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MilliporeSigma

S6311

Sigma-Aldrich

Anti-phospho-S6-Kinase (pThr389) antibody produced in rabbit

affinity isolated antibody, buffered aqueous glycerol solution

Sinónimos:

Anti-phospho-p70S6K (pThr389)

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.44

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

mouse, rat, human

technique(s)

western blot (chemiluminescent): 1:1,000 using serum-treated NIH3T3 cell extract, or insulin-treated HeLa, COS, and C6 cell extracts

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

General description

p70 S6 kinase or p70S6K is a protein that belongs to Ser/Thr protein kinase family. It has a crucial role in cell growth and G1 cell cycle progression. It also has a pivotal role in phosphorylating eEF2k at a conserved serine residue and hence regulating the protein synthesis. Rabbit anti-phospho-(p70S6K) antibody can identify p70 S6 kinase and p85 S6 kinase when phosphorylated at (Thr389). Anti-phospho-S6-kinase (pThr389) antibody reacts specifically with p70 S6 kinase of rat, mouse and human. This product can also detect few phosphorylated isoforms of Protein Kinase C when present at high level in cells.

Immunogen

A synthetic phospho-(Thr389) peptide corresponding to residues around (Thr389) of human p70 S6 kinase, coupled to KLH.

Application

Anti-phospho-S6-kinase (pThr389) antibody can be used in western blotting (chemiluminescent) (diluted 1:1000) using serum-treated NIH3T3 cell extract or insulin-treated HeLa, COS, and C6 cell extracts.

Physical form

Solution in 10 mM sodium HEPES, pH 7.5, containing 150 mM sodium chloride, 100 μg/ml bovine serum albumin and 50% glycerol

Disclaimer

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.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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J Chung et al.
Nature, 370(6484), 71-75 (1994-07-07)
Platelet-derived growth factor receptor (PDGF-R) phosphorylation at tyrosines 740/751 and insulin receptor phosphorylation of insulin receptor substrate-1 effects the recruitment and activation of phosphatidylinositol-3-OH kinase (PI(3)K). Changes in PI(3)K activity correlate with cell growth but its downstream signal transducers are
N Pullen et al.
FEBS letters, 410(1), 78-82 (1997-06-23)
The activation of p70s6k is accompanied by a complex series of phosphorylation events. In this review we propose a model of activation which divides p70s6k into four functional modules that cooperate in leading to full enzyme activity. In the light
Diane Evrard et al.
Cancers, 14(18) (2022-09-24)
Mammalian target of rapamycin (mTOR) regulates cellular functions by integrating intracellular signals and signals from the tumor microenvironment (TME). The PI3K-AKT-mTOR pathway is activated in 70% of head and neck squamous cell carcinoma (HNSCC) and associated with poor prognosis. This
X Wang et al.
The EMBO journal, 20(16), 4370-4379 (2001-08-14)
Elongation factor 2 kinase (eEF2k) phosphorylates and inactivates eEF2. Insulin induces dephosphorylation of eEF2 and inactivation of eEF2 kinase, and these effects are blocked by rapamycin, which inhibits the mammalian target of rapamycin, mTOR. However, the signalling mechanisms underlying these
James Yu et al.
PloS one, 6(7), e21415-e21415 (2011-07-14)
We have shown that inhibition of mTOR in granulosa cells and ovarian follicles results in compromised granulosa proliferation and reduced follicle growth. Further analysis here using spontaneously immortalized rat granulosa cells has revealed that mTOR pathway activity is enhanced during

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