Recombinant Human Rac-Beta Serine/Threonine-Protein Kinase (AKT2) Protein (His-SUMO)

Name: Recombinant Human Rac-Beta Serine/Threonine-Protein Kinase (AKT2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10175P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Rac-Beta Serine/Threonine-Protein Kinase (AKT2) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P31751
Target Symbol	AKT2
Synonyms	Akt2; AKT2_HUMAN; HIHGHH; Murine thymoma viral (v-akt) homolog 2; murine thymoma viral (v-akt) homolog-2; Oncogene AKT2 protein kinase B beta; PKB; PKB beta; PKBB; PKBBETA; PRKBB; Protein kinase Akt 2; Protein kinase Akt-2; Protein kinase B beta; RAC beta; rac protein kinase beta; RAC-BETA; RAC-beta serine/threonine-protein kinase; RAC-PK-beta; RACbeta; v akt murine thymoma viral oncogene homolog 2; V-AKT murine thymoma viral oncogene homolog 2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	NEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIRE
Expression Range	2-481aa
Protein Length	Partial
Mol. Weight	71.6kDa
Research Area	Apoptosis
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	AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, 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 recently 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. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. Phosphorylates CLK2 on 'Thr-343'.
Subcellular Location	Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Early endosome.
Protein Families	Protein kinase superfamily, AGC Ser/Thr protein kinase family, RAC subfamily
Database References	HGNC: 392 OMIM: 125853 KEGG: hsa:208 STRING: 9606.ENSP00000375892 UniGene: PMID: 29667444 AKT2 and XIST expression was identified as a potential biomarker participating in the effect of ATP5J in colorectal cancer PMID: 29484395 Authors present the first evidence that miR-608 behaves as a tumour suppressor in A549 and SK-LU-1 cells through the regulation of AKT2. PMID: 29075783 the present study suggested that PHB2 may promote Prostate cancer cell migration by inhibiting the expression of AKT2. These results provide information regarding the role of PHB2 in Prostate cancer migration and malignancy PMID: 29207197 Data found that S131 of Akt2 is not phosphorylated by CK2 although the consensus sequence recognized by CK2 (S/T-x-x-E/D/pS/pT) is conserved. A single sequence element, a T at position n+1, hampers phosphorylation, causing an alpha-helix structure preventing the recognition of its own consensus by CK2. Using synthetic peptides, study suggests that Akt2 S131 could be phosphorylated by kinases of the Plk family. PMID: 29494643 Findings demonstrate that DSBs trigger pro-survival autophagy in an ATM- and p53-dependent manner, which is curtailed by AKT2 signaling. PMID: 28837154 genetic association studies in population of men in Finland: Data suggest that a partial loss-of-function variant in AKT2 (p.Pro50Thr) is associated with type 2 diabetes in the population studied; this AKT2 variant is associated with reduced insulin-mediated glucose uptake in multiple insulin-sensitive tissues. PMID: 29141982 miR2965p/AKT2 axis serves important roles in Hepatocellular carcinoma carcinogenesis and progression. PMID: 28586057 miR296 is downregulated in tissue from patients with pancreatic cancer and pancreatic carcinoma cell lines. These findings suggested that it may function as a tumor suppressor via inhibiting the growth, migration and invasion of pancreatic cancer cells. AKT2 was validated as a direct target of miR296 in pancreatic cancer cells. PMID: 28534950 miR-143-3p acts as a novel tumor suppressive miRNA by regulating gastric tumor growth, migration and invasion through directly targeting AKT2 gene PMID: 28404925 Our findings suggest that Akt2 might be associated with the resistance to anti-EGFR therapies, especially the use of erlotinib against PC, and that this resistance can be overcome by combined treatment with a PI3K inhibitor. Akt2 expression could become a predictive biomarker for erlotinib resistance in PC. PMID: 28440469 Studied action of linoleic acid (LA) on cell migration and neoplasm invasiveness of breast cancer cells. Findings show Akt2 activation requires EGFR and PI3K activity, whereas migration and invasion are dependent on FFAR4, EGFR and PI3K/Akt activity. PMID: 28456993 Analysis of genomic data from TCGA demonstrated coamplification of CCNE1 and AKT2 Overexpression of Cyclin E1 and AKT isoforms, in addition to mutant TP53, imparted malignant characteristics in untransformed fallopian tube secretory cells, the dominant site of origin of high-grade serous ovarian cancer PMID: 27663592 Recent studies reveal that AKT2-NOX2 signaling has critical roles in Ca mobilization, ROS generation, degranulation, and control of the ligand-binding function of cell surface molecules, thereby promoting heterotypic cell-cell interactions in thromboinflammation. PMID: 28650848 The expression levels of AKT2 and CDC25C showed lower expression in neural tube defects. And the percentage of methylated region of AKT2 promoter were increased in neural tube defects. PMID: 27871477 Report frequency of genetic variation in Akt2 and discuss link to type 2 diabetes. PMID: 28931550 IRF5 and IRF5 disease-risk variants