMID: 23785074
      9. Akt2 mediates insulin-dependent Rac1 activation in muscle cells. PMID: 23499910
      10. In corpus striatum slices, basal activity of Akt2 regulates DAT cell surface expression. PMID: 22778840
      11. BAFF/BAFF-R involved in autoantibody production in rats with collagen-induced arthritis via PI3K-Akt-mTOR signaling and the regulation of paeoniflorin. PMID: 22391142
      12. analysis of resistance of Akt kinase and PP2A to dephosphorylation through ATP-dependent conformational plasticity PMID: 22031698
      13. Findings link prenatal hypoxia to down-regulation of components of hepatic and muscle Akt expression in adult offspring. PMID: 20923964
      14. Reduced Akt2 leads to up-regulation of Rab4a expression in cardiomyocytes in a cell-autonomous fashion that may involve activation of PPARalpha. PMID: 20728450
      15. The results suggest the possibility that an age-related decline in pAkt2Thr308, acting by a mechanism other than reduced pAS160Thr642, may play a role in the insulin resistance in the soleus of old rats. PMID: 20339009
      16. The downstream mediator of PI3-K, Akt/protein kinase B, also exhibited differentiation-dependent activation, which regulates the development of the differentiated trophoblast giant cell phenotype. PMID: 12089343
      17. Phosphorylation of cardiac protein kinase B is regulated by palmitate. PMID: 12181135
      18. These results suggest that, with brief calorie restriction, enhanced Akt2 phosphorylation may play a role in increasing insulin sensitivity in rat skeletal muscles. PMID: 12799317
      19. Akt inhibits BID-mediated apoptosis downstream of BID cleavage via promotion of mitochondrial hexokinase association and antagonism of tBID-mediated BAX and BAK activation at the mitochondria. PMID: 14701745
      20. reductions in expression of IRS-1 and insulin-stimulated phosphorylation of IRS-1 and Akt2 are associated with insulin resistance in mtDNA-depleted L6 GLUT4myc myocytes PMID: 15764607
      21. in skeletal muscle, insulin stimulates translocation of aPKC zeta and lambda, but not Akt2, to the plasma membrane PMID: 15802290
      22. The data reveal a novel type of cross-talk between P2Y12 and IGF-I receptors that proceeds through Gbetagamma-, Ca2+-and PLD2-dependent activation of the Pyk2/Src pathway resulting in GTP-loading of Rap1 required for an increased PKB phosphorylation. PMID: 16236484
      23. p122RhoGAP Ser-322 acts as an integrator of signal transduction in a manner dependent on the cellular context and is a substrate for protein kinase B and ribosomal S6 kinase PMID: 16338927
      24. kinetic analysis of Akt1, Akt2 and Akt3 shows that ATP is an initiating factor for the catalysis of AKT enzymes and may play a role in the regulation AKT enzyme activity in cells PMID: 16540465
      25. Akt-1 and Akt-2 have distinct roles in muscle glucose metabolism; moderate reductions in IRS-1 expression do not result in the development of insulin resistance in skeletal muscle in vivo PMID: 17021050
      26. EGF but not insulin specifically upregulated Akt 2 and 3. PMID: 18535289
      27. Endogenous protein kinase B-beta/Akt2 phosphorylates and inhibits the cardiac Na+/H+ exchanger NHE1. PMID: 18757828
      28. the anti-apoptotic properties of insulin are mediated partly by increasing HO-1 expression at transcriptional level via IRS1/PI3K/Akt2 activation PMID: 18854316
      29. Akt2, but not other isoforms, specifically regulates B23 sumoylation and protein stability PMID: 18931307
      30. results suggest a crosstalk between Akt2 and TGFbeta signaling that involves a mechanism requiring EGFR down-regulation during the entire tumor promotion process starting from the early stage PMID: 19309364
      31. PKB/Akt directly phosphorylates NR2C on serine 1096 PMID: 19477150



    • 亚细胞定位:
      Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Early endosome.
    • 蛋白家族:
      Protein kinase superfamily, AGC Ser/Thr protein kinase family, RAC subfamily
    • 数据库链接:

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