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Sigma-Aldrich

Anti-phospho-PRAS40 (Thr246) (Proline-Rich AKT substrate) Antibody

Upstate®, from rabbit

Synonym(s):

40 kDa proline-rich AKT substrate, AKT1 substrate 1 (proline-rich), proline-rich Akt substrate, 40 kDa

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

species reactivity

mouse, human

manufacturer/tradename

Upstate®

technique(s)

western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

phosphorylation (pThr246)

Gene Information

human ... AKT1S1(84335)
mouse ... Akt1S1(67605)

General description

PRAS40 (Proline Rich Akt Substrate, 40 kDa), also known as AKT1S1, is a ubiquitously express protein that is phosphorylated on residue Thr246 via the PI3K/Akt pathway. It was originally discovered as an Akt substrate as it has the putative Akt phosphorylation motif of RxRxxpS/pT2. This phosphorylation allows it to bind 14-3-3 and Raptor of the mTOR complex mTORC1. PRAS40 is known to bind to and regulate mTORC1 (mTOR, Raptor, mLST8) kinases activity that is activated by insulin downstream of PI3K and Akt and subsequently phosphorylates p70S6K and 4EBP1. PRAS40 is known to have a putative TOS motif (FVMDE) that allows it bind to Raptor of mTORC1 in the absence of insulin1. It is thought that through it binding to the Raptor, PRAS40 inhibits the kinase activity of mTORC1 by preventing to bind to its substrates such as p70S6K and 4EBP1.

Specificity

Recognizes phosphorylated PRAS40 (Thr246)), Mr 40 kDa.

Immunogen

Peptide corresponding to amino acid region encompassing the human phospho-PRAS40 (Thr246).

Application

Anti-phospho-PRAS40 (Thr246) (Proline-Rich AKT substrate) Antibody is an antibody against phospho-PRAS40 (Thr246) for use in WB.
Immunoblot Analysis: A 1:1000 dilution of this lot detected phosphorylated PRAS40 (Thr246) in RIPA lysates of unstimulated and PDGF stimulated NIH3T3 cells.

Quality

Routinely evaluated by Western Blot on PDGF stimulated NIH3T3 cell lysates.

Western Blot Analysis:
A 1:1000 dilution of this lot detected phosphorylated PRAS40 (Thr246) in RIPA lysates of unstimulated and PDGF stimulated NIH3T3 cells.

Target description

Approx. 40 kDa

Physical form

Format: Purified
Purified rabbit polyclonal IgG in buffer containing PBS (without Mg2+ and Ca2+), pH 7.3 containing 1.0 mg/mL BSA (IgG, protease free) and 0.05% sodium azide and 50% glycerol.

Analysis Note

Control
PDGF stimulated NIH3T3 cells.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

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

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Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Inositol polyphosphate multikinase is a physiologic PI3-kinase that activates Akt/PKB.
Maag, D; Maxwell, MJ; Hardesty, DA; Boucher, KL; Choudhari, N; Hanno, AG; Ma, JF; Snowman et al.
Proceedings of the National Academy of Sciences of the USA null
Regulation of Akt during torpor in the hibernating ground squirrel, Ictidomys tridecemlineatus.
McMullen DC, Hallenbeck JM
Journal of Comparative Physiology. B, Biochemical, Systemic, and Environmental Physiology null
Paul M Titchenell et al.
Cell metabolism, 23(6), 1154-1166 (2016-05-31)
During insulin-resistant states such as type II diabetes mellitus (T2DM), insulin fails to suppress hepatic glucose production (HGP) yet promotes lipid synthesis. This metabolic state has been termed "selective insulin resistance" to indicate a defect in one arm of the
Noriko Oshiro et al.
The Journal of biological chemistry, 289(5), 2658-2674 (2013-12-18)
Activation of mammalian target of rapamycin complex 1 (mTORC1) by amino acids is mediated in part by the Rag GTPases, which bind the raptor subunit of mTORC1 in an amino acid-stimulated manner and promote mTORC1 interaction with Rheb-GTP, the immediate

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