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Documentos Principais

07-888

Sigma-Aldrich

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

Upstate®, from rabbit

Sinônimo(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

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

fonte biológica

rabbit

Nível de qualidade

forma do anticorpo

affinity purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

reatividade de espécies

mouse, human

fabricante/nome comercial

Upstate®

técnica(s)

western blot: suitable

Isotipo

IgG

nº de adesão NCBI

nº de adesão UniProt

Condições de expedição

dry ice

modificação pós-traducional do alvo

phosphorylation (pThr246)

Informações sobre genes

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

Descrição geral

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.

Especificidade

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

Imunogênio

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

Aplicação

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.

Qualidade

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.

Descrição-alvo

Approx. 40 kDa

forma física

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.

Nota de análise

Control
PDGF stimulated NIH3T3 cells.

Outras notas

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

Informações legais

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

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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 2


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “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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