Rabbit AKT1 Monoclonal Antibody | anti-AKT1 antibody

AKT1, phosphorylated (Ser473) (Rac PKa, PKBa) (Biotin)

Cat. Num. AAA6242941

• Gene Names: AKT1; AKT; PKB; RAC; CWS6; PRKBA; PKB-ALPHA; RAC-ALPHA
• Reactivity: Bovine, Chicken, Human, Mouse, Rat, Xenopus
• Applications: Western Blot
• Purity: Purified by Protein A Affinity Chromatography.
• Synonyms: AKT1; Monoclonal Antibody; phosphorylated (Ser473) (Rac PKa; PKBa) (Biotin); anti-AKT1 antibody

• Host: Rabbit
• Reactivity: Bovine, Chicken, Human, Mouse, Rat, Xenopus
• Clonality: Monoclonal
• Isotype: IgG
• Clone Number: 5H45
• Specificity: Recognizes phosphorylated Akt1/PKBa, Mr ~60kD. Crossreactivity to phosphorylated Akt2 and Akt3 likely based on sequence homology. Species Crossreactivity: Human and mouse. Predicted crossreactivity with rat, bovine, chicken, and Xenopus based on immunogen sequence homology.
• Purity/Purification: Purified by Protein A Affinity Chromatography.
• Form/Format: Supplied as a liquid in PBS, pH 7.2. No preservative added. Labeled with Biotin.

• Applicable Applications for anti-AKT1 antibody: Western Blot (WB)
• Immunogen: KLH-conjugated, synthetic peptide containing a pSer that corresponds to amino acid position 473 of human Akt1/PKBa. The immunizing sequence is identical in mouse and bovine Akt1. Akt2 and Akt3 share significant homology with the peptide immunogen sequence.
• Conjugate: Biotin
• Preparation and Storage: Store at -20 degree C.

Testing Data

(Untreated (Lanes 1 and 3) or PDGF stimulated (lanes 2 and 4) NIH-3T3 cell lysate was resolved by electrophoresis, transferred to nitrocellulose and probed with antiphospho-Akt1/PKBa (Ser473) (0.4ug/ml, lanes 1 and 2). Or Total Anti-Akt1/PKBa (1:1000, Lanes 3 and 4). Proteins were visualized using a goat anti-rabbit secondary antibody conjugated to HRP and a chemiluminescence detection system. Arrow indicates phosphorylated Akt1/PKBa (~60kD).)

Product Categories/Family for anti-AKT1 antibody

Antibodies; Transcription Factors

References

1. Cross, D.A., et al., Nature 378: 785-789, 1995. 2. James, S.R., et al., Biochem. J. 315: 709-713, 1996. 3. Alessi, D.R., et al., Curr. Biol. 8: 69-81, 1998. 4. Alessi, D.R., et al., Curr. Biol. 7: 776-789, 1997. 5. Cohen, P., et al., FEBS Lett. 410: 3-10, 1997. General References:1. Spieker-Polet H, et al. Proc Natl Acad Sci. 1995 Sep 26;92(20):9348-52. 2. Liguori MJ, et al. Hybridoma. 2001 Jun; 20(3):189-98. 3. G.Cano1, F. Milanezi2, D. Leitao2,3, S. Ricardo2, M.J. Brito1, F. C. Schmitt2-3 1Garcia da Orta Hospital, Almada, Portugal,2 Inst. Molec. Pathology and Immunology of Porto University, Portugal,3 Medical Faculty of Porto university, Portugal Diagn Cytopathol, 2003 Oct; 29(4): 207 -11. 4. L.K. Diaz* and N.Sneige *Department of Pathology,Northwestern University, Chicago,+ Department of Pathology, University of Texas, Huston, Adv Anat Pathol,2005; 12(1), 10-19. 5. Z. Huang1, W. Zhu2, G. Szekeres3, H. Xia1 1Spring Bioscience Corp, Fremont,CA, 2 Epitomics Inc, Burlingame,CA,, 4Histopathology Ltd, Hungary, Appl Immunohistochem Mol Morphol. 2005; 13 (1): 91-95 6. S. Rossi1, E. Orvieto1, S.Chinellato1, A. Furlanetto1, L.Laurino1, F. Facchetti2, AP Dei Tos 2 1Department of Pathology, 2Treviso, Italy; *Brescia, University School of Medicine, Brescia, Italy., Abstract presented at USCAP 2004. Modern Pathology 2004; 17 (suppl 1): 361A 7. M. Blechner, E. Ballesteros, D. Mandich, D. Stevens, R. Cartun, Hartford Hospital, Hartford, CT. Abstract presented at USCAP 2004. Modern Pathology 2004; 17 (suppl 1): 241A 8. W. Cheuk, K.O.Y. Wong, C.S.C. Wong and J.K.C. Chan, Department of Pathology, Queen Elizabeth Hospital, Hong Kong, Am J Surg Path, 2004; 28 (6): 801-807. 9. G.B. Budd, E. Tso, B. Yoder, T. Choueiri, P. Elson, S. Tarr, M. Skacel, R. Tubbs, A. Dawson, D. Hicks, Cleveland Clinic Foundation, Cleveland, OH, Abstract presented at ASCO Annual meeting, June 2004, New Orleans 10. S. M. Tarr, S. Short, K. Hansen, T. Morken, H. Xia, E. Downs-Kelly, R. R. Tubbs, D. G. Hicks, Department of Pathology and Laboratory Medicine. The Cleveland Clinic Foundation, Cleveland, Ohio. Lab Vision Corp., Fremont, Ca., Spring Bioscience Corp, Fremont,CA, Abstract presented at Association for Molecular Pathology meeting, Los Angeles, 2004 11. A.M. Gown, T.S. Barry, P. Kandalaft, L.C. Goldstein, C.C. Tse and D.O. Treaba, Clinical Research Division, PhenoPath Laboratories and IMPRIS, Seattle, WA, Abstract presented at USCAP 2005. Modern Pathology 2005; 18, suppl.1,pag 35A 12. D.O. Treaba, A.W. Hing, L.C. Goldstein, T.S. Barry, P. Kandalaft, C.B. Gilks, T.O. Nielsen and A.M. Gown, Clinical Research Division, PhenoPath Laboratories and IMPRIS, Seattle, WA, USA Genetic Pathology Evaluation Centre, University of British Columbia, Vancouver, BC, Canada, Abstract presented at USCAP 2005. Modern Pathology 2005; 18, suppl.1,pag 53A 13. S. Rossi1, L. Laurino1, A. Furlanetto1, S.Chinellato1, E. Orvieto1, F. Canal1, F. Facchetti2, A.P. Dei Tos1 1 Depart. Pathology, Hospital of Treviso, Italy, 2 Brescia University School of Medicine, Brescia, Italy, Am J Clin Pathol, 2005, Aug;124(2):295-302

NCBI and Uniprot Product Information

• NCBI GI #: 62241013
• NCBI GeneID: 207
• NCBI Accession #: NP_001014431.1
• NCBI GenBank Nucleotide #: NM_005163
• UniProt Accession #: P31749; Q9BWB6; B2RAM5
• 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
• Protein Family: Potassium channel
• 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