Analytical Data
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Gene name
dda
- Application
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Alternative Names
dda；C19orf58；PCIA1；DET1- and DDB1-associated Protein 1
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Species
E.coli
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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
P32270
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Expression Region
1-439aa
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AA Sequence
MTFDDLTEGQKNAFNIVMKAIKEKKHHVTINGPAGTGKTTLTKFIIEALISTGGTGIILAAPTHAAKKILSKLSGKEASTIHSILKINPVTYEENVLFEQKEVPDLAKCRVLICDEVSMYDRKLFKILLSTIPPWCTIIGIGDNKQIRPVEPGENTAYISPFFTHKDFYQCELTEVKRSNAPIIDVATDVRNGKWNYDKVVDGHGVRGFTGDTALRDFMVNYFSIVKSLDDLFENRVMAFTNKSVDKLNSIIRKKIFETDKDFIVGEIIVMQEPLFKTYKIDGKPVSEIIFNNGQLVRIIEAEYTSTFVKARGVPGEYLIRHWDLTVETYGDDEYYREKIKIISSDEELYKFNLFLAKTAETYKNWNKGGKAPWSDFWDAKSQFSKVKALPASTFHKAQGMSVDRAFIYTPCIHYADVELAQQLLYVGVTRGRYDVFYV
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Molecular Weight
54.0 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
DDA (Dipeptidyl Aminopeptidase A) is an important enzyme that plays a crucial role in various biological processes, including peptide metabolism and biological signaling. The interest in recombinant DDA proteins has surged due to their potential therapeutic applications and industrial uses. Historically, DDA was primarily studied for its involvement in the renin-angiotensin system, which is critical in regulating blood pressure and fluid balance. Researchers aimed to elucidate the enzyme's structure-function relationship, leading to better understanding of its catalytic mechanisms. With advancements in genetic engineering and protein expression technologies, scientists can produce DDA in a recombinant form, allowing for detailed studies of its properties and activities. This has paved the way for investigating its role in various diseases, including hypertension and heart failure, as well as its potential as a drug target. Moreover, the recombinant DDA proteins offer a more efficient and reliable means for pharmaceutical applications, particularly in drug design and enzyme replacement therapies. The ongoing research focuses on optimizing expression systems, improving purification techniques, and characterizing the enzyme's kinetics to enhance its efficacy and scalability for industrial applications. As the field progresses, the implications of DDA research could extend to novel therapeutic strategies and biotechnological innovations, making it a significant focus in both academic and industrial realms.
