Analytical Data
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Gene name
RHOQ
- Application
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Alternative Names
RHOQ;ARHQ;RASL7A;TC10;Rho-related GTP-binding Protein RhoQ
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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
P17081
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Expression Region
1-202aa
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AA Sequence
MAHGPGALML KCVVVGDGAV GKTCLLMSYA NDAFPEEYVP TVFDHYAVSV TVGGKQYLLG LYDTAGQEDY DRLRPLSYPM TDVFLICFSV VNPASFQNVK EEWVPELKEY APNVPFLLIG TQIDLRDDPK TLARLNDMKE KPICVEQGQK LAKEIGACCY VECSALTQKG LKTVFDEAII AILTPKKHTV KKRIGSRCIN CC
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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
RHOQ, a member of the Rho GTPase family, plays a crucial role in various cellular processes, including cytoskeletal dynamics, cell migration, and intracellular signaling. Research into RHOQ has gained momentum due to its potential implications in cancer progression and other diseases characterized by aberrant cell behavior. The protein functions as a molecular switch, cycling between an active GTP-bound state and an inactive GDP-bound form, which regulates its interaction with downstream effectors. Investigating RHOQ's signaling pathways and its regulatory mechanisms can provide insights into its role in pathological conditions. The study of recombinant RHOQ proteins is particularly significant because it allows for detailed biochemical and structural analyses, facilitating the understanding of its function and interactions at a molecular level. Researchers employ various methods, such as X-ray crystallography and NMR spectroscopy, to study these proteins, while techniques like pull-down assays and cell-based assays are used to explore their interactions with other cellular components. The exploration of RHOQ's biological functions and its potential as a therapeutic target presents a promising area of study, as modulating its activity could lead to novel strategies for managing diseases driven by dysregulated Rho GTPases. Overall, the research on RHOQ recombinant proteins is pivotal for elucidating the complex network of signaling pathways in which it is involved and providing insights into the molecular underpinnings of various diseases.
