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anti-Human AKT Anticorps:
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Human Polyclonal AKT Primary Antibody pour IHC, WB - ABIN6713950
Wu, Zhang, Tao, Dong: Lipoxin A(4) inhibits transition of epithelial to mesenchymal cells in proximal tubules. dans American journal of nephrology 2010
Show all 40 Pubmed References
Human Polyclonal AKT Primary Antibody pour IHC, IP - ABIN6712278
Fu, Lv, Guan, Ma, Ji, He, Shi, Hou: Metallothionein 1G functions as a tumor suppressor in thyroid cancer through modulating the PI3K/Akt signaling pathway. dans BMC cancer 2014
Show all 31 Pubmed References
Human Polyclonal AKT Primary Antibody pour IHC, WB - ABIN6713951
Li, He, Feng, Zhang, Tang, Bian, Bai, Zhou, Jiang, Heximer, Qin, Huang, Liu, Huang: Regulator of G protein signaling 5 protects against cardiac hypertrophy and fibrosis during biomechanical stress of pressure overload. dans Proceedings of the National Academy of Sciences of the United States of America 2010
Show all 28 Pubmed References
Human Polyclonal AKT Primary Antibody pour IHC, WB - ABIN361978
Kim, Lee, Kim, Bahk: A Proteomic approach for protein-profiling the oncogenic ras induced transformation (H-, K-, and N-Ras) in NIH/3T3 mouse embryonic fibroblasts. dans Proteomics 2008
Show all 21 Pubmed References
Human Polyclonal AKT Primary Antibody pour CyTOF, FACS - ABIN4900619
Wang, Yue, Kim, Fu, Khuri, Sun: Enhancing mammalian target of rapamycin (mTOR)-targeted cancer therapy by preventing mTOR/raptor inhibition-initiated, mTOR/rictor-independent Akt activation. dans Cancer research 2008
Show all 21 Pubmed References
Human Polyclonal AKT Primary Antibody pour ELISA, ICC - ABIN6259867
He, Cao, Liu, Li, Xu, Liu, Shi: Quercetin reverses experimental pulmonary arterial hypertension by modulating the TrkA pathway. dans Experimental cell research 2016
Show all 19 Pubmed References
Human Polyclonal AKT Primary Antibody pour ELISA, ICC - ABIN6255359
Yao, Jiang, Zhang, Liu, Du, Feng: Chrysin alleviates allergic inflammation and airway remodeling in a murine model of chronic asthma. dans International immunopharmacology 2016
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Human Polyclonal AKT Primary Antibody pour IHC, WB - ABIN362584
Bahk, Cho, Kim: A cross-talk between oncogenic Ras and tumor suppressor PTEN through FAK Tyr861 phosphorylation in NIH/3T3 mouse embryonic fibroblasts. dans Biochemical and biophysical research communications 2008
Show all 15 Pubmed References
Mouse (Murine) Polyclonal AKT Primary Antibody pour WB - ABIN4886448
Qin, Niu, Wang, Xu, Qiao, Gu: Heparanase induced by advanced glycation end products (AGEs) promotes macrophage migration involving RAGE and PI3K/AKT pathway. dans Cardiovascular diabetology 2013
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Chicken Monoclonal AKT Primary Antibody pour WB - ABIN3043108
Wang, Li, Lu, Bao, Zhao: Luteolin ameliorates cardiac failure in type I diabetic cardiomyopathy. dans Journal of diabetes and its complications 2012
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High AKT1 expression is associated with Hodgkin's lymphoma.
Knocking down Akt1 and Jak1 genes using siRNAs could increase levels of apoptosis.
High expressions of AKT1 is associated with non-small cell lung cancer.
Study demonstrated that expression of RhoB was decreased in osteosarcoma primary samples and cell lines. miR-19a, which exhibits abnormal expression in highly metastatic osteosarcoma cell lines, could inhibit the expression of RhoB and promote the lung metastasis of osteosarcoma cells in vivo. Results indicate that miR-19a-mediated RhoB is a critical regulator for the dephosphorylation of AKT1 in osteosarcoma cells.