increase glycolysis and human m1 macrophage polarization by regulating proximal signaling and Akt2 activation. PMID: 27545875 the direct interaction of AKT2 and EF2 was found to be dynamically regulated in embryonic rat cardiomyocytes PMID: 23823123 Data identify MTSS1 as a new Akt2-regulated gene, and point to suppression of MTSS1 as a key step in the metastasis-promoting effects of Akt2 in CRC cells. PMID: 28068324 Akt2, Erk2, and IKK1/2 phosphorylate Bcl3, converting Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. PMID: 28689659 Results indicate that AKT2 modulates pulmonary fibrosis through inducing TGF-beta1 and IL-13 production by macrophages, and inhibition of AKT2 may be a potential strategy for treating Idiopathic pulmonary fibrosis. PMID: 28455433 The p.Glu17Lys mutation of AKT2 confers low-level constitutive activity upon the kinase and produces hypoglycemia with suppressed fatty acid release from adipose tissue, but not fatty liver, hypertriglyceridemia, or elevated hepatic de novo lipogenesis. PMID: 28541532 Studies provide evidence that AKT2 counteracts oxidative-stress-induced apoptosis and is required for alpha-beta thymocyte survival and differentiation. Also, it plays a critical role in antagonizing cardiomyocyte apoptosis. [review] PMID: 26953242 Akt2 role in the human lung cancer cell proliferation, growth, motility, invasion and endothelial cell tube formation PMID: 26234648 This study demonstrates novel regulatory circuits involving miR-148a-3p/ERBB3/AKT2/c-myc and DNMT1 that controls bladder cancer progression, which may be useful in the development of more effective therapies against bladder cancer. PMID: 27906180 Both in our animal model and in human Age-related macular degeneration (AMD), the AKT2-NF-kappaB-LCN-2 signalling axis is involved in activating the inflammatory response. PMID: 28026019 identified a novel association between the coding variant (p.Pro50Thr) in AKT2 and fasting plasma insulin (FI), a gene in which rare fully penetrant mutations are causal for monogenic glycemic disorders. Carriers of the FI-increasing allele had increased 2-h insulin values, decreased insulin sensitivity, and increased risk of type 2 diabetes. PMID: 28341696 AKT2 can regulate miR-200a in a histology- or stage-specific manner and this regulation is independent of subsequent involvement of miR-200a in epithelial-mesenchymal transition. PMID: 27189341 Quinoline-type inhibitors bind in the Akt2 PH domain. PMID: 28036396 TGF-beta signaling through Akt2 induces phosphorylation of heterogeneous nuclear ribonucleoprotein E1 (hnRNP E1) at serine-43 (p-hnRNP E1), driving epithelial to mesenchymal transition and metastasis. PMID: 27067543 miR-29b plays an important role in TGF-beta1-mediated epithelial-mesenchymal transition in ARPE-19 cells by targeting Akt2. PMID: 25263462 miR-148a functions as tumor suppressor in Renal cell carcinoma by targeting AKT2. PMID: 27878305 MiR-650 could inhibit the proliferation, migration and invasion of rheumatoid arthritis synovial fibroblasts through targeted regulation of AKT2 expression. PMID: 28129626 High AKT2 expression is associated with gallbladder cancer. PMID: 26803515 miR-302b inhibits SMMC-7721 cell invasion and metastasis by targeting AKT2 PMID: 26254095 No association has been found between AKT2 polymorphisms and oesophageal squamous cell carcinoma risk. PMID: 26828791 High AKT2 expression is associated with ovarian cancer. PMID: 26512921 Active, phosphorylated Akt2 translocates to the nucleus in Notch-expressing cells, resulting in GSK-3beta inactivation in this compartment. PMID: 26711268 controls endothelial Jagged1 expression and, thereby, Notch signalling regulating VSMC maintenance. PMID: 26971877 These studies identify Akt2 as a critical kinase that regulates radixin phosphorylation and leads to Mrp-2 translocation and function. PMID: 26500117 miR-612 directly suppressed AKT2, which in turn inhibited the downstream epithelial-mesenchymal transition-related signaling pathway. PMID: 26158514 the correlation between RLN2 and p-AKT or RLN2 and p-ERK1/2 expression was investigated. PMID: 26229955 the biological effect of Akt2 in colorectal cancer cells PMID: 25134663 miR-137 which is frequently down-regulated in gastric cancer is potentially involved in gastric cancer tumorigenesis and metastasis by regulating AKT2 related signal pathways PMID: 26102366 miR-615-5p inhibits pancreatic cancer cell proliferation, migration, and invasion by targeting AKT2 PMID: 25856297 QSAR based docking studies identify marine algal callophycin A as inhibitor of protein kinase B beta. PMID: 25936945 we assayed expression of myosin II.. this assay is a powerful predictor of the use of ZEB2/Akt2 as a marker for tumor progression in serous ovarian cancers. PMID: 25894377 Up-regulation of AKT2 was associated with chemoresistance in renal cell carcinoma. PMID: 25951903 findings suggested that AKT2 may be one of the targets of miR29s in gastric cancer PMID: 25428377 PIK3CA and AKT2 mutations occurred at low frequency in gastric cancer. PMID: 25771729

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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.

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