Mammalian target of Rapamycin
Rapamycin and analogs are promising anticancer agents currently under clinical trials. When rapamycin complexed with FKBP12, rapamycin binds to and inhibits the target of rapamycin (TOR) protein, a 289-kDa phosphatidylinositide 3-kinase–related kinase (PIKK). The mammalian Target Of Rapamycin (mTOR) is a nutrient-sensing protein kinase that regulates numerous cellular processes including cell cycle progression, DNA recombination/DNA damage detection and chondrocyte differentiation along the bone growth in several species (1). The mTOR is composed of 20 in tandem repeats-HEAT which are implicated in protein–protein interactions. The mTOR protein consists of several functional domains including a carboxy terminal FAT domain, FBR domain, a kinase domain and a FATC domain. FATC domain is essential for mTOR activity and site directed mutagenesis of a single amino acid in the FATC domain results in complete loss of mTOR activity. MTOR undergoes auto phosphorylation via its intrinsic serine/threonine kinase activity and upon activation it regulates protein synthesis through phosphorylation and activation of repressor of mRNA translation 4E-BP1 and via phosphorylation and activation of S6 kinase. A regulatory associated protein of TOR (RAPTOR), PI3 kinase and ATK kinase are all known positive regulators of mTOR.
mTOR has significant homology to S. cerevisiae protein TOR1, in rat mTOR is a 289 kDa protein which has been shown to interact with immunophilin FKBP12 in a rapamycin-dependent manner. The Rapamycin-FKBP12 complex is known to inhibit progression through G1 cell cycle stage by interfering with mitogenic signaling pathways. Mammalian target of rapamycin (mTOR) forms two complexes, mTORC1 and mTORC2, that play central roles in cell growth and functions. Only mTORC1 is directly inhibited by the immunosuppressive drug rapamycin. A large portion of mTOR is localized to the endoplasmic reticulum and Golgi in many common cells (1). The mTOR targeting important for its function and the targeting is directed by HEAT repeats and the two intervening interunit spaces (2).
The mTOR-selective antibody was generated against a peptide from the tyrosine kinase domain that is unique to mTOR protein. The affinity purified mono epitope-specific rabbit polyclonal antibody strongly labels a 250-290kDa protein of mTOR in PC-mTOR western blot positive western blot positive controls. FabGennix Inc. will conjugate this and other antibodies from its catalog to either secondary enzymes (alk-Pase or HRP) or fluorescent probes at a nominal cost upon request. FabGennix also provides custom antibody production services for researchers that are looking for high affinity mono and polylconal antibodies in various species. We specialize in making application specific antibodies that are useful in IHC, confocal and other applications where native antigen is detected. For a complete listing of all FabGennix antibodies please visit www.Fabgennix.com.
For research use only, not for diagnostic or therapeutic use.
Data Sheets
MSDS
General Information
Citations
Search FabGennix Product Citation Data Base
Search