LncRNA TP73-AS1 promoted the progression of lung adenocarcinoma via PI3K/AKT pathway.
we demonstrated that overexpression of CHP2 enhanced G1-S phase transition mediated by AKT activation, which subsequently induced phosphorylation and inactivation of FOXO3a in breast cancer cells.
this study suggests that miR-633 deletion can activate the AKT/mTOR pathway by targeting AKT1 to participate in the pathogenesis of systemic lupus erythematosus.
The effects of oridonin were verified in patient-derived xenograft tumors expressing high levels of AKT. In summary, our results indicate that oridonin acts as an AKT inhibitor to suppress the growth of esophageal squamous cell carcinoma (ESCC) by attenuating AKT signaling.
verall, the present study uncovered a yet unrecognized nuclear coupling of AKT and provides insights into the involvement of AKT in the interaction network of nuclear actin.
Report AKT1 p.Glu17Lys mutations occuring in intraductal papillary mucinous neoplasms of minor salivary glands.
study revealed that berberine not only up-regulates mRNA and protein levels of p21/cip1 and p27/kip1 but also increases their nuclear localization and post-translational protein stability. Further, Akt inhibition was found to mediate berberine-mediated up-regulation of p21/cip1 but not the p27/kip1.
SMOX plays a central role in the formation of bile canalicular lumen in liver cells by activating Akt pathway through acrolein production.
Study shows that the lack of Akt1 in human lung endothelial cells promotes prostate cancer cell transendothelial migration in vitro and metastasis to the mouse lungs in vivo involving increased nuclear localisation of beta-catenin and suppression of endothelial tight-junction proteins.
results suggest that HBP1 phosphorylation by AKT blocks its functions as transcriptional regulator and tumor suppressor.
Tumor necrosis factor receptor-associated factor 6 (TRAF6)-mediated proto-oncogene protein Akt (AKT) ubiquitination and subsequent phosphorylation played an essential role in the control of tumor cell malignant behavior.
Low Frequency Magnetic Fields Induce Autophagy-associated Cell Death in Lung Cancer through miR-486-mediated Inhibition of Akt/mTOR Signaling Pathway.
miR493 acted as a onco-miR in prostate cancer cells and promoted cell proliferation via inhibiting tumor suppresser PHLPP2 expression and activating Akt signaling pathway.
REVIEW: Oncogenic Roles of the PI3K/AKT/mTOR Axis
Circular RNA circNRIP1 acts as a microRNA-149-5p sponge to promote gastric cancer progression via the AKT1/mTOR pathway.
Upregulation of AKT1 is associated with Angiogenesis in Degenerated Discs.
present study highlighted that overexpression of miR-203 may function as a cardioprotective regulator in DCM by targeting PIK3CA via inactivation of PI3K/Akt signaling pathway.
The in vivo results revealed that DHL significantly attenuated LPS-induced pathological injury and reduced cytokines expression in the lung. NF-kappaB, p38 MAPK/MK2 and Akt signaling molecules were also involved in the anti-inflammatory effect.
Hippo has a role in suppressing IRS2/AKT signaling prevents hepatic steatosis and liver cancer in a mouse model
High-concentration hydrogen may exert cardioprotective effects through a PI3K-Akt1-dependent mechanism.
Our data indicate that the increased vulnerability of the diabetic myocardium to ischemia/reperfusion-induced apoptosis/dysfunction is attributable, in part, to decreased myocardial Sirt1 activity which leads to a decrease in Akt activation, an increase in Drp1 activity, culminating in excessive mitochondrial fission and ROS production.
Analysis of NF-kappaB activation caused by transient expression of proteins involved in the MyD88-dependent pathway in TLR signaling revealed that AKT1 suppressed signaling that occurs between activation of IKKbeta and that of NF-kappaB.
AMPK is an essential regulator for Akt activation by various stresses.
