Phospho-AKT1S1 (T246) Antibody
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Product Specs
Buffer
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Form
Liquid
Lead Time
Typically, we can ship products within 1-3 business days after receiving your order. Delivery times may vary depending on the purchase method or location. Please consult your local distributor for specific delivery times.
Synonyms
40 kDa proline rich AKT substrate antibody; 40 kDa proline-rich AKT substrate antibody; AKT1 S1 antibody; AKT1 substrate 1 (proline rich) antibody; AKT1 substrate 1 antibody; AKT1S 1 antibody; AKT1S1 antibody; AKTS1_HUMAN antibody; Lobe antibody; MGC2865 antibody; PRAS 40 antibody; PRAS antibody; PRAS40 antibody; Proline rich akt substrate antibody; Proline rich Akt substrate 40 kDa antibody; Proline-rich AKT1 substrate 1 antibody
Target Names
Uniprot No.
Target Background
Function
Phospho-AKT1S1 (T246) Antibody targets AKT1S1, a subunit of mTORC1, which plays a crucial role in regulating cell growth and survival in response to nutrient and hormonal cues. mTORC1 is activated in response to growth factors or amino acids. Activation through growth factors involves AKT1-mediated phosphorylation of TSC1-TSC2, ultimately leading to activation of the RHEB GTPase. This activation potently stimulates the protein kinase activity of mTORC1. Amino acid signaling to mTORC1 requires its relocation to the lysosomes, a process facilitated by the Ragulator complex and the Rag GTPases. Activated mTORC1 upregulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. It phosphorylates EIF4EBP1, releasing it from inhibition of the elongation initiation factor 4E (eiF4E). Furthermore, mTORC1 phosphorylates and activates S6K1 at 'Thr-389', promoting protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, AKT1S1 negatively regulates mTOR activity in a manner dependent on its phosphorylation state and binding to 14-3-3 proteins. It inhibits RHEB-GTP-dependent mTORC1 activation. AKT1S1 is a substrate for AKT1 phosphorylation but can also be activated by AKT1-independent mechanisms. It may also play a role in nerve growth factor-mediated neuroprotection.
Gene References Into Functions
- The Akt-PRAS40 pathway is activated by uric acid, inhibiting autophagy and mirroring the uric acid-induced proinflammatory cytokine phenotype. PMID: 28484006
- Crystal structures of RAPTOR-TOS motif complexes elucidate the determinants of TOS recognition. Additionally, an mTOR FKBP12-rapamycin-binding (FRB) domain-substrate complex establishes a second substrate-recruitment mechanism. A truncated mTOR-PRAS40 complex reveals that PRAS40 inhibits both substrate-recruitment sites. PMID: 29236692
- Studies indicate that activated PRAS40 serves as a regulator of TGFA-triggered exosome secretion and as a common regulator of distinct microenvironmental and oncogenic signal-triggered exosome secretion in both normal and tumor cell types. PRAS40 is the first identified regulator for stress-induced exosome secretion. PMID: 28674187
- PRAS40 was downregulated in DU145 cells following MYO6 knockdown. PMID: 27431378
- Phosphorylation of S202/203 of AKT1S1 by PKM2 releases AKT1S1 from raptor and facilitates its binding to 14-3-3. This results in hormonal- and nutrient-signals independent activation of mTORC1 signaling, leading to accelerated oncogenic growth and autophagy inhibition in cancer cells. PMID: 26876154
- The frameshift mutation detected in this study would prematurely terminate amino-acid synthesis in AKT1S1 protein, resembling a typical loss-of-function mutation. PMID: 25648575
- Supporting this concept, AKT1S1 mRNA, a downstream target of the TGFb-miR-96 signaling pathway, was identified. Its translated protein negatively regulates mTOR kinase. PMID: 25531317
- This review examines the role of PRAS40 and possible feedback mechanisms, along with alterations in AKT/PRAS40/mTOR signaling implicated in the pathogenesis of tumor progression. [review] PMID: 26003731
- Findings suggest that dual phosphorylation of PRAS40 by Akt and mTORC1 promotes the formation of a nuclear-specific PRAS40- and RPL11-containing complex distinct from mTORC1. This complex inhibits the RPL11-HDM2-p53 pathway. PMID: 24704832
- PRAS40 as a regulator of insulin sensitivity in hSkMC. PMID: 24576065
- PRAS40 possesses a functional nuclear export signal. Enforced nuclear accumulation of PRAS40 impairs insulin action, underscoring its function in regulating insulin sensitivity. PMID: 23712034
- Data indicate that PRAS40 modulates insulin action in skeletal muscle. Knockdown of PRAS40 inhibits insulin action in cultured myotubes and is associated with upregulation of IRS1 (insulin receptor substrate 1) degradation via proteasome proteolysis. PMID: 23460019
- WISP1 regulates PRAS40 by sequestering it intracellularly through post-translational phosphorylation. PMID: 22873724
- A study identified tuberin and PRAS40 as potent anti-apoptotic gatekeepers in early stem-cell differentiation. This research provides new insights into the regulation of early stem-cell maintenance and differentiation and identifies a new role for the tumor suppressor tuberin and the oncogenic protein PRAS40. PMID: 22090422
- This review summarizes the regulation and potential function(s) of PRAS40 within the complex Akt- and mTOR-signaling network in both health and disease. [REVIEW] PMID: 22354785
- Findings suggest that PRAS40 promotes the development of ESFT. PMID: 22241085
- PRAS40 is known for its ability to regulate the mammalian target of rapamycin complex 1 kinase activity, playing a key regulatory role at the intersection of signal transduction pathways activated by growth factor receptors. PMID: 21906675
- Phosphorylation of PRAS40 is crucial for the activation of mTOR in CNI-induced VEGF overexpression and renal cancer progression. PMID: 21886838
- Dissociation of PRAS40 from insulin-stimulated 4E-BP protein binding to mTORC1 and enhanced mTORC1 substrate binding result from Akt and mTORC1 activation. This makes little or no contribution to mTORC1 signaling. PMID: 21914810
- PIM1-activated pPRAS40, AKT-activated pFOXO3a, and their complex formation with 14-3-3 could be key regulators of radiation-induced radioresistance in NSCLC cells. PMID: 21910584
- PRAS40 is a significant regulator of insulin sensitivity of the Akt-mTOR pathway and a potential target for the treatment of cancers, insulin resistance, and hamartoma syndromes. PMID: 17277771
- PRAS40 inhibits cell growth, S6K1 phosphorylation, and rheb-induced activation of the mTORC1 pathway. PMID: 17386266
- PRAS40 regulates mTORC1 kinase activity by functioning as a direct inhibitor of substrate binding. PMID: 17510057
- PRAS40 acts downstream of mTORC1 but upstream of its effectors, such as S6K1 and 4E-BP1. PMID: 17604271
- Activation of mTORC1 signaling by phorbol esters does not require PRAS40 to be phosphorylated at Thr(246), bind to 14-3-3, or be released from mTORC1. PMID: 18215133
- After mTORC1 kinase activation by upstream regulators, PRAS40 is phosphorylated directly by mTOR, contributing to the relief of PRAS40-mediated substrate competition. PMID: 18372248
Database Links
Subcellular Location
Cytoplasm, cytosol.
Tissue Specificity
Widely expressed with highest levels of expression in liver and heart. Expressed at higher levels in cancer cell lines (e.g. A-549 and HeLa) than in normal cell lines (e.g. HEK293).
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