14-279
Akt1/PKBα Protein, inactive, 50 g
Unactive, N-terminal His6-tagged recombinant full-length human Akt1, for use in Kinase Assays.
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About This Item
UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.26
Productos recomendados
biological source
human
Quality Level
recombinant
expressed in baculovirus infected Sf21 cells
mol wt
Mw 59 kDa
manufacturer/tradename
Upstate®
technique(s)
activity assay: suitable (kinase)
NCBI accession no.
UniProt accession no.
shipped in
dry ice
General description
N-terminal His6-tagged recombinant full-length human Akt1
Quality
routinely evaluated by phosphorylation of Crosstide
Other Notes
For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
signalword
Warning
hcodes
Hazard Classifications
Skin Sens. 1
Storage Class
10 - Combustible liquids
wgk_germany
WGK 2
Certificados de análisis (COA)
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Jorge Vera et al.
eLife, 4 (2015-11-28)
The PP2A phosphatase is often inactivated in cancer and is considered as a tumour suppressor. A new pathway controlling PP2A activity in mitosis has been recently described. This pathway includes the Greatwall (GWL) kinase and its substrates endosulfines. At mitotic
Hiroshi Senoo et al.
Nature cell biology, 21(7), 867-878 (2019-07-03)
mTORC2 plays critical roles in metabolism, cell survival and actin cytoskeletal dynamics through the phosphorylation of AKT. Despite its importance to biology and medicine, it is unclear how mTORC2-mediated AKT phosphorylation is controlled. Here, we identify an unforeseen principle by
Chia-Chen Chen et al.
Developmental cell, 18(4), 592-604 (2010-04-24)
FoxO transcription factors and TORC1 are conserved downstream effectors of Akt. Here, we unraveled regulatory circuits underlying the interplay between Akt, FoxO, and mTOR. Activated FoxO1 inhibits mTORC1 by TSC2-dependent and TSC2-independent mechanisms. First, FoxO1 induces Sestrin3 (Sesn3) gene expression.
Dos D Sarbassov et al.
Molecular cell, 22(2), 159-168 (2006-04-11)
The drug rapamycin has important uses in oncology, cardiology, and transplantation medicine, but its clinically relevant molecular effects are not understood. When bound to FKBP12, rapamycin interacts with and inhibits the kinase activity of a multiprotein complex composed of mTOR
Stoichiometry of site-specific protein phosphorylation estimated with phosphopeptide-specific antibodies.
Miinea, Cristinel P and Lienhard, Gustav E
Biotechniques, 34, 828-831 (2003)
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