SDS-Page
(Recombinant AKT1 protein gel 10% SDS-PAGE Coomassie staining MW: 60.5 kDa Purity: ?95%)
AKT1 recombinant protein
Recombinant AKT1 protein
Kinase Activity Assay Conditions: 1 uM STK S3 substrate was incubated with different concentrations AKT1 protein in a 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, 5 nM SEB and 100 uM ATP for 1 hour. The 10 ul detection reagents containing TK antibody and SA-XL665, each of which was 1:100 diluted with 1×Detection Buffer were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature, and HTRF KinEASE STK assay was used to detect the enzymatic activity.
Shipping Temp: Dry Ice
SDS-Page
(Recombinant AKT1 protein gel 10% SDS-PAGE Coomassie staining MW: 60.5 kDa Purity: ?95%)
SDS-Page
(Recombinant AKT1 protein gel 10% SDS-PAGE Coomassie staining MW: 60.5 kDa Purity: ?95%)
Testing Data
(HTRF assay for recombinant AKT1 protein activity 1 uM STK S3 substrate was incubated with different concentrations AKT1 protein a 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, 5 nM SEB and 100 uM ATP for 1 hour. The 10 ul detection reagents containing STK antibody and SA-XL665, each of which was 1:100 diluted with 1× Detection Buffer were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature. HTRF KinEASE STK assay was used to detect the enzymatic activity.)
Testing Data
(HTRF assay for recombinant AKT1 protein activity 1 uM STK S3 substrate was incubated with different concentrations AKT1 protein a 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, 5 nM SEB and 100 uM ATP for 1 hour. The 10 ul detection reagents containing STK antibody and SA-XL665, each of which was 1:100 diluted with 1× Detection Buffer were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature. HTRF KinEASE STK assay was used to detect the enzymatic activity.)
Testing Data
(HTRF assay for recombinant AKT1 protein activity 1 uM STK S3 substrate was incubated with different concentrations AKT1 protein a 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, 5 nM SEB and 100 uM ATP for 1 hour. The 10 ul detection reagents containing STK antibody and SA-XL665, each of which was 1:100 diluted with 1× Detection Buffer were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature. HTRF KinEASE STK assay was used to detect the enzymatic activity.)
Testing Data
(HTRF assay for recombinant AKT1 protein activity 1 uM STK S3 substrate was incubated with different concentrations AKT1 protein a 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, 5 nM SEB and 100 uM ATP for 1 hour. The 10 ul detection reagents containing STK antibody and SA-XL665, each of which was 1:100 diluted with 1× Detection Buffer were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature. HTRF KinEASE STK assay was used to detect the enzymatic activity.)
Background: AKT1 (AKT Serine/Threonine Kinase 1), also known as Protein Kinase B Alpha, PRKBA or PKB Alpha, is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidateshave been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake and the storage of glucose. It also regulates cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase), mediates insulin-stimulated protein synthesis by phosphorylating TSC2. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. AKT has an important role in the regulation of NF-kappa-B-dependentgene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the correct neuron positioning, dendritic development and synapse formation.
AKT1-specific substrates have been recently identified, including palladin (PALLD), which phosphorylation modulates cytoskeletal organization and cell motility; prohibitin (PHB), playing an important role in cell metabolism and proliferation; and CDKN1A, for which phosphorylation at Thr-145 induces its release from CDK2 and cytoplasmic relocalization. Theserecent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation.
NCBI and Uniprot Product Information
NCBI Description
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. [provided by RefSeq, Jul 2011]
Uniprot Description
Akt1: an oncogenic AGC kinase that plays a critical role in regulating cell survival and metabolism in many different signaling pathways. Dual phosphorylation is required for its activation. T308 is phosphorylated by PDK1 in the PI3 kinase pathway, and S473 is phosphorylated by mTOR in the mTORC2 pathway. The 'Lys-63'-linked ubiquitination of AKT1 by TRAF6 is important for its translocation to the plasma membrane, phosphorylation, and activation. When Akt is fully phosphorylated it translocates into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its proteosomal degradation. Hyperactive or overexpressed in a number of cancers including breast, prostate, lung, pancreatic, liver, ovarian and colorectal. Over 160 protein substrates are known including many that regulate transcription, metabolism, apoptosis, cell cycle, and growth.
