Kinase Akt1/PKB alpha Inactive Enzyme Active Protein | PKAkt1/PKBa active protein

Recombinant Human Protein Kinase Akt1/PKB alpha Inactive Enzyme

Cat. Num. AAA142753

• Gene Names: AKT1; AKT; PKB; RAC; CWS6; PRKBA; PKB-ALPHA; RAC-ALPHA
• Purity: Greater than 90% as determined by SDS-PAGE.
• Synonyms: Kinase Akt1/PKB alpha Inactive Enzyme; Recombinant Human Protein Kinase Akt1/PKB alpha Inactive Enzyme; PKAkt1/PKBa Human; Protein Kinase Akt1/PKB alpha; Inactive enzyme Human Recombinant; RAC-alpha serine/threonine-protein kinase; EC 2.7.11.1; RAC-PK-alpha; Protein kinase B; PKB; C-AKT; AKT1; AKT; RAC; PRKBA; MGC99656; RAC-ALPHA; PKAkt1/PKBa active protein

• Host: Sf9 Insect Cells
• Purity/Purification: Greater than 90% as determined by SDS-PAGE.
• Form/Format: PKAkt1 1.9mg/ml, in 50mM Tris-HCl, 100mM NaCl, 1mM DTT, 25mM beta glycerophosphate, 50% glycerol, pH 8.5.; Sterile Filtered clear solution.
• Sequence Length: 480

• Unit Defenition: 1 Unit is defined as 1 picomole phosphate transferred to the synthetic peptide (RPRAATF) per min at 30 degree C.
• Activity: No protease activity (Twinning test). The Specific activity is 235 U/mg.
• Preparation and Storage: Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. Avoid multiple freeze-thaw cycles.

Related Product Information for PKAkt1/PKBa active protein

Description: PKAkt1 is a glycosilated polypeptide having a molecular mass of 59.1 kDa, fused with a polyhistidine tag at N-terminus (to facilitate removal of Akt1 kinase from the reaction mixture).Inactive enzyme, suitable for negative control experiments or for phosphorylation as a substrate.Recombinant Protein Kinase B is purified by proprietary chromatographic techniques.

Introduction: Akt1, also known as "Akt" or protein kinaseB (PKB) is an important molecule in mammaliancellular signaling.In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. These enzymesare members of the serine/threonine-specific protein kinasefamily (EC2.7.11.1).Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesispathways, and is therefore a key signaling protein in the cellular pathways that lead to skeletal muscle hypertrophy, and general tissue growth. Since it can block apoptosis, and thereby promote cell survival, Akt1 has been implicated as a major factor in many types of cancer. Akt (now also called Akt1) was originally identified as the oncogenein the transforming retrovirus, AKT8.

Product Categories/Family for PKAkt1/PKBa active protein

Protein Kinases; Enzymes; Protein Kinase Akt1/PKB alpha

NCBI and Uniprot Product Information

• NCBI GI #: 62241013
• NCBI GeneID: 207
• NCBI Accession #: NP_001014431.1
• NCBI GenBank Nucleotide #: NM_001014431.1
• UniProt Accession #: P31749; Q9BWB6; B2RAM5; B7Z5R1
• Molecular Weight: 48,347 Da
• NCBI Official Full Name: RAC-alpha serine/threonine-protein kinase
• NCBI Official Synonym Full Names: v-akt murine thymoma viral oncogene homolog 1
• NCBI Official Symbol: AKT1
• NCBI Official Synonym Symbols: AKT; PKB; RAC; CWS6; PRKBA; PKB-ALPHA; RAC-ALPHA
• NCBI Protein Information: RAC-alpha serine/threonine-protein kinase; AKT1m; PKB alpha; RAC-PK-alpha; protein kinase B alpha; proto-oncogene c-Akt; rac protein kinase alpha
• UniProt Protein Name: RAC-alpha serine/threonine-protein kinase
• UniProt Gene Name: AKT1
• UniProt Synonym Gene Names: PKB; RAC; PKB; PKB alpha
• UniProt Entry Name: AKT1_HUMAN

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: Oncoprotein; Kinase, protein; EC 2.7.11.1; Protein kinase, AGC; Protein kinase, Ser/Thr (non-receptor); AGC group; AKT family

Chromosomal Location of Human Ortholog: 14q32.32

Cellular Component: microtubule cytoskeleton; nucleoplasm; mitochondrion; cytoplasm; plasma membrane; spindle; intercellular junction; cytosol; nucleus

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; regulation of myelination; positive regulation of nitric oxide biosynthetic process; nerve growth factor receptor signaling pathway; protein ubiquitination; glucose homeostasis; regulation of cell migration; G1/S-specific positive regulation of cyclin-dependent protein kinase activity; protein amino acid phosphorylation; 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; striated muscle cell differentiation; negative regulation of protein kinase activity; positive regulation of fat cell differentiation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription factor activity; positive regulation of endothelial cell proliferation; regulation of nitric-oxide synthase activity; response to oxidative stress; negative regulation of apoptosis; negative regulation of autophagy; negative regulation of fatty acid beta-oxidation; translation; apoptosis; protein amino acid autophosphorylation; positive regulation of cellular protein metabolic process; regulation of glycogen biosynthetic 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; cell differentiation; nitric oxide biosynthetic process; activated T cell apoptosis; aging; epidermal growth factor receptor signaling pathway; negative regulation of proteolysis; phosphoinositide-mediated signaling; myelin maintenance in the peripheral nervous system; protein modification process; positive regulation of peptidyl-serine phosphorylation; endocrine pancreas development; 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; vascular endothelial growth factor receptor signaling pathway; blood coagulation; phosphorylation; hyaluronan metabolic process

Disease: Schizophrenia; Cowden Syndrome 6; Proteus Syndrome; Breast Cancer; Ovarian Cancer