Data show that oncogenic phosphatidylinositol 3-kinase, catalytic, alpha polypeptide (PI3K)-proto-oncogene protein Akt (AKT)-activated epidermis exhibits a growth disadvantage even though its cells are more proliferative.
IL-15 regulates Bcl-2 family members Bim and Mcl-1 through JAK/STAT and PI3K/AKT pathways in T cells.
The role of Akt signaling in the hemangioendothelioma growth.
Akt1 deficiency leads to growth retardation.
CD36 knockdown in C2C12 myotubes accelerated insulin-stimulated Akt activation.
CLOCK phosphorylation by AKT on Ser-845 regulates its nuclear translocation and the expression levels of certain core circadian genes in insulin-sensitive tissues.
Exosomes derived from pancreatic cancer cells induce insulin resistance in C2C12 myotube cells through the Pik3cd/Akt/FoxO1 pathway.
Endothelial Akt1 signaling is necessary for ischemic resolution post-injury and likely reflects the consequence of NO insufficiency critical for vascular repair.
Akt1 plays a critical role in regulating satellite cell proliferation during load-induced muscle hypertrophy.
PIP5K1alpha was found to be required for AKT activation and calcium release, both of which were important for skeletal muscle differentiation.
Kcnj13 mutants exhibit a shorter trachea as well as defective smooth muscle cell alignment and polarity. Kcnj13 is essential to maintain ion homeostasis in tracheal smooth cells, which is required for actin polymerization and is mediated, at least in part, through activation of the actin regulator, AKT.
M-CSF-evoked ERK1/2 activation was decreased, whereas AKT activation was enhanced in SHP2-deficient BMMs. ERK1/2, via its downstream target RSK2, mediates this negative feedback by negatively regulating phosphorylation of M-CSF receptor at Tyr721 and, consequently, its binding to p85 subunit of PI3K and PI3K activation.
Site-directed mutagenesis of Akt at Cys224 revealed that S-nitrosylation at this site was pivotal for the reduced phosphorylation at Akt Ser473, which led to impaired Akt signaling. Furthermore, on HHcy challenge, as compared with GSNOR(+/+)ApoE(-/-) littermate controls, GSNOR(-/-)ApoE(-/-) double knockout mice showed reduced T-cell activation with concurrent reduction of atherosclerosis.
Phosphorylation of Akt on the Pdk1 site, Thr342, is significantly reduced by Toll signaling, and expression of mutant Akt(T342D) rescues cell and animal growth, nutrient storage, and viability in animals with active Toll signaling.
Our findings demonstrate a non-autonomous activation of a ROS sensing mechanism by Ask1 and Akt1 to replace the missing tissue after damage. Collectively, these results provide the basis for understanding the molecular mechanism of communication between dying and living cells that triggers regeneration.
The metabolic defects of cycG mutant animals are abrogated by a concomitant loss of Wdb, CycG presumably influences Akt1 activity at the PP2A nexus; Well rounded (Wrd), another B' subunit of PP2A in Drosophila, binds CycG similar to Wdb, and that its loss ameliorates some, but not all, of the metabolic defects of cycG mutants.
Our findings demonstrated that lovastatin restored LRRK2-G2019S neurite degeneration by augmenting Akt/NRF2 pathway and inhibiting downstream GSK3b activity, which decreased phospho-tau levels. We suggested that lovastatin is a potential disease-modifying agent for LRRK2-G2019S parkinsonism.
subtle manipulation of foxo through Akt1 can enhance survival during adverse nutrient conditions in Drosophila.
The developmental delay of these novel Akt1 hypomorphs results in a latent phenotype uncovered by generation of somatic clones
these data show that Drosophila Trbl has a conserved role to bind Akt and block Akt-mediated insulin signaling, and implicate Trib proteins as novel sites of signaling pathway integration that link nutrient availability with cell growth and proliferation
AKT1 and caspase-dependent regulation of Acn stability adjusts basal autophagy levels.
