AKT2 Antibody (YA3952)(PBS only)
(Synonyms: PKBB; PRKBB; PKBBETA; RAC-BETA)AKT2 Antibody (YA3952) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to AKT2.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF, ELISA
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Reactivity :
Human, Rat, Monkey
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Formulation:
Supplied in PBS, pH 7.4.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|---|
| Dilution Ratio | 1:500-1:2000 | 1:200-1:1000 | 1:200-1:1000 | 1:10000 |
Product Details
AKT2 Antibody (YA3952) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to AKT2.
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Host Mouse
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Species ReactivityHuman, Rat, Monkey
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Observed Molecular WeightObserved band size: 56 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 56 kDa
Purified recombinant fragment of human AKT2 aa 2-149.
affinity purified.
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
AKT2 (protein kinase Bβ) is a serine/threonine kinase that functions downstream of phosphoinositide 3-kinase (PI3K) and mediates insulin-dependent regulation of glucose transport, glycogen synthesis, and metabolic homeostasis[1][2]. Mechanistically, AKT2 is a central effector of insulin receptor signaling and controls glucose utilization through phosphorylation networks linked to cellular metabolism and nutrient storage[2][3]. In disease contexts, AKT2 was originally identified as an oncogenic kinase amplified in ovarian carcinoma and later shown to contribute to malignant phenotypes in multiple tumor models through enhanced survival and growth signaling[1]. Genetic studies further established its metabolic importance, as Akt2-deficient mice develop insulin resistance, glucose intolerance, dyslipidemia, adipose tissue loss, and progressive diabetic phenotypes, supporting its essential role in systemic glucose regulation[2][3]. Compared with related isoforms, AKT1 is more strongly associated with organismal growth and developmental regulation, whereas AKT2 displays a more specialized function in insulin-responsive tissues and metabolic control[4][5]. Isoform-specific analyses in skeletal muscle from patients with type 2 diabetes demonstrated impaired insulin-stimulated AKT2 activation and altered phosphorylation patterns, linking defective AKT2 signaling to human metabolic disease[6]. For experimental applications, ATP-competitive AKT inhibitors such as GSK690693 directly target the AKT kinase domain and are widely used to investigate AKT-dependent signaling mechanisms in cancer and metabolic research models[7].
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Subcellular Localization
Cytoplasm; Nucleus; Cell membrane; Peripheral membrane protein; Early endosome
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Expression
Tissue_specificity:Widely expressed. Expressed in myoblasts (PubMed: 17565718) -
Isoforms & Post-Translational Modification
P31751 has 2 isomers: P31751-1: 55769 Da (predicted); P31751-2: 51083 Da (predicted).
Phosphorylation on Thr-309 and Ser-474 is required for full activity (PubMed:12086620, PubMed:12434148, PubMed:15890450, PubMed:20059950). Phosphorylation of the activation loop at Thr-309 by PDPK1/PDK1 is a prerequisite for full activation (By similarity). Phosphorylated and activated by PDPK1/PDK1 in the presence of phosphatidylinositol 3,4,5-trisphosphate (PubMed:9512493). Phosphorylation by mTORC2 in response to growth factors plays a key role in AKT1 activation: mTORC2 phosphorylates different sites depending on the context, such as Ser-474 or Ser-478, thereby facilitating subsequent phosphorylation of the activation loop by PDPK1/PDK1 (By similarity);Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6 catalyzes 'Lys-63'-linked AKT2 ubiquitination; this modification may be important for AKT2 recruitment to the plasma membrane and for AKT2 activating phosphorylation (PubMed:19713527). When phosphorylated, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3 in the nucleus, leading to its degradation by the proteasome (PubMed:20059950);O-GlcNAcylation at Thr-306 and Thr-313 inhibits activating phosphorylation at Thr-309 via the disruption of the interaction between AKT and PDPK1/PDK1 -
Subunit
Interacts with BTBD10 (By similarity). Interacts with KCTD20 (By similarity). Interacts (via PH domain) with MTCP1, TCL1A and TCL1B; this interaction may facilitate AKT2 oligomerization and phosphorylation, hence increasing kinase activity (PubMed:10983986). Interacts with PHB2; this interaction may be important for myogenic differentiation (By similarity). Interacts (when phosphorylated) with CLIP3/ClipR-59; this interaction promotes AKT2 recruitment to the plasma membrane (By similarity). Interacts with WDFY2/ProF (via WD repeats 1-3) (PubMed:16792529)
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SwissProt ID
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Synonyms
PKBB; PRKBB; PKBBETA; RAC-BETA
Documentation
References
[1]. Cheng JQ, et al. AKT2, a putative oncogene encoding a member of a subfamily of protein-serine/threonine kinases, is amplified in human ovarian carcinomas. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9267-71. [Content Brief]
[2]. Cho H, et al. Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta). Science. 2001 Jun 1;292(5522):1728-31. [Content Brief]
[3]. Garofalo RS, et al. Severe diabetes, age-dependent loss of adipose tissue, and mild growth deficiency in mice lacking Akt2/PKB beta. J Clin Invest. 2003 Jul;112(2):197-208. [Content Brief]
[4]. Alibardi L. Stimulation of regenerative blastema formation in lizards as a model to analyze limb regeneration in amniotes. Histol Histopathol. 2019 Oct;34(10):1111-1120. doi: 10.14670/HH-18-123. Epub 2019 May 6. PMID: 31058307. et al. Stimulation of regenerative blastema formation in lizards as a model to analyze limb regeneration in amniotes. Histol Histopathol. 2019 Oct;34(10):1111-1120. [Content Brief]
[5]. Irie HY, et al. Distinct roles of Akt1 and Akt2 in regulating cell migration and epithelial-mesenchymal transition. J Cell Biol. 2005 Dec 19;171(6):1023-34. [Content Brief]
[6]. Cozzone D, et al. Isoform-specific defects of insulin stimulation of Akt/protein kinase B (PKB) in skeletal muscle cells from type 2 diabetic patients. Diabetologia. 2008 Mar;51(3):512-21. [Content Brief]
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