Analytical Data
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Gene name
RHO
- Application
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Alternative Names
OPN2; RP4; Opsin 2; Rod Pigment; Retinitis Pigmentosa 4; Visual Purple
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Species
Mouse
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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
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Expression Region
Met1~Cys110
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Molecular Weight
42kDa
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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
RHO proteins, a subfamily of the Ras superfamily of small GTPases, play a crucial role in regulating various cellular processes, including cytoskeletal dynamics, cell migration, and adhesion. They are involved in the signaling pathways that control cell shape and motility, making them essential for numerous physiological functions and developmental processes. Dysregulation of RHO proteins has been implicated in various diseases, including cancer, where altered signaling can contribute to tumor progression and metastasis. Research on recombinant RHO proteins has become increasingly important as it provides insights into the molecular mechanisms underlying these pathways. By studying RHO proteins in a controlled environment, scientists can better understand their structure-function relationships and interactions with downstream effectors. The production of recombinant RHO proteins allows for detailed biochemical assays and structural studies, facilitating the development of potential therapeutic targets aimed at modulating RHO signaling. Advances in recombinant protein technology, including improved expression systems and purification techniques, have enhanced our ability to study these proteins in vitro and in vivo, offering a deeper understanding of their roles in health and disease. As a result, RHO proteins remain a significant focus of research in cell biology and oncology, pointing to their critical importance in both basic science and therapeutic development.