Akt1 governs two critical elements of synapse development, neurotransmitter receptor localization, and postsynaptic membrane elaboration
Tsc2 mutants showed a dramatic decrease in the levels of phosphorylated Akt, and interestingly, Akt mutants phenocopied Tsc2 mutants, leading to the hypothesis that Tsc2 and Akt might work via the same genetic pathway to regulate synapse growth.
Hippo signaling not only blocks cell division and promotes apoptosis, but also regulates cellular growth by inhibiting the Akt pathway activity.
Regeneration of Drosophila sensory neuron axons and dendrites is regulated by the Akt pathway involving Pten and microRNA bantam.
Overexpression of Akt enhanced Sindbis virus replication.
Perturbation of the Akt/Gsk3-beta signalling pathway is common to Drosophila expressing expanded untranslated CAG, CUG and AUUCU repeat RNAs.
dAkt activation under wild-type conditions is defined by feedback inhibition that depends on TOR Complex 1
Studies indicate that knockdown of dGirdin in the Drosophila wing imaginal disc cells resulted in reduction of cell size and this was enhanced by half reduction of the Akt gene dose.
dS6K activity is dependent on the Drosophila homologue of the phosphoinositide-dependent protein kinase 1, dPDK1, demonstrating that both dPDK1, as well as dTOR, mediated dS6K activation is phosphatidylinositide-3,4,5-trisphosphate (PIP3)-independent.
A mutation in the pleckstrin homology (PH) domain of Akt that reduces its affinity for PIP3 sufficed to rescue the lethality of flies devoid of PTEN activity.
stimulates growth by phosphorylating the tuberous sclerosis complex 2 (Tsc2) tumour suppressor and inhibiting formation of a Tsc1-Tsc2 complex
cell growth control by PTEN and it's ability to regulate known cell size regulators involved in protein translation (review)
The role of the PI3K/Akt/mTOR pathway in inflammatory regulation is independent of the activation of TLRs/NF-kappaB. Cross-talk between PI3K/Akt/mTOR and TLRs/NF-kappaB signaling pathways promote inflammation.
Thus, activation of STAT3 and inactivation of AKT signaling are involved in structural regression of the corpus luteum.
the measurement of levels of PI3K-Akt pathway components in FCs from ovarian follicles carrying oocytes with distinct developmental competences is a useful tool to identify putative molecular pathways involved in the acquisition of oocyte competence.
These results demonstrate that activation of AKT is required for gonadotropin regulation of CTNNB1 accumulation and subsequent ovarian E2 production.
Caveolin-1 scaffolding domain residue phenylalanine 92 modulates Akt signaling
TG2 contributes to 5-hydroxytryptamine-induced distal pulmonary artery smooth muscle cell proliferation via promotion of AKT signaling, likely via its serotonylation.
results suggest that PI3K-Akt activity is important for the internalization of S. aureus and phosphorylation of GSK-3alpha, GSK-3beta, and NF-kappaB.
The current study was designed to determine mechanisms underlying 20-hydroxyeicosatetraenoic acid -stimulated nitric oxide (NO) release, and particularly the role of NADPH oxidase, reactive oxygen species, and PI3-kinase in stimulated NO release.
PI3K/Akt and p53 are redox-regulated in bovine aortic endothelial cells exposed to hydrogen peroxide
Thus our data demonstrate that hypoxia-induced adventitial fibroblast proliferation requires activation and interaction of PI3K, Akt, mTOR, p70S6K, and ERK1/2.
Gab1 tyrosine phosphorylation is stimulated by flow shear stress to mediate protein kinase B and endothelial nitric-oxide synthase activation in endothelial cells
Losartan metabolite stimulates eNOS phosphorylation and suppresses tumor necrosis factor alpha-induced endothelial cell apoptosis by activating AKT1.
prostaglandin F2alpha phosphorylates TSC2 and activates mTOR and ribosomal protein S6 kinase signaling in an AKT-independent manner
Results suggest that the mitogenic response to FGF-2 in vivo in the corneal endothelial layer may be inhibited by TGF-beta2-induced suppression of the PI3-kinase/AKT signaling pathway.
