Analytical Data
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Gene name
TOP2A
- Application
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Alternative Names
TOP2A; DNA topoisomerase 2-alpha; TOP2; DNA topoisomerase II; alpha isozyme
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11388-1
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Expression Region
S1354-D1473
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Protein Length
Partial
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Molecular Weight
20 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
TOP2A (Topoisomerase II Alpha) is a vital enzyme that manages DNA topology during cellular processes such as replication, transcription, and chromosome segregation. It plays a crucial role in resolving DNA tangles and knots, preventing genomic instability. Dysregulation of TOP2A is implicated in various cancers, making it a significant target for therapeutic interventions. Research has focused on the biochemical and structural characterization of TOP2A to understand its mechanism of action and interaction with DNA and inhibitors. Notably, the development of TOP2A-targeting chemotherapeutic agents, such as etoposide and doxorubicin, underscores the enzyme's importance in oncology. Understanding the structure-function relationship of TOP2A through recombinant protein studies has provided insights into its catalytic mechanisms and the effects of mutations that may confer drug resistance. Furthermore, the elucidation of TOP2A's role in cell cycle regulation and its interactions with other proteins involved in DNA damage response has opened new avenues for targeted cancer therapies. The continued exploration of TOP2A's complex biology and its implications in disease progression is critical for developing innovative strategies to combat cancer and improve patient outcomes.
