Analytical Data
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Gene name
rgy2
- Application
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Alternative Names
(Helicase)(Topoisomerase)
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Species
Aquifex aeolicus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O67226
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Expression Region
1-280aa
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Molecular Weight
39.5 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
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Protein Description
RGY2, also known as a putative regulatory protein, has garnered attention in the field of molecular biology due to its potential role in various biological processes. Research indicates that RGY2 may participate in cellular signaling pathways and may be implicated in stress responses and developmental processes in different organisms. The interest in RGY2 stems from its unique structural features and sequence homology to other known regulatory proteins, suggesting a conserved function across species. Studies have illustrated its involvement in modulating gene expression and protein interactions, which are critical for maintaining cellular homeostasis. Furthermore, in recent years, the exploration of RGY2 has expanded into understanding its therapeutic potential, particularly in the context of diseases where regulatory dysfunctions are evident. Ongoing investigations aim to elucidate the molecular mechanisms behind RGY2's function, providing insights into its role in health and disease, and paving the way for its application in biotechnology and medicine.
