R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Rheb (E1G1R) Rabbit mAb #13879
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 16 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Rheb (E1G1R) Rabbit mAb recognizes endogenous levels of total Rheb protein. This antibody does not cross-react with RhebL1 protein. Bands of unknown origin may be detected at 30 kDa and 50 kDa in some cell lines.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu165 of human Rheb protein.
Background
Ras Homolog Enriched in Brain (Rheb) is an evolutionarily conserved member of the Ras family of small GTP-binding proteins originally found to be rapidly induced by synaptic activity in the hippocampus following seizure (1). While it is expressed at relatively high levels in the brain, Rheb is widely expressed in other tissues and may be induced by growth factor stimulation. Like other Ras family members, Rheb triggers activation of the Raf-MEK-MAPK pathway (2). Biochemical and genetic studies demonstrate that Rheb has an important role in regulating the insulin/TOR signaling pathway (3-6). The mammalian target of rapamycin (mTOR) is a serine/threonine protein kinase that acts as a sensor for ATP and amino acids, balancing the availability of nutrients with translation and cell growth. The tuberin/hamartin (TSC2/TSC1) complex inhibits mTOR activity indirectly by inhibiting Rheb through the tuberin GAP activity (7).
- Yamagata, K. et al. (1994) J Biol Chem 269, 16333-9.
- Yee, W.M. and Worley, P.F. (1997) Mol Cell Biol 17, 921-33.
- Inoki, K. et al. (2003) Genes Dev 17, 1829-34.
- Stocker, H. et al. (2003) Nat Cell Biol 5, 559-65.
- Saucedo, L.J. et al. (2003) Nat Cell Biol 5, 566-71.
- Zhang, Y. et al. (2003) Nat Cell Biol 5, 578-81.
- Li, Y. et al. (2004) Trends Biochem Sci 29, 32-8.
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