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- Tel: 858.663.9055
- Email: info@nsjbio.com
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Mechanistic target of rapamycin (mTOR), also known as FRAP1, is a central regulator of cell growth, metabolism, and protein synthesis that integrates signals from growth factors, nutrients, and cellular energy status. Phospho-mTOR (pSer2448) Antibody, clone IFF-13, is designed to detect mTOR phosphorylated at serine 2448, a key regulatory site associated with activation of mTOR signaling and downstream control of translation.
mTOR functions within two distinct complexes, mTORC1 and mTORC2, which regulate different aspects of cellular physiology. Phosphorylation at Ser2448 is commonly associated with mTORC1 activity and reflects signaling downstream of the PI3K-AKT pathway. Activation of mTORC1 promotes protein synthesis through phosphorylation of downstream targets such as ribosomal protein S6 kinase (S6K) and 4E-BP1, leading to increased translation initiation and cellular growth.
Phosphorylation of mTOR at Ser2448 is dynamically regulated by upstream signaling inputs, including growth factor stimulation, cytokine signaling, and nutrient availability. Increased phosphorylation is typically observed in response to mitogenic signals, while inhibition of the pathway, such as through targeted drugs or nutrient deprivation, leads to reduced phosphorylation. Detection of Ser2448 phosphorylation therefore provides a reliable readout of mTOR pathway activation and signaling status.
Unlike total mTOR detection, which reflects overall protein expression, phospho-specific detection at Ser2448 enables assessment of functional activation of the pathway. This distinction is critical in studies of signaling dynamics, drug response, and metabolic regulation, where changes in phosphorylation state are often more informative than total protein levels.
Subcellularly, activated mTOR is localized primarily in the cytoplasm, where it associates with lysosomal membranes and signaling complexes that regulate translation and metabolism. Immunohistochemistry and immunofluorescence studies typically reveal cytoplasmic staining patterns consistent with its role in coordinating growth and biosynthetic processes.
Dysregulation of mTOR signaling is a hallmark of many cancers and metabolic diseases. Hyperactivation of mTOR promotes increased protein synthesis, cell growth, and survival, contributing to tumor progression and therapeutic resistance. As a result, phospho-mTOR is widely used as a biomarker for pathway activation and as a readout for response to mTOR inhibitors and related targeted therapies.
Phospho-mTOR (pSer2448) Antibody, clone IFF-13, enables selective detection of the activated form of mTOR, supporting studies of PI3K-AKT-mTOR signaling, translation control, and cellular growth regulation. Its specificity for Ser2448 phosphorylation makes it a valuable tool for investigating pathway activation and pharmacologic modulation in a wide range of biological systems.
This antibody is part of our full phospho antibody collection which can be explored for additional phosphorylation-specific targets and pathway markers.
Optimal dilution of the Phospho-mTOR (pSer2448) Antibody / mTOR Signaling and Translation Control Marker should be determined by the researcher.
A synthetic peptide specific to the region of human mTOR protein surrounding phosphorylated serine 2448 was used as the immunogen for the Phospho-mTOR (pSer2448) Antibody.
Store the Phospho-mTOR (pSer2448) Antibody at -20oC.
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