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Merck
CN

14-279

Akt1/PKBα蛋白(失活,50 g)

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

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UNSPSC Code:
12352202
NACRES:
NA.26
eCl@ss:
32160405
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产品名称

Akt1/PKBα蛋白(失活,50 g), Unactive, N-terminal His6-tagged recombinant full-length human Akt1, for use in Kinase Assays.

biological source

human

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

Quality Level

Analysis Note

通过Crosstide 的磷酸化进行常规评估。

General description

N末端带有His6标签的重组全长人Akt1

Other Notes

比活相关数据,请参阅检验报告以获取该酶的单独批次。

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

pictograms

Exclamation mark

signalword

Warning

hcodes

Hazard Classifications

Skin Sens. 1

存储类别

10 - Combustible liquids

wgk

WGK 2


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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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