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Key Documents

14-279

Sigma-Aldrich

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

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)

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

Pictograms

Exclamation mark

signalword

Warning

hcodes

Hazard Classifications

Skin Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2


Osvědčení o analýze (COA)

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Navštívit knihovnu dokumentů

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
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
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
Han C Dan et al.
Oncotarget, 7(16), 21064-21075 (2016-03-31)
The ser-thr Akt plays a critical role in the regulation of cell survival, cell growth and proliferation, as well as energy metabolism and is dysregulated in many cancers. The regulation of Akt activity depends on the phosphorylation at two sites:

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