• Western blot of Arabidopsis lysate showing specific immunolabeling of the ~53 kDa S6K1 phosphorylated at Thr449 in the first lane (-). Phosphospecificity is shown in the second lane (P) where immunolabeling is blocked by preadsorption with the phosphopeptide used as antigen, but not by the corresponding non-phosphopeptide in the third lane (NP).

Anti-Phospho-S6K1-Thr449 antibody (STJA0003774)

SKU:
STJA0003774-100

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Host: Rabbit
Applications: WB
Reactivity: Arabidopsis
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-Phospho-S6 Kinase 1-Thr449 is suitable for use in Western Blot research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: 100 µl in 10 mM HEPES (pH 7.5) , 150 mM NaCl, 100 µg per ml BSA and 50% Glycerol.
Purification: This antibody was antigen affinity purified from pooled serum.
Dilution Range: WB 1:1000
IHC
ICC
IP
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Immunogen: Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr449 conjugated to KLH.
Background Ribosomal s6 kinase is a member of a family of protein kinases involved in signal transduction. The subfamily S6K has two known homologuesS6K1 and S6K2. First characterized in mammals, S6K1 is controlled by target-of-rapamycin (TOR) kinase, which plays a central regulatory role in growth signaling pathways (Dufner and Thomas 1999). Osmotic stress inhibition of S6K is mediated by the TOR kinase pathway (Mahfouz et al., 2006). The activation of mammalian S6K1 involves phosphorylation at thr389 (Pearson et al., 2005) , however its orthologue in Arabidopsis suggests that plant S6K1 thr449 is its functional equivalent (Schepetilnikov et al., 2011). The phytohormone auxin triggers TOR activation, which is followed by S6K1 phosphorylation at thr449, which in turn is critical for translation reinitiation (Schepetilnikov et al., 2013). Rapamycin effectively inactivates S6K1 thr449 phosphorylation in Arabidopsis seedlings, which suppresses TOR PK activity and ultimately plant growth (Xiong Y and Sheen J, 2011). Western blot of Arabidopsis lysate showing specific 449 immunolabeling of the ~53 kDa S6K1 phosphorylated at Thr in the first lane (-). Phosphospecificity is shown in the second

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