Analytical Data
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Gene name
dhaA
- Application
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Alternative Names
dhaA；3-hydroxy-D-aspartate aldolase
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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
Q8U671
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Expression Region
1-304aa
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AA Sequence
MKEHRHMTEKSPHSAFGDGAKAYDVPAFGLQIHTVEHGSGAPIVFLHGNPTSSYLWRHIFRRLHGHGRLLAVDLIGYGQSSKPDIEYTLENQQRYVDAWFDALDLRNVTLVLQDYGAAFGLNWASRNPDRVRAVAFFEPVLRNIDSVDLSPEFVTRRAKLRQPGEGEIFVQQENRFLTELFPWFFLTPLAPEDLRQYQTPFPTPHSRKAILAGPRNLPVDGEPASTVAFLEQAVNWLNTSDTPKLLLTFKPGFLLTDAILKWSQVTIRNLEIEAAGAGIHFVQEEQPETIARLLDAWLTRIAGN
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Molecular Weight
41.8 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
DhaA is a key enzyme involved in the metabolism of dimethylsulfoniopropionate (DMSP), a compound found in marine phytoplankton that plays a crucial role in global sulfur cycles and climate regulation. The study of DhaA is particularly relevant in understanding its function in DMSP degradation, which has implications for marine ecology and biogeochemical cycles