protein

RHEB Protein, Human (GST)

HY-P71260

10 μg

160 USD

RHEB Protein, Human (GST)

proteins

E. coli

10 μg

160 USD

RHEB is an important small GTPase that acts as an allosteric activator of the mTORC1 complex, a key nutrient sensor that controls cell growth and biomass production. In response to signals such as nutrients and growth factors, RHEB activates the MTOR kinase within mTORC1 by inducing conformational changes. RHEB Protein, Human (GST) is the recombinant human-derived RHEB protein, expressed by E. coli , with N-GST labeled tag. The total length of RHEB Protein, Human (GST) is 184 a.a., with molecular weight of ~45.0 kDa.

Human

RHEB, a small GTPase, functions as a crucial allosteric activator of the canonical mTORC1 complex, a pivotal nutrient sensor orchestrating cellular biomass generation and growth. In response to cues such as nutrients, growth factors, or amino acids, RHEB plays a specific role in activating the protein kinase activity of MTOR within the mTORC1 complex. This activation is achieved through inducing a conformational change that aligns residues in the active site of MTOR, thereby enhancing the phosphorylation of key downstream effectors like ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1). Additionally, RHEB is essential for the localization of the TSC-TBC complex to lysosomal membranes, providing spatial regulation to mTORC1 activity. Conversely, during starvation, the TSC-TBC complex inactivates RHEB, preventing mTORC1 activation and contributing to cellular adaptation under nutrient-deprived conditions. Notably, RHEB exhibits low intrinsic GTPase activity, further emphasizing its role in dynamically regulating mTORC1 signaling.

GTP-Binding Protein Rheb; Ras Homolog Enriched in Brain; RHEB; RHEB2

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 8% Trehalose, 4% Mannitol, 50 mM NaCl, 10 mM GSH, 0.05% Tween 80, pH 6.5.

Room temperature in continental US; may vary elsewhere.