Analytical Data
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Gene name
DTD1
- Application
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Alternative Names
DTD1；C20orf88；DUEB；HARS2;D-aminoacyl-tRNA deacylase 1
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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
Q8TEA8
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Expression Region
1-209aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKAVVQR VTRASVTVGG EQISAIGRGI CVLLGISLED TQKELEHMVR KILNLRVFED ESGKHWSKSV MDKQYEILCV SQFTLQCVLK GNKPDFHLAM PTEQAEGFYN SFLEQLRKTY RPELIKDGKF GAYMQVHIQN DGPVTIELES PAPGTATSDP KQLSKLEKQQ QRKEKTRAKG PSESSKERNT PRKEDRSASS GAEGDVSSER EP
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Molecular Weight
26 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 the DTD1 (D-amino acid transferase 1) recombinant protein has gained significant attention due to its pivotal role in the metabolism of D-amino acids, which are non-standard amino acids that occur in various organisms and are involved in numerous biological processes. DTD1 is responsible for catalyzing the transfer of D-amino acids into biological systems, influencing processes such as neurotransmission, cell signaling, and microbial interactions. Understanding the mechanisms underlying DTD1 activity is crucial, as alterations in D-amino acid levels have been linked to several neurodegenerative diseases and metabolic dysfunctions. Through recombinant protein technology, researchers aim to express and purify DTD1, facilitating detailed kinetic studies, structural analysis, and the exploration of its enzymatic properties. This research not only enhances our biochemical understanding of D-amino acid metabolism but also holds potential therapeutic implications for managing diseases associated with D-amino acid dysregulation. Thus, the investigation of DTD1 as a recombinant protein is a promising avenue to unravel the complexities of amino acid metabolism and its implications in health and disease.
