AKT3, Monoclonal Antibody

AKT3; AKT3 kinase; AKT3_HUMAN; DKFZp434N0250; MPPH; PKB gamma; PKBG; PRKBG; Protein kinase AKT-3; Protein Kinase AKT3; Protein kinase B gamma; RAC gamma; RAC gamma serine/threonine protein kinase; RAC-gamma serine/threonine-protein kinase; RAC-PK-gamma; RACPK Gamma; Serine threonine protein kinase AKT 3; Serine threonine protein kinase AKT3; STK 2; STK-2; STK2; V AKT murine thymoma viral oncogene homolog 3 (protein kinase B, gamma); V AKT murine thymoma viral oncogene homolog 3; V AKT murine thymoma viral oncogene homolog 3 protein kinase B gamma

For Research Use Only. Not for use in diagnostic procedures.

Monoclonal

IgG1

Mouse

Akt3 antibody detects endogenous levels of total Akt3

Affinity-Chromatography

Phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

1mg/ml (lot specific)

Store at -20 degree C. Stable for 12 months from date of receipt.

Manufactured in an ISO 9001:2015 Certified Laboratory.

Manufactured in a lab with traceable raw materials manufactured on site. Coordinated product portfolio of antibodies, pairs, conjugates, recombinant proteins, and immunoassay materials available, please inquire.

Small volumes of anti-AKT3 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Description: Akt3 (also designated protein kinase B gamma or v-akt murine thymoma viral oncogene homolog 3), with 479-amino acid protein (about 53kDa), belongs to the AKT serine/threonine protein kinase family, which also includes Akt1 and Akt2. AKT kinases are known to be regulators of cell signaling in response to insulin and growth factors. They are involved in a wide variety of biological processes including cell proliferation, differentiation, apoptosis, tumorigenesis, as well as glycogen synthesis and glucose uptake.Akt3 is not required for the maintenance of normal carbohydrate metabolism but is essential for the attainment of normal organ size. Identifying Akt3 as a selective target in melanoma cells also provides new therapeutic opportunities for patients in the advanced stages of this disease.
Function: AKT3 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. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis.
Subunit Structure: Interacts (via PH domain) with TCL1A; this enhances AKT3 phosphorylation and activation. Interacts with TRAF6. Interacts with KCTD20 (By similarity). Interacts with BTBD10 (By similarity).
Post-translational Modifications: Phosphorylation on Thr-305 and Ser-472 is required for full activity. Ubiquitinated. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome. O-GlcNAcylation at Thr-302 and Thr-309 inhibits activating phosphorylation at Thr-305 via disrupting the interaction between AKT and PDK1.
Similarity: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI3K) results in its targeting to the plasma membrane. Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.

Western Blot (WB), ELISA (EIA)

ELISA: 1:10000
WB: 1:500-1:2000

Figure 1: Western blot analysis using Akt3 mouse mAb against truncated Akt3 recombinant protein (1) and human ovary carcinoma tissue lysate (2).

Observed: 55 kDa
Predicted: 56 kDa

AKT serine/threonine kinase 3

RAC-gamma serine/threonine-protein kinase

RAC-gamma serine/threonine-protein kinase

PKBG; PKB gamma  [Similar Products]

The protein encoded by this gene is a member of the AKT, also called PKB, serine/threonine protein kinase family. AKT kinases are known to be regulators of cell signaling in response to insulin and growth factors. They are involved in a wide variety of biological processes including cell proliferation, differentiation, apoptosis, tumorigenesis, as well as glycogen synthesis and glucose uptake. This kinase has been shown to be stimulated by platelet-derived growth factor (PDGF), insulin, and insulin-like growth factor 1 (IGF1). Alternatively splice transcript variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2008]

AKT3 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. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis.

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