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PRAS40 (Thr356) Antibody

Product Specifications

Background

PRAS40 (proline-rich Akt/PKB substrate of 40 kDa) acts at the intersection of the Akt- and mTOR-mediated signaling pathways and its phosphorylation by Akt and by mTORC1 results in dissociation of PRAS40 from mTORC1 which may relieve an inhibitory constraint on mTORC1 activity (Wiza et al., 2012) . Phosphorylation of PRAS40 by Akt and association with 14-3-3 has also been indicated to be crucial for insulin to stimulate mTOR. (Vander Haar et al., 2007) . The primary function of PRAS40 in vivo in Drosophila has been shown to regulate TORC1 activity, and not to act as a downstream target and effector of TORC1 (Pallares et al., 2012) .

Synonyms

40 kDa proline rich AKT substrate antibody, 40 kDa proline-rich AKT substrate antibody, AKT1 S1 antibody, AKT1 substrate 1 (proline rich) antibody, AKT1 substrate 1 antibody, AKT1S 1 antibody, AKT1S1 antibody, AKTS1_HUMAN antibody, Lobe antibody, MGC2865 antibody, PRAS 40 antibody, PRAS antibody, PRAS40 antibody, Proline rich akt substrate antibody, Proline rich Akt substrate 40 kDa antibody, Proline-rich AKT1 substrate 1 antibody

Swiss Prot

Q7JXA2

Modification Site

Thr356

Host

Rabbit

Cross Reactivity

Drosophila

Target

PRAS40 (Thr356)

Clonality

Polyclonal

Isotype

IgG

Conjugation

Unconjugated

Source

Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr356 of Drosophila PRAS40, conjugated to keyhole limpet hemocyanin (KLH) .

Applications

WB

Purification

Antigen Affinity purification from Pooled whole antiserum

Concentration

Lot Dependent

Dilution

WB (1:300-5000)

Buffer

10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.

Modification

Phosphorylation

Storage Conditions

Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

Specificity

Specific for endogenous levels of the ~60 kDa PRAS40 protein phosphorylated at Thr356. The immunolabeling is completely eliminated by treatment with λ-phosphatase.
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