Analytical Data
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Gene name
RHOER0001_5437
- Application
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Alternative Names
/
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Species
Rhodococcus erythropolis SK121
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
C3JU82
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Expression Region
1-390aa
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Molecular Weight
45.6 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
The study of the recombinant protein RHOER0001_5437 has garnered significant interest due to its potential implications in various biological processes and therapeutic applications. This protein, belonging to the family of rhodopsin-like receptors, is hypothesized to play a crucial role in cellular signaling pathways that regulate physiological functions. Given the increasing prevalence of diseases related to receptor dysfunction, understanding the structure and function of RHOER0001_5437 could lead to novel approaches in drug discovery and targeted therapies. Researchers are particularly focused on characterizing its binding properties, signaling mechanisms, and interactions with other biomolecules. Furthermore, exploring the protein's behavior in different cellular environments can provide insights into its biological relevance, which may contribute to unraveling pathways involved in pathological conditions. Overall, the investigation of RHOER0001_5437 not only enhances our understanding of receptor biology but also holds promise for innovative medical interventions.