These results suggest that bGPR40 mediates LCFA signaling in mammary epithelial cells and thereby plays an important role in cell proliferation and survival.
Data show that laminar shear stress stimulates vascular smooth muscle cell apoptosis via the Akt pathway.
The intracellular mechanism of action of CART in regulation of FSH-induced MAPK signaling.
AMPK and AKT are both downstream of PI3K and that AKT activation is partially dependent on AMPK. The interrelationship between AMPK and AKT, although known to be individually important in mediating VEGF activation of eNOS, is clearly characterized.
These findings highlight novel and essential roles of PFKFB4 activity in later stages of neural crest (NC) development that are wired into the NC gene regulatory network.
Once inside in proximal tubule cells, glucose is diverted to the hexosamine biosynthetic pathway increasing O-GlcNAcylation of several intracellular proteins, including PKB.
Studied the effects of microRNA-27a on myogenin expression and the Akt/FoxO1 signal pathway during porcine myoblast differentiation. Overexpression of miR-27a suppressed myogenin expression during porcine myoblast differentiation, whereas inhibition of miR-27a promoted the mRNA and protein expression levels of myogenin; overexpression of miR-27a decreased the level of P-Akt/Akt and increased the protein level of FoxO1.
SCF is a critical regulatory factor for conceptus development and implantation during pregnancy in pigs.
These results indicate glycine enhances muscle protein mass under an inflammatory condition. The beneficial roles of glycine on the muscle are closely associated with maintaining Akt-mTOR-FOXO1 signaling and suppressing the activation of TLR4 and/or NOD2 signaling pathways.
Data show that homocysteine (Hcy) can ameliorate the endothelium-independent hypoxic coronary vasoconstriction, in which the inhibition of PI3K/Akt signaling pathway may be involved.
In pigs, lactose synthesis was significantly elevated with the increase of milk production and AKT1 could positively regulate lactose synthesis.
In conclusion, our observations reveal that PRRSV triggers the activation of FAK-PI3K-AKT-Rac1 signaling pathway to facilitate its entry into cells.
Host PI3K and Akt1 play a role in viral gene expression, leading to an increase in porcine reproductive and respiratory syndrome virus replication.
Activity of AKT is not essential for induction of germinal vesicle breakdown in porcine oocytes but plays a substantial role during progression of meiosis to MI/MII-stage.
IL-4 induced activation of Akt/SREBP-1/lipid biosynthesis in EC, resulting in protection against membrane attack complex and melittin, in association with mitochondrial protection.
findings show that megalin is the sensor that determines whether cells will be protected or injured by albumin; it binds protein kinase B (PKB) in a D-3-phosphorylated phospholipid-insensitive manner, anchoring PKB in the luminal plasma membrane [
protein kinase B (PKB/Akt)was localized in the granulosa cells of primordial follicles and in the basal layers of the granulosa cells of preantral and antral follicles, but were not localized in atretic follicles and corpora lutea
Akt signaling in porcine patellofemoral joint cartilage is dependent upon frequency of loading, cartilage zone, and the time interval between loading and cartilage harvest.
in VSMCs exposed to hyperglycemia, IGF-I stimulation of Shc facilitates the transfer of Grb2 to p85 resulting in enhanced PI3K activation and AKT phosphorylation leading to enhanced cell proliferation and migration
There was no correlation of infarct size with expression or phosphorylation of AKT in ischemic postconditioning.
CIPK23 and AtKC1 exhibit distinct effects; however, they act synergistically and balance K(+) uptake/leakage to modulate AKT1-mediated low potassium responses in Arabidopsis.
results suggest that NO decreases K(+) absorption by promoting the synthesis of vitamin B6 PLP, which further represses the activity of K(+) channel AKT1 in Arabidopsis.
Examination of the athak5 atakt1 double mutant, revealing novel aspects of an uptake system as yet unidentified by genetic means.
AKT1 is regulated by CIPK23 in guard cells and is involved in water stress responses.