Protein type: EC 2.7.11.1; Protein kinase, Ser/Thr (non-receptor); Protein kinase, AGC; Oncoprotein; Kinase, protein; AGC group; AKT family
Chromosomal Location of Human Ortholog: 14q32.32
Cellular Component: nucleoplasm; microtubule cytoskeleton; mitochondrion; cytoplasm; plasma membrane; spindle; intercellular junction; nucleus; cytosol
Molecular Function: identical protein binding; protein serine/threonine kinase activity; protein binding; phosphatidylinositol-3,4,5-triphosphate binding; enzyme binding; protein kinase C binding; nitric-oxide synthase regulator activity; protein serine/threonine/tyrosine kinase activity; kinase activity; phosphatidylinositol-3,4-bisphosphate binding; ATP binding; protein kinase activity
Biological Process: negative regulation of JNK cascade; positive regulation of nitric oxide biosynthetic process; regulation of myelination; nerve growth factor receptor signaling pathway; protein ubiquitination; glucose homeostasis; regulation of cell migration; protein amino acid phosphorylation; G1/S-specific positive regulation of cyclin-dependent protein kinase activity; germ cell development; positive regulation of glucose import; cell projection organization and biogenesis; protein catabolic process; maternal placenta development; response to food; platelet activation; glycogen biosynthetic process; fibroblast growth factor receptor signaling pathway; positive regulation of nitric-oxide synthase activity; positive regulation of blood vessel endothelial cell migration; glucose metabolic process; positive regulation of lipid biosynthetic process; positive regulation of cell growth; insulin-like growth factor receptor signaling pathway; cellular response to insulin stimulus; response to heat; T cell costimulation; positive regulation of fat cell differentiation; negative regulation of protein kinase activity; striated muscle cell differentiation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of endothelial cell proliferation; positive regulation of transcription factor activity; response to oxidative stress; regulation of nitric-oxide synthase activity; negative regulation of apoptosis; negative regulation of autophagy; negative regulation of fatty acid beta-oxidation; translation; apoptosis; protein amino acid autophosphorylation; regulation of glycogen biosynthetic process; positive regulation of cellular protein metabolic process; positive regulation of glycogen biosynthetic process; negative regulation of cell size; negative regulation of caspase activity; glucose transport; signal transduction; nitric oxide metabolic process; regulation of translation; apoptotic mitochondrial changes; protein kinase B signaling cascade; inflammatory response; nitric oxide biosynthetic process; cell differentiation; activated T cell apoptosis; aging; negative regulation of proteolysis; epidermal growth factor receptor signaling pathway; phosphoinositide-mediated signaling; myelin maintenance in the peripheral nervous system; protein modification process; endocrine pancreas development; positive regulation of peptidyl-serine phosphorylation; osteoblast differentiation; cell proliferation; G-protein coupled receptor protein signaling pathway; peptidyl-serine phosphorylation; protein import into nucleus, translocation; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; insulin receptor signaling pathway; positive regulation of vasoconstriction; innate immune response; gene expression; positive regulation of protein amino acid phosphorylation; blood coagulation; vascular endothelial growth factor receptor signaling pathway; phosphorylation; hyaluronan metabolic process
Disease: Schizophrenia; Cowden Syndrome 6; Proteus Syndrome; Breast Cancer; Ovarian Cancer
Research Articles on AKT1
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Product Notes
The AKT1 akt1 (Catalog #AAA389202) is a Recombinant Protein produced from Baculovirus and is intended for research purposes only. The product is available for immediate purchase. Recombinant AKT1 protein is suitable for use in the study of enzyme kinetics, inhibitor screening, and selectivity profiling. Kinase Activity Assay Conditions: 1 uM STK S3 substrate was incubated with different concentrations AKT1 protein in a 10 ul reaction system containing 1×Enzymatic Buffer, 5 mM MgCl2, 1 mM DTT, 5 nM SEB and 100 uM ATP for 1 hour. The 10 ul detection reagents containing TK antibody and SA-XL665, each of which was 1:100 diluted with 1×Detection Buffer were added and incubated with the reactions for 30 min. All the operations and reactions were performed at room temperature, and HTRF KinEASE STK assay was used to detect the enzymatic activity. Researchers should empirically determine the suitability of the AKT1 akt1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "AKT1, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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