Analytical Data
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Gene name
RheB
- Application
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Alternative Names
RHEB;RHEB2;GTP-binding Protein Rheb
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15382
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Expression Region
1-181aa
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AA Sequence
MPQSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSYDPTIENTFTKLITVN GQEYHLQLVDTAGQDEYSIFPQTYSIDINGYILVYSVTSIKSFEVIKVIH GKLLDMVGKVQIPIMLVGNKKDLHMERVISYEEGKALAESWNAAFLESSA KENQTAVDVFRRIILEAEKMDGAASQGKSSC
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Molecular Weight
23 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
RheB, a member of the Ras superfamily of GTPases, plays a crucial role in cellular signaling and regulation, particularly in the context of bacterial pathogenesis and cellular proliferation. The study of RheB is significant due to its involvement in various biological processes, including the regulation of gene expression, cell cycle control, and response to environmental stresses. Researchers have recognized that understanding the structure and function of RheB can provide insights into its mechanism of action, particularly how it interacts with other proteins and cellular components. This is particularly relevant given the role of GTPases in signaling pathways that malfunction in diseases such as cancer. The development of recombinant RheB proteins has facilitated advanced studies, allowing for the exploration of its biochemical properties, interaction networks, and potential as a therapeutic target. Additionally, the manipulation of RheB in model organisms has provided valuable information regarding its physiological roles and its contribution to virulence in pathogenic bacteria. Overall, the exploration of RheB as a recombinant protein extends our understanding of GTPase functions and opens the door for innovative approaches in drug design and therapeutic development against diseases linked to GTPase dysregulation.