These findings provide further insights into the signaling network consisting of CBL-CIPK-PP2C interactions in the activation of the AKT1 channel.
Electrophysiological results showed that AtKC1 inhibited the AKT1-mediated inward K(+) currents and negatively shifted the voltage dependence of AKT1 channels.
AtHAK5 and AKT1 are vital for plant growth and development at low K+ concentrations.
In the range between 0.01 and 0.05 mM K+ AtHAK5 and AtAKT1 are the only contributors to K+ acquisition. At higher K+ concentrations, unknown systems come into operation and participate together with AtAKT1 in low-affinity K+ uptake.
Potassium transport and gene expression in A. thaliana deficient at this site.
CIPK23 directly phosphorylates the K+ transporter AKT1
Data show that interacting calcium sensors (CBL1 and CBL9) together with CIPK23, but not either alone, activated the AKT1 channel in a Ca(2+)-dependent manner, connecting the Ca(2+) signal to K(+) uptake through activation of a K(+) channel.
AtAKT1 mediates K+ absorption at high concentrations, and remains active in the presence of NH4+ although activity is reduced.
AtKC1-AKT1 channels in Arabidopsis roots facilitate growth under K+-limiting conditions
the LIN-28/let-7/AKT/DAF-16 axis is a program that plays an important role in balancing reproduction and somatic maintenance.
this study shows that akt-1 and akt-2 negatively regulate DNA-damage-induced apoptosis in the C. elegans germline and the antiapoptotic activity of akt-1 is independent of its target gene daf-16 but dependent on cep-1/p53.
Modulation of pptr-1 affects insulin/IGF-1 signaling pathway-associated phenotypes including life span, dauer, stress resistance, and fat storage; study shows that PPTR-1 functions by regulating worm AKT-1 phosphorylation at Thr 350.
Exogenous AKT was transcribed, and AKT was overexpressed, inducing the phosphorylation of p70S6K (Thr389) and 4E-BP1 (Thr37/46) in goat fetal fibroblasts.
findings suggested that the expressions of the cardiac CACNA1C were under the CLOCK-BMAL1 regulation, probably through the PI3K-Akt signal pathway
This study has identified Akt as a novel intracellular pathway required for neural crest differentiation.
Overexpression of human Akt1 enhances adipogenesis and leads to lipoma formation in zebrafish.
The serine-threonine protein kinase encoded by the AKT1 gene is catalytically inactive in serum-starved primary and immortalized fibroblasts. AKT1 and the related AKT2 are activated by platelet-derived growth factor. The activation is rapid and specific, and it is abrogated by mutations in the pleckstrin homology domain of AKT1. It was shown that the activation occurs through phosphatidylinositol 3-kinase. In the developing nervous system AKT is a critical mediator of growth factor-induced neuronal survival. Survival factors can suppress apoptosis in a transcription-independent manner by activating the serine/threonine kinase AKT1, which then phosphorylates and inactivates components of the apoptotic machinery. Mutations in this gene have been associated with the Proteus syndrome. Multiple alternatively spliced transcript variants have been found for this gene.
, RAC-alpha serine/threonine-protein kinase
, protein kinase B alpha
, proto-oncogene c-Akt
, rac protein kinase alpha
, AKT1 kinase
, protein kinase B-alpha
, proto-oncogene c-AKT
, related to A and C kinases
, Akt kinase
, dAkt kinase
, protein kinase B
, related to PKA to PKC protein kinases
, related to the A and C kinases
, actin, cytoplasmic 1
, gamma non-muscle actin
, RAC protein kinase alpha RAC-PK alpha
, murine thymoma viral (v-akt) oncogene homolog 1
, thymoma viral proto-oncogene 1
, v-akt murine thymoma viral oncogene-like protein 1
, serine/threonine protein kinase
, protein kinase Akt-1
, protein kinase B, alpha
, v-akt murine thymoma viral oncogene homolog 1
, v-akt murine thymoma viral oncogene-like 1