Analytical Data
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Gene name
DTD2
- Application
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Alternative Names
D-tyrosyl-tRNA deacylase 2
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96FN9
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Expression Region
1-168aa
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Molecular Weight
34.7 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 study of DTD2 (dGTP diphosphate ribosyltransferase 2) recombinant protein has garnered significant interest in the field of molecular biology and biochemistry due to its potential implications in cellular stress responses and nucleotide metabolism. DTD2 is an enzyme that plays a crucial role in maintaining nucleotide pool homeostasis by catalyzing the transfer of ADP-ribose to target proteins, which may regulate various cellular processes, including DNA repair and apoptosis. Dysregulation of DTD2 has been associated with several diseases, including cancer and neurodegenerative disorders, indicating its importance in cellular function and survival. Furthermore, as a member of the ADP-ribosyltransferase family, the understanding of DTD2's structure and function could provide insights into the broader mechanisms of post-translational modifications. The ability to produce recombinant DTD2 protein enables researchers to study its enzymatic activity, identify potential substrates, and explore its interactions with other biomolecules in more detail. This research could pave the way for developing targeted therapies that modulate DTD2 activity, offering new avenues for treating diseases linked to nucleotide metabolism disruptions. Overall, the investigation of DTD2 recombinant protein highlights its essential role in cellular physiology and opens up new possibilities for therapeutic interventions.
