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14-279 Sigma-AldrichAkt1/PKBα Protein, inactive, 50 µg

inactive, N-terminal His6-tagged recombinant full-length human Akt1, for use in Kinase Assays.

Akt1/PKBα Protein, inactive, 50 µg MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

SDS
CoA
References

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Overview

Replacement Information

Description
Catalogue Number	14-279
Brand Family	Upstate
Trade Name	Upstate
Description	Akt1/PKBα Protein, inactive, 50 µg
Overview	N-terminal His6-tagged recombinant full-length human Akt1

References

Product Information
Quality Level	MQ100

Applications
Application	inactive, N-terminal His6-tagged recombinant full-length human Akt1, for use in Kinase Assays.
Key Applications	Kinase Assay

Biological Information
Source	expressed by baculovirus in Sf21 insect cells
Specific Activity	For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
Entrez Gene Number	NM_001014431.1 NM_001014432.1 NM_005163.2
Entrez Gene Summary	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. Multiple alternatively spliced transcript variants have been found for this gene.
Gene Symbol	AKT1 RAC PRKBA MGC99656 RAC-ALPHA RAC-PK-alpha C-AKT PKB AKT
Protein Target	Akt1/PKBα
Purification Method	Ni²⁺/NTA-agarose
Target Sub-Family	AGC
UniProt Number	P31749
UniProt Summary	FUNCTION: SwissProt: P31749 # General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis, partly by playing a role in both insulin-induced phosphorylation of 4E-BP1 and in insulin-induced activation of p70 S6 kinase. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase. SIZE: 480 amino acids; 55686 Da SUBUNIT: Interacts with CENTG1 isoform 2 (PIKE-A) in the presence of guanine nucleotides. The C-terminus interacts with CCDC88A/GRDN. Interacts with AKTIP. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nucleus after activation by integrin-linked protein kinase 1 (ILK1). TISSUE SPECIFICITY: In all human cell types so far analyzed. DOMAIN: SwissProt: P31749 Binding of the PH domain to the phosphatidylinositol 3- kinase alpha (PI(3)K) results in its targeting to the plasma membrane. PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity. Ser-473 phosphorylation by the Rictor-mTor complex favors Thr-308 phosphorylation by PDPK1. Ser-473 phosphorylation is enhanced by interaction with CENTG1 isoform 2 (PIKE-A). SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily. & Contains 1 AGC-kinase C-terminal domain. & Contains 1 PH domain. & Contains 1 protein kinase domain.
Molecular Weight	59kDa

Physicochemical Information

Dimensions

Materials Information

Toxicological Information

Safety Information according to GHS

Safety Information

Product Usage Statements
Quality Assurance	routinely evaluated by phosphorylation of Crosstide
Usage Statement	Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage and Shipping Information
Storage Conditions	6 months at -20°C

Packaging Information
Material Size	50 µg

Transport Information

Supplemental Information

Specifications

Global Trade Item Number
Catalogue Number	GTIN
14-279	04053252624872

Documentation

Akt1/PKBα Protein, inactive, 50 µg SDS

Title
Safety Data Sheet (SDS)

Akt1/PKBα Protein, inactive, 50 µg Certificates of Analysis

Title	Lot Number
Akt1/PKB#945;, unactive - D8SN004U-N	D8SN004U-N
Akt1/PKB#945;, unactive - D8SN004U-O	D8SN004U-O
Akt1/PKB#945;, unactive - D8SN004U-P	D8SN004U-P
Akt1/PKB#945;, unactive - D8SN004U-Q	D8SN004U-Q
Akt1/PKB#945;, unactive - D8SN004U-R	D8SN004U-R
Akt1/PKB#945;, unactive - D8SN004U-S	D8SN004U-S
Akt1/PKB#945;, unactive - D8SN004U-T	D8SN004U-T
Akt1/PKBα, unactive - D8SN004U-U	D8SN004U-U

References

Reference overview	Application	Pub Med ID
Stoichiometry of site-specific protein phosphorylation estimated with phosphopeptide-specific antibodies. Mîinea, Cristinel P and Lienhard, Gustav E BioTechniques, 34: 828-31 (2003) 2003	Kinase Assay	12703308
Synergistic Activation of Endothelial Nitric-oxide Synthase (eNOS) by HSP90 and Akt: CALCIUM-INDEPENDENT eNOS ACTIVATION INVOLVES FORMATION OF AN HSP90-Akt-CaM-BOUND eNOS COMPLEX Takahashi, S. and Mendelsohn, M. E. J Biol Chem, 278:30821-7 (2003) 2003	Kinase Assay	12799359
Inhibition of integrin-linked kinase/protein kinase B/Akt signaling: mechanism for ganglioside-induced apoptosis Wang, X. Q., et al J Biol Chem, 276:44504-11 (2001) 2001	Immunoprecipitation, Immunoblotting (Western)	11577096
Complex formation and cooperation of protein kinase C theta and Akt1/protein kinase B alpha in the NF-kappa B transactivation cascade in Jurkat T cells Bauer, B., et al J Biol Chem, 276:31627-34 (2001) 2001	Kinase Assay	11410591
3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. Alessi, D R, et al. Curr. Biol., 8: 69-81 (1998) 1998		9427642
Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha. Alessi, D R, et al. Curr. Biol., 7: 261-9 (1997) 1997		9094314
Mechanism of activation of protein kinase B by insulin and IGF-1. Alessi, D R, et al. EMBO J., 15: 6541-51 (1996) 1996 Show Abstract Insulin activated endogenous protein kinase B alpha (also known as RAC/Akt kinase) activity 12-fold in L6 myotubes, while after transfection into 293 cells PKBalpha was activated 20- and 50-fold in response to insulin and IGF-1 respectively. In both cells, the activation of PKBalpha was accompanied by its phosphorylation at Thr308 and Ser473 and, like activation, phosphorylation of both of these residues was prevented by the phosphatidylinositol 3-kinase inhibitor wortmannin. Thr308 and/or Ser473 were mutated to Ala or Asp and activities of mutant PKBalpha molecules were analysed after transfection into 293 cells. The activity of wild-type and mutant PKBalpha was also measured in vitro after stoichiometric phosphorylation of Ser473 by MAPKAP kinase-2. These experiments demonstrated that activation of PKBalpha by insulin or insulin-like growth factor-1 (IGF-1) results from phosphorylation of both Thr308 and Ser473, that phosphorylation of both residues is critical to generate a high level of PKBalpha activity and that the phosphorylation of Thr308 in vivo is not dependent on phosphorylation of Ser473 or vice versa. We propose a model whereby PKBalpha becomes phosphorylated and activated in insulin/IGF-1-stimulated cells by an upstream kinase(s).		8978681

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Life Science Research > Proteins and Enzymes > Purified Kinases

Life Science Research > Drug Discovery and Development > Kinase & Phosphatase Screening > Purified Kinases

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