Rabbit Pan-AKT Polyclonal Antibody | anti-Pan-AKT antibody

anti-Pan-AKT antibody

Cat. Num. AAA7611954

• Gene Names: AKT1; AKT; PKB; RAC; CWS6; PRKBA; PKB-ALPHA; RAC-ALPHA
• Reactivity: Human, Mouse, Rat
• Applications: ELISA, Western Blot, Immunohistochemistry, Immunofluorescence, Immunoprecipitation
• Purity: >=95% as determined by SDS-PAGE. Immunogen affinity purified
• Synonyms: Pan-AKT; Polyclonal Antibody; anti-Pan-AKT antibody; AKT1/AKT2/AKT3

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: >=95% as determined by SDS-PAGE. Immunogen affinity purified
• Form/Format: Liquid. PBS with 0.02% sodium azide and 50% glycerol pH7.3

• Applicable Applications for anti-Pan-AKT antibody: ELISA (EIA), Western Blot (WB), Immunohistochemistry (IHC), Immunofluorescence (IF), Immunoprecipitation (IP)
• Application Notes: WB: 1:200-1:800; IHC: 1:20-1:100; IF: 1:20-1:100; IP: 1:20-1:100
• Immunogen: human AKT1/AKT2/AKT3
• Preparation and Storage: Store at -20 degree C for 12 months. Avoid repeated freeze/thaw cycles.

Immunohistochemistry (IHC)

(Immunohistochemistry of paraffin-embedded rat kidney tissue slide using MBS7611954(Pan-AKT Antibody) at dilution of 1:50)

Immunofluorescence (IF)

(Immunofluorescent analysis of U2OS cells using MBS7611954(Pan-AKT Antibody) at dilution of 1:50.)

Western Blot (WB)

(A549 cells were subjected to SDS PAGE followed by western blot with MBS7611954(Pan-AKT Antibody) at dilution of 1:500)

Related Product Information for anti-Pan-AKT antibody

Human AKT serine-threonine protein kinase family includes three members AKT1,AKT2, AKT3, which are also often referred to as protein kinase B alpha, beta, and gamma. These highly similar AKT proteins all have an N-terminal pleckstrin homology domain, a serine/threonine-specific kinase domain and a C-terminal regulatory domain. These proteins are phosphorylated by phosphoinositide 3-kinase (PI3K). AKT/PI3K forms a key component of many signalling pathways that involve the binding of membrane-bound ligands such as receptor tyrosine kinases, G-protein coupled receptors, and integrin-linked kinase. These AKT proteins therefore regulate a wide variety of cellular functions including cell proliferation, survival, metabolism, and angiogenesis in both normal and malignant cells. AKT proteins are recruited to the cell membrane by phosphatidylinositol 3,4,5-trisphosphate (PIP3) after phosphorylation of phosphatidylinositol 4,5-bisphosphate (PIP2) by PI3K. Subsequent phosphorylation of both threonine residue 308 and serine residue 473 is required for full activation of the AKT1 protein encoded by this gene.

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; P31751; Q9Y243
• Molecular Weight: 55,686 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; PKB alpha; RAC-PK-alpha; proto-oncogene c-Akt; protein kinase B alpha; 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: 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