Analytical Data
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Gene name
TOP1
- Application
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Alternative Names
TOPI; DNA Topoisomerase 1
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Species
Human
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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
P11387
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Expression Region
Met1~Ser250
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Molecular Weight
38kDa
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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
TOP1, or Topoisomerase I, is a critical enzyme involved in DNA replication, transcription, and repair processes. This enzyme alleviates the torsional strain that builds up ahead of the replication fork by introducing transient single-strand breaks in the DNA helix. The study of TOP1 has gained significant attention due to its role in cellular processes and its implications in cancer biology. Dysregulation or overexpression of TOP1 is often associated with various malignancies, making it a promising target for cancer therapies. Additionally, inhibitors of TOP1, such as camptothecin and its derivatives, have shown potent antitumor activity, thereby highlighting the importance of this protein in drug development. Recent research has focused on elucidating the detailed mechanisms of TOP1 action, its interactions with nucleic acids, and the molecular basis of resistance to TOP1 inhibitors. Understanding these aspects is crucial for designing more effective therapeutic strategies and overcoming resistance mechanisms. Furthermore, advancements in structural biology techniques, including X-ray crystallography and cryo-electron microscopy, have provided valuable insights into the conformational states of TOP1, paving the way for the rational design of novel inhibitors. The ongoing exploration of TOP1 remains essential for enhancing our understanding of its biological functions and improving the efficacy of cancer therapies targeting this pivotal enzyme.
