Analytical Data
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Gene name
RHOQ
- Application
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Alternative Names
ARHQ; RASL7A; TC10; TC10A; Ras-like protein family member 7A
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17081
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Expression Region
Met1~Cys202
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Molecular Weight
52kDa
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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
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Protein Description
RHOQ, a member of the Rho family of GTPases, plays a crucial role in various cellular processes, including cytoskeletal organization, cell migration, and signal transduction. Its dysregulation is associated with several diseases, including cancer and neurological disorders, making it a significant target for therapeutic interventions. The interest in studying RHOQ has surged in recent years due to its potential implications in understanding cellular dynamics and developing targeted treatments. Recombinant RHOQ proteins are pivotal in elucidating the biochemical mechanisms underlying its function, as they allow for detailed investigation of its interactions with other cellular proteins and downstream signaling pathways. This research is often facilitated by various techniques such as X-ray crystallography and NMR spectroscopy, which provide structural insights into RHOQ's conformational states. The development of efficiently expressed and purified recombinant RHOQ proteins has enabled scientists to explore its role in cellular physiology and pathophysiology, paving the way for novel therapeutic strategies. Additionally, the generation of specific antibodies against RHOQ recombinant proteins has enhanced the ability to study its expression patterns and functional consequences in different biological contexts. As researchers continue to delve deeper into the molecular mechanics of RHOQ, its comprehensive characterization through recombinant protein studies will undoubtedly contribute to a better understanding of its regulatory networks and the development of innovative approaches to combat RHOQ-related diseases.
