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Render Timestamp: 2024-12-20T12:18:21.536Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-20 06:14:21.120
Product last modified at: 2024-06-27T13:36:10.090Z
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PDP - Template Name: Blocking Peptide
PDP - Template ID: *******6db2f4c

Phospho-mTOR (Ser2448) Blocking Peptide #1230

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Important Ordering Details

Custom Ordering Details: This product is assembled upon order. Please allow two-four weeks for your product to be processed.

    Product Information

    Product Usage Information

    Use as a blocking reagent to evaluate the specificity of antibody reactivity in dot blot protocols.

    Storage

    Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA, 5% glycerol and 1% DMSO. Store at –20°C.

    Product Description

    This peptide is used to specifically block #2971 Phospho-mTOR (Ser2448) Antibody reactivity.

    Quality Control

    The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide reacts with #2971 Phospho-mTOR (Ser2448) Antibody in dot blot.

    Background

    The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).
    No product specific background information is currently available for this product.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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