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Key Documents

SAB4200312

Sigma-Aldrich

Anti-PRAS40 (C-terminal) antibody produced in rabbit

~1.5 mg/mL, affinity isolated antibody

Synonym(s):

Anti-AKT1S1

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.44

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~40 kDa

species reactivity

mouse, human, rat

concentration

~1.5 mg/mL

technique(s)

immunohistochemistry: 5-10 μg/mL using formalin-fixed, paraffin-embedded human breast carcinoma.
immunoprecipitation (IP): 5-10 μg using extracts of HEK-293T cells.
indirect immunofluorescence: 8-16 μg/mL using PC12 cells.
western blot: 1.5-3.0 μg/mL using NIH3T3 cell extracts.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

Proline-rich Akt-substrate of 40 kDa (PRAS40) is a raptor binding protein. PRAS40 contains a target of rapamycin (TOR) signaling (TOS) motif.

Specificity

Anti-PRAS40 (C-terminal) antibody is specific for human, mouse and rat PRAS40. In Immunoblotting, detection of the PRAS40 band is specifically inhibited by the PRAS40 immunizing peptide.

Immunogen

synthetic peptide corresponding to a sequence at the C-terminus of human PRAS40, conjugated to KLH. The corresponding sequence is identical in mouse and rat PRAS40.

Application

Anti-PRAS40 (C-terminal) antibody is suitable for use in western blot (1.5-3.0 μg/mL using NIH3T3 cell extracts) and indirect immunofluorescence (8-16 μg/mL using PC12 cells). The product may also be used for immunoprecipitation (5-10 μg using extracts of HEK-293T cells) and immunohistochemistry (5-10 μg/mL using formalin-fixed, paraffin-embedded human breast carcinoma tissues).

Biochem/physiol Actions

Proline-rich Akt-substrate of 40 kDa (PRAS40) inhibits mammalian target of rapamycin complex 1(mTORC1) kinase activity. It is involved in the PI3KAkt/protein kinase B (PKB) survival pathway. Phosphorylation of PRAS40 by Akt and mTORC1 disrupts the binding between mTORC1 and PRAS40 and relieves the inhibitory effect of PRAS40 on mTORC1 activity. The binding of PRAS40 to 14-3-3 requires amino acids and insulin, which is partially inhibited by rapamycin. PRAS40 is a component of the mTORC1 protein complex, which inhibits cell growth in insulin deprived cells. Furthermore, during nutrient or serum deprivation, PRAS40 binds mammalian target of rapamycin (mTOR) and inhibits insulin-stimulated mTOR signaling. PRAS40 activation has also been implicated in pulmonary and breast carcinogenesis. Thus, PRAS40 may be considered as a target protein for treating insulin resistance and various cancers.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

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

flash_point_f

Not applicable

flash_point_c

Not applicable


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Mammalian target of rapamycin complex 1: signalling inputs, substrates and feedback mechanisms
Dunlop EA and Tee AR
Cellular Signalling, 21(6), 827-835 (2009)
Bei Huang et al.
Acta pharmacologica Sinica, 26(10), 1253-1258 (2005-09-22)
To study the expression of proline-rich Akt-substrate PRAS40 in the cell survival pathway and tumor progression. The effects of three key kinase inhibitors on PRAS40 activity in the cell survival pathway, serum withdrawal, H(2)O(2) and overexpression of Akt were tested.
Yasemin Sancak et al.
Molecular cell, 25(6), 903-915 (2007-03-28)
The heterotrimeric mTORC1 protein kinase nucleates a signaling network that promotes cell growth in response to insulin and becomes constitutively active in cells missing the TSC1 or TSC2 tumor suppressors. Insulin stimulates the phosphorylation of S6K1, an mTORC1 substrate, but

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