Analytical Data
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Gene name
DNTT
- Application
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Alternative Names
DNTT；TDT；DNA nucleotidylexotransferase
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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
P04053
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Expression Region
1-509aa
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AA Sequence
MDPPRASHLSPRKKRPRQTGALMASSPQDIKFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIECIRAGKPVEMTGKHQLVVRRDYSDSTNPGPPKTPPIAVQKISQYACQRRTTLNNCNQIFTDAFDILAENCEFRENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVLNDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVWAFLPDAFVTMTGGFRRGKKMGHDVDFLITSPGSTEDEEQLLQKVMNLWEKKGLLLYYDLVESTFEKLRLPSRKVDALDHFQKCFLIFKLPRQRVDSDQSSWQEGKTWKAIRVDLVLCPYERRAFALLGWTGSRQFERDLRRYATHERKMILDNHALYDKTKRIFLKAESEEEIFAHLGLDYIEPWERNA
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Molecular Weight
62.5kDa
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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
DNTT (deoxynucleotidyl transferase) is an important enzyme involved in nucleotide metabolism, playing a critical role in DNA synthesis and repair processes. Understanding the structure and function of DNTT is essential for elucidating its role in cellular processes, especially in the context of cancer and genetic disorders where nucleotide metabolism may be impaired. Recent studies have focused on the recombinant expression of DNTT to facilitate in-depth biochemical analyses and structure-function studies. The recombinant protein allows researchers to investigate the catalytic mechanisms, substrate specificity, and regulatory pathways associated with DNTT activity. Furthermore, the production of DNTT in a controlled environment enables the development of potential therapeutic applications, such as gene therapy and cancer treatment, where modulation of nucleotide metabolism could improve therapeutic outcomes. Advances in molecular cloning and protein engineering techniques have enabled the optimization of DNTT yield and activity, paving the way for innovative research in this field. By providing insights into the functionality of DNTT and its interaction with other biomolecules, these studies aim to contribute to the broader understanding of nucleotide metabolism in health and disease.
