AKT1 Antibody (YA5108)
(Synonyms: AKT1; PKB; RAC; RAC-alpha serine/threonine-protein kinase; Protein kinase B; PKB; Protein kinase B alpha; PKB alpha; Proto-oncogene c-Akt; RAC-PK-alpha)AKT1 Antibody (YA5108) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to AKT1.
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Host:
Mouse
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Application:
WB
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Reactivity :
Human, Mouse, Rat, Bovine, Chicken, Pig
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Formulation:
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
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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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|---|---|
| Dilution Ratio | 1:1000-1:2000 |
Product Details
AKT1 Antibody (YA5108) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to AKT1.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat, Bovine, Chicken, Pig
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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.
Purified recombinant human Akt1 (C-terminus) protein fragments expressed in E.coli.
affinity purified.
Non-conjugated
Unmodified
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
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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
AKT1 (protein kinase Bα, PKBα) is a serine/threonine kinase that functions as a central effector of the PI3K/AKT/mTOR signaling pathway, regulating cellular growth, survival, metabolism, proliferation, and differentiation across multiple tissues and cell types[1][2][3]. Activation of AKT1 occurs downstream of PI3K through phosphoinositide-dependent kinase-1 (PDK1) -mediated phosphorylation, enabling downstream regulation of targets involved in protein synthesis, apoptosis control, and metabolic adaptation[4][5]. Mechanistically, AKT1 contributes to angiogenesis, physiological tissue growth, immune-cell function, and stress-response signaling, making it a critical node in both normal physiology and disease-associated signaling networks[2][4][5]. In disease models, dysregulated AKT signaling is strongly associated with cancer, metabolic disorders, cardiovascular pathology, and inflammatory conditions, and constitutive activation of AKT-dependent pathways promotes oncogenic progression and therapeutic resistance[2][6][7]. Compared with related isoforms, AKT1 exhibits distinct biological functions despite substantial structural homology with AKT2 and AKT3; genetic studies demonstrate that AKT1 deficiency primarily causes growth retardation, whereas AKT2 deficiency induces insulin resistance and diabetes, and AKT3 loss predominantly affects brain development[4][5]. Isoform-specific investigations further show that AKT1 and AKT2 can exert non-redundant or even opposing effects on migration, invasion, inflammation, and fibrogenesis depending on cellular context[2][6][8]. For experimental applications, increasing efforts focus on developing AKT1-selective inhibitors and isoform-selective cellular models, which provide valuable tools for dissecting AKT isoform-specific signaling and for evaluating targeted therapeutic strategies with improved selectivity profiles[6][7][9].
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Subcellular Localization
Cytoplasm; Nucleus; Cell membrane; Mitochondrion intermembrane space
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Expression
Tissue_specificity:This protein is expressed in prostate cancer, and its expression level gradually increases from normal to malignant (protein level) . It is expressed in all human cell types analyzed to date. The phosphorylated form of Tyr-176 is significantly increased in the progressive stages of breast cancer (i.e., from normal to hyperplastic (ADH) , ductal carcinoma in situ (DCIS) , invasive ductal carcinoma (IDC) , and lymph node metastasis (LNMM) stages) . -
Isoforms & Post-Translational Modification
AKT1 has 2 isomers: P31749-1: 55686 Da (predicted); P31749-2: 48347 Da (predicted).
O-GlcNAcylation at Thr-305 and Thr-312 inhibits activating phosphorylation at Thr-308 via disrupting the interaction between AKT1 and PDPK1. O-GlcNAcylation at Ser-473 also probably interferes with phosphorylation at this site;Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity. Phosphorylation of the activation loop at Thr-308 by PDPK1/PDK1 is a prerequisite for full activation. 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 Thr-450, Ser-473, Ser-477 or Thr-479, thereby facilitating subsequent phosphorylation of the activation loop by PDPK1/PDK1. -
Subunit
Interacts (via the C-terminus) with CCDC88A (via its C-terminus). Interacts with AGAP2 (isoform 2/PIKE-A); the interaction occurs in the presence of guanine nucleotides. Interacts with AKTIP. Interacts (via PH domain) with MTCP1, TCL1A and TCL1B. Interacts with CDKN1B; the interaction phosphorylates CDKN1B promoting 14-3-3 binding and cell-cycle progression. Interacts with MAP3K5 and TRAF6. Interacts with BAD, PPP2R5B, STK3 and STK4. Interacts (via PH domain) with SIRT1. Interacts with SRPK2 in a phosphorylation-dependent manner. Interacts with RAF1. Interacts with TRIM13; the interaction ubiquitinates AKT1 leading to its proteasomal degradation. Interacts with TNK2 and CLK2. Interacts (via the C-terminus) with THEM4 (via its C-terminus). Interacts with and phosphorylated by PDPK1.
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SwissProt ID
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Synonyms
AKT1; PKB; RAC; RAC-alpha serine/threonine-protein kinase; Protein kinase B; PKB; Protein kinase B alpha; PKB alpha; Proto-oncogene c-Akt; RAC-PK-alpha
Documentation
References
[1]. Guerau-de-Arellano M, et al. Akt isoforms in the immune system. Front Immunol. 2022 Aug 23;13:990874. [Content Brief]
[2]. Reyes-Gordillo K, et al. Akt1 and Akt2 Isoforms Play Distinct Roles in Regulating the Development of Inflammation and Fibrosis Associated with Alcoholic Liver Disease. Cells. 2019 Oct 29;8(11):1337. [Content Brief]
[3]. O'Neill BT, et al. Akt1 in the cardiovascular system: friend or foe? J Clin Invest. 2005 Aug;115(8):2059-64. [Content Brief]
[4]. Tellai AD, et al. The complex post-transcriptional regulation of genes coding for methionine adenosyl transferase: New insights for liver cancer. Biochimie. 2025 Nov;238(Pt A):19-28. [Content Brief]
[5]. Quambusch L, et al. Cellular model system to dissect the isoform-selectivity of Akt inhibitors. Nat Commun. 2021 Sep 6;12(1):5297. [Content Brief]
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