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AKT2

v-akt murine thymoma viral oncogene homolog 2

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 PI3P-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 (PI3K) 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'.

Gene Name: v-akt murine thymoma viral oncogene homolog 2
Family/Subfamily: Protein Kinase , RAC/AKT
Synonyms: AKT2, PKB beta, PKBBETA, PRKBB, Protein kinase Akt-2, Protein kinase B beta, RAC-PK-beta, Rac protein kinase beta, RAC-BETA, HIHGHH, PKBB
Target Sequences: NM_001626 NP_001617.1 P31751

Publications (2)

1
Inhibition of protein kinase Akt1 by apoptosis signal-regulating kinase-1 (ASK1) is involved in apoptotic inhibition of regulatory volume increase. Subramanyam M, Takahashi N, Hasegawa Y, Mohri T, Okada Y. The Journal of biological chemistry. 2010 285:6109-17. [PubMed:20048146] [PMC:PMC2825405] Related Antibodies: LS-C19061.
2
AKT isoforms have distinct hippocampal expression and roles in synaptic plasticity. Levenga J, Wong H, Milstead RA, Keller BN, LaPlante LE, Hoeffer CA. eLife. 2017 November;6:pii: e30640. (Human) [Full Text Article] [PubMed:29173281] [PMC:PMC5722612] Related Antibodies: LS-C156232.

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AKT2 Protein
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E. coli
His-SUMO
71.6 kD
1 mg/$1,355; 100 µg/$420; 20 µg/$323
AKT2 Protein - Recombinant Protein Kinase B Beta By SDS-PAGE
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E. coli
His-T7
35.1 kDa
10 µg/$275; 50 µg/$402; 100 µg/$642; 200 µg/$802; 1 mg/$1,876; 500 µg/$1,430; 5 mg/$2,838; 2 mg/$2,060
AKT2 Protein - Western validation with an anti-DDK antibody * L: Control HEK293 lysate R: Over-expression lysate
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293T Cells
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55.6 kDa
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AKT2 Protein - 12.5% SDS-PAGE Stained with Coomassie Blue.
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Wheat Germ Extract
GST, N-terminus
10 µg/$479; 25 µg/$670
AKT2 Protein - Purified recombinant protein AKT2 was analyzed by SDS-PAGE gel and Coomassie Blue Staining
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HEK 293 Cells
Myc-DDK (Flag)
55.6 kDa
20 µg/$1,107
AKT2 Protein - Western validation with an anti-DDK antibody * L: Control HEK293 lysate R: Over-expression lysate
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HEK 293 Cells
Myc-DDK (Flag)
55.6 kDa
100 µg/$710
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Baculovirus
His-GST
Less than 1.0 EU/µg protein (determined by LAL method).
83.6 kDa
50 µg/$707
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The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).