AKT2 Antibody

Figure 1: Western blot analysis using AKT2 mouse mAb against A431 (1), Jurkat (2), HEK293 (3), A549 (4), MCF-7 (5) and PC-12 (6) cell lysate.
Figure 2: Immunohistochemical analysis of paraffin-embedded human Thymus tissues using anti-AKT2 mAb
Figure 3: Immunofluorescence analysis of PANC-1 (left) and Hela (right) cells using AKT2 mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye. Red: Actin filaments have been labeled with Alexa Fluor-555 phalloidin.

SPECIFICATION
CITATIONS
PROTOCOLS
BACKGROUND

Product Information
Application Applications Legend: WB=Western Blot IHC=Immunohistochemistry IHC-P=Immunohistochemistry (Paraffin-embedded Sections) IHC-F=Immunohistochemistry (Frozen Sections) IF=Immunofluorescence FC=Flow Cytopmetry IC=Immunochemistry ICC=Immunocytochemistry E=ELISA IP=Immunoprecipitation DB=Dot Blot CHIP=Chromatin Immunoprecipitation FA=Fluorescence Assay IEM=Immuno electron microscopy EIA=Enzyme Immunoassay	WB, IHC, ICC, E
Primary Accession	P31751
Reactivity	Human, Rat, Monkey
Host	Mouse
Clonality	Monoclonal
Clone Names	1B6
Isotype	IgG2b
Calculated MW	60kDa
Description	Akt2 (also designated protein kinase B beta or v-akt murine thymoma viral oncogene homolog 2 ), with 481-amino acid protein (about 53kDa), belongs to the AKT serine/threonine protein kinase family, which also includes Akt1 and Akt3. They are involved in a wide variety of biological processes including cell proliferation, differentiation, apoptosis, tumorigenesis, as well as glycogen synthesis and glucose uptake. Among the members of AKT family, Akt2 is associated with the development of human cancers. Akt2 inhibits cisplatin-induced JNK/p38 and Bax activation through phosphorylation of ASK1 and thus, plays an important role in chemoresistance. Further, Akt2 plays a specific role in muscle differentiation.
Immunogen	Purified recombinant fragment of human AKT2 expressed in E. Coli.
Formulation	Ascitic fluid containing 0.03% sodium azide.

Additional Information
Gene ID	208
Other Names	RAC-beta serine/threonine-protein kinase, 2.7.11.1, Protein kinase Akt-2, Protein kinase B beta, PKB beta, RAC-PK-beta, AKT2
Dilution	WB~~1/500 - 1/2000 IHC~~1/200 - 1/1000 IF~~1/200 - 1/1000
Storage	Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
Precautions	AKT2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.

Protein Information
Name	AKT2 (HGNC:392)
Function	Serine/threonine kinase closely related to AKT1 and AKT3. All 3 enzymes, AKT1, AKT2 and AKT3, are collectively known as AKT kinase. AKT regulates many processes including metabolism, proliferation, cell survival, growth and angiogenesis, through the phosphorylation of a range of downstream substrates. Over 100 substrates have been reported so far, although for most of them, the precise AKT kinase catalyzing the reaction was not specified. AKT regulates 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 also regulates 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 (PubMed:21432781, PubMed:21620960). In response to lysophosphatidic acid stimulation, inhibits the ciliogenesis cascade. In this context, phosphorylates WDR44, hence stabilizing its interaction with Rab11 and preventing the formation of the ciliogenic Rab11-FIP3-RAB3IP complex. Also phosphorylates RAB3IP/Rabin8, thus may affect RAB3IP guanine nucleotide exchange factor (GEF) activity toward Rab8, which is important for cilia growth (PubMed:31204173).
Cellular Location	Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Early endosome {ECO:0000250\|UniProtKB:Q60823}. Note=Through binding of the N-terminal PH domain to phosphatidylinositol (3,4,5)- trisphosphate (PtdIns(3,4,5)P3) or phosphatidylinositol (3,4)- bisphosphate (PtdIns(3,4)P2), recruited to the plasma membrane. Cell membrane recruitment is facilitated by interaction with CLIP3 Colocalizes with WDFY2 in early endosomes (By similarity). Localizes within both nucleus and cytoplasm in proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts (PubMed:17565718). {ECO:0000250\|UniProtKB:Q60823, ECO:0000269\|PubMed:17565718}
Tissue Location	Widely expressed. Expressed in myoblasts (PubMed:17565718).

Research Areas

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Application Protocols

Provided below are standard protocols that you may find useful for product applications.

Western Blot Protocol

Blocking Peptides Protocol

Dot Blot Protocol

Immunohistochemistry Protocol

Immunofluorescence Protocol

Immunoprecipitation Protocol

Flow Cytomety Protocol

Cell Culture Protocol

References

1. Am J Physiol Endocrinol Metab. 2004 Jul;287(1):E8-E15. 2. Oncol Rep. 2004 Jan;11(1):25-32. 3. Cancer Res. 2003 Jan 1;63(1):196-206.

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