Analytical Data
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Gene name
rgy2
- Application
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Alternative Names
rgy2；topR-2；Reverse gyrase 2
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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
O67226
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Expression Region
1-280aa
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AA Sequence
MALELIERGCPNCGGVISSDRLEKGLPCSKCLPKPTEEKVCDALEELKTLKYLKPFCDTDKSLERFINFFEKAVGAKPWSLQRVWAKRVFMNQSFAIVAPTGVGKTTFGLVMSLFLKGRVLAIFPTRLLAQQAGDRLSELAQKVGVNKKILIYQSKKNIREQFLNGDWDILLGTNMFLHKNFENLINFKFKLIFIDDIDSFLKRGKNVDYLFKLLGFSGEEIKLALKENKTQRDYDRLARIRKRKRDTVLIVSSATLKPRGKRAYLFRNLLGFDVQKAIT
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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
Related Products
Protein Description
The research on the rgy2 recombinant protein has gained significant attention due to its potential applications in various fields such as biotechnology, medicine, and agriculture. The rgy2 gene, derived from a specific organism or cell line, encodes a protein that is hypothesized to have unique biochemical properties or functionalities. Initial studies have suggested that rgy2 may play a crucial role in metabolic processes, cellular signaling, or stress response mechanisms. Understanding the structural and functional characteristics of the rgy2 protein is essential for elucidating its biological role and exploring its applications. Recombinant protein technology enables the production of rgy2 in large quantities, facilitating detailed analyses and assays. Researchers are particularly interested in its potential as a therapeutic agent, given its possible involvement in disease pathways. Furthermore, due to its properties, the rgy2 protein might be useful in crop improvement strategies, enhancing resistance to environmental stresses or increasing yield. Ongoing studies are focusing on optimizing expression systems, characterizing the protein's structure-function relationship, and determining its effects in specific biological contexts. This line of research not only deepens our understanding of rgy2's biological significance but also opens avenues for innovative solutions in health and agriculture. The significance of the rgy2 recombinant protein research is underscored by its implications for enhancing human health and improving food security in a rapidly changing world.
