Analytical Data
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Gene name
TDP2
- Application
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Alternative Names
TDP2；EAP2；；Tyrosyl-DNA phosphodiesterase 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
O95551
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Expression Region
1-362aa
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AA Sequence
MELGSCLEGGREAAEEEGEPEVKKRRLLCVEFASVASCDAAVAQCFLAEN DWEMERALNSYFEPPVEESALERRPETISEPKTYVDLTNEETTDSTTSKI SPSEDTQQENGSMFSLITWNIDGLDLNNLSERARGVCSYLALYSPDVIFL QEVIPPYYSYLKKRSSNYEIITGHEEGYFTAIMLKKSRVKLKSQEIIPFP STKMMRNLLCVHVNVSGNELCLMTSHLESTRGHAAERMNQLKMVLKKMQE APESATVIFAGDTNLRDREVTRCGGLPNNIVDVWEFLGKPKHCQYTWDTQ MNSNLGITAACKLRFDRIFFRAAAEEGHIIPRSLDLLGLEKLDCGRFPSD HWGLLCNLDIIL
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Molecular Weight
67 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
TDP2 (tyrosyl-DNA phosphodiesterase 2) is a crucial enzyme involved in the repair of DNA double-strand breaks caused by topoisomerase II (Top2) activity. The mechanism by which Top2 creates transient breaks in DNA is vital for processes such as DNA replication and transcription; however, when these breaks fail to complete correctly, they can lead to genomic instability, contributing to various diseases, including cancer. TDP2 specifically recognizes and resolves the toxic adducts formed when topoisomerase II covalently binds to the ends of DNA breaks. Dysfunction in TDP2 has been linked to therapeutic resistance in cancers treated with topoisomerase inhibitors, making it an essential target for cancer research. Understanding TDP2's structure and function could provide insights into developing novel therapeutic strategies to enhance the effectiveness of existing chemotherapy regimens. Recent advancements in structural biology techniques, including X-ray crystallography and cryo-electron microscopy, have enabled researchers to elucidate the detailed molecular mechanisms of TDP2 activity, paving the way for targeted drug design. As such, TDP2 not only plays a significant role in maintaining genomic integrity but also represents a potential biomarker and therapeutic target in oncology, highlighting the importance of ongoing research in this area.
