Akt3 Antibody [C10D18] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000 IP1:100

Application
WB, IP

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
56 kDa 60 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
Akt3 Antibody [C10D18] detects endogenous levels of total Akt3 protein.

Clone
C10D18

Synonym(s)
AKT serine/threonine kinase 3; AKT3; DKFZp434N0250; MPPH; MPPH2; PKB gamma; PKB-GAMMA; PKBG; PRKBG; RAC-PK-gamma; serine threonine protein kinase, Akt-3; STK-2

Background
Akt3 (RAC‑γ serine/threonine kinase) is a member of the Akt/PKB family of AGC kinases that functions as a key effector of PI3K signaling and shows preferential expression and activity in brain, kidney, and heart, where it contributes to regulation of growth, metabolism, survival, and inflammatory responses in a tissue‑selective manner. The kinase shares the conserved domain architecture of Akt isoforms with an N‑terminal pleckstrin homology domain that binds phosphoinositides, a central kinase domain that contains the activation loop threonine site corresponding to Thr305 in Akt3, and a C‑terminal hydrophobic motif that includes Ser472, with phosphorylation at both regulatory sites acting in concert to generate full catalytic activity in response to PI3K‑generated PIP3 and PDK1/mTORC2 input. Akt3 is recruited to membranes after stimulation of receptor tyrosine kinases, cytokine receptors, GPCRs, or antigen receptors that activate class I PI3K, and membrane localization permits PDK1 phosphorylation of the activation loop and mTORC2 phosphorylation of the hydrophobic motif, while phosphatases such as PTEN, PP2A, and PHLPP restrain this activation cycle and set the signaling threshold for downstream responses. Akt3 shares many substrates with Akt1 and Akt2, including regulators of apoptosis, cell‑cycle progression, metabolism, and mTORC1, and phosphorylates proteins that control TSC1/TSC2 complex activity, mTORC1 output, GSK3‑dependent control of cyclin D1 and glycogen synthesis, and FoxO transcription factors, thereby linking growth factor and nutrient availability to biosynthesis, proliferation, and survival. Akt3 also displays isoform‑biased functions: high expression and signaling activity in neural tissues supports brain growth and neuronal survival, and disruption or reduction of Akt3 activity is associated with decreased brain size and neurodevelopmental phenotypes, while elevated Akt3 signaling contributes to tumor cell survival and proliferation in estrogen receptor‑negative breast cancer, PTEN‑deficient prostate cancer, and other malignancies where it frequently represents the predominant active Akt isoform. In immune and inflammatory contexts Akt3 modulates responses such as inflammatory demyelinating disease and adipose tissue expansion, where Akt3 activity influences balance between proliferation, differentiation, and inflammatory signaling, supporting disease‑specific roles that are partly distinct from Akt1 and Akt2 and that make Akt3 a candidate isoform‑selective target in oncology, neurology, and metabolic disease.

Background

Akt3 (RAC‑γ serine/threonine kinase) is a member of the Akt/PKB family of AGC kinases that functions as a key effector of PI3K signaling and shows preferential expression and activity in brain, kidney, and heart, where it contributes to regulation of growth, metabolism, survival, and inflammatory responses in a tissue‑selective manner. The kinase shares the conserved domain architecture of Akt isoforms with an N‑terminal pleckstrin homology domain that binds phosphoinositides, a central kinase domain that contains the activation loop threonine site corresponding to Thr305 in Akt3, and a C‑terminal hydrophobic motif that includes Ser472, with phosphorylation at both regulatory sites acting in concert to generate full catalytic activity in response to PI3K‑generated PIP3 and PDK1/mTORC2 input. Akt3 is recruited to membranes after stimulation of receptor tyrosine kinases, cytokine receptors, GPCRs, or antigen receptors that activate class I PI3K, and membrane localization permits PDK1 phosphorylation of the activation loop and mTORC2 phosphorylation of the hydrophobic motif, while phosphatases such as PTEN, PP2A, and PHLPP restrain this activation cycle and set the signaling threshold for downstream responses. Akt3 shares many substrates with Akt1 and Akt2, including regulators of apoptosis, cell‑cycle progression, metabolism, and mTORC1, and phosphorylates proteins that control TSC1/TSC2 complex activity, mTORC1 output, GSK3‑dependent control of cyclin D1 and glycogen synthesis, and FoxO transcription factors, thereby linking growth factor and nutrient availability to biosynthesis, proliferation, and survival. Akt3 also displays isoform‑biased functions: high expression and signaling activity in neural tissues supports brain growth and neuronal survival, and disruption or reduction of Akt3 activity is associated with decreased brain size and neurodevelopmental phenotypes, while elevated Akt3 signaling contributes to tumor cell survival and proliferation in estrogen receptor‑negative breast cancer, PTEN‑deficient prostate cancer, and other malignancies where it frequently represents the predominant active Akt isoform. In immune and inflammatory contexts Akt3 modulates responses such as inflammatory demyelinating disease and adipose tissue expansion, where Akt3 activity influences balance between proliferation, differentiation, and inflammatory signaling, supporting disease‑specific roles that are partly distinct from Akt1 and Akt2 and that make Akt3 a candidate isoform‑selective target in oncology, neurology, and metabolic disease.

References
https://pubmed.ncbi.nlm.nih.gov/25927491/ https://pubmed.ncbi.nlm.nih.gov/28483982/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%