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100 µl

Ref. YIF-LF-MA0365
AB FRONTIER

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Neuf 331.00 H.T.

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Détails Produit

Product description: Monoclonal Antibody. Recognizes the Human protein. Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol. Mammalian target of rapamycin (mTOR), a serine/threonine kinase involved in diverse cellular processes, including protein translation, mRNA turnover, and protein stability, mediates, at least in part, some of the biological actions of Akt. As a Kinase subunit of both mTORC1 (complex1) and mTORC2 (complex2), mTOR regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation. Kinase subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Growth factor-stimulated mTORC1 activation involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino-acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-421', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Phosphorylates MAF1 leading to attenuation of its RNA polymerase III-repressive function. mTORC2 is also activated by growth. factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.

Alternate Names/Synonyms: mTOR; MTOR; FRAP; EC=2.7.11.1; Rapamycin Target Protein 1; Mammalian Target of Rapamycin; Rapamycin and FKBP12 target 1; Mechanistic Target of Rapamycin; Serine/Threonine-Protein Kinase mTOR

Product Type: Monoclonal Antibody

Clone: 53E11

Isotype: Mouse IgG1 kappa

Immunogen: Recombinant human His-mTOR protein purified from E. coli.

Applications: WB

Species Crossreactivity: Human

Formulation: Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.

Short Term Storage: +4°C

Long Term Storage: -20°C

Shipping: BLUE ICE

Use & Stability: Stable for at least 1 year after receipt when stored at -20°C.

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Literature References: 1) Sukumari-Ramesh S. Et al. (2011) Surg. Neurol. Int. 23;2:22. (General)2) Dufner A. Thomas G. (1999) Exp. Cell Res. 253:100–109. (General)3) Gingras A.C. Et al. (1998) Genes Dev. 12:502–13. (General)4) Mamane Y. Et al. (2006) Oncogene. 25:6416–22. (General)5) Kim D.-H. Et al. (2002) Cell 110:163-175. (General)6) Hara K. Et al. (2002) Cell 110:177-189. (General)7) Kim D.-H. Et al. (2003) Mol. Cell 11:895-904. (General)8) Sarbassov D.D. Et al. (2004) Curr. Biol. 14:1296-1302. (General) 9) Jacinto E. Et al. (2004) Nat. Cell Biol. 6:1122-1128. (General)10) Sarbassov D.D. Et al. (2005) Science 307:1098-1101. (General)11) Garcia-Martinez J.M. Alessi D.R. (2008) Biochem. J. 416:375-385. (General)12) Sancak Y. Et al. (2008) Science 320:1496-1501. (General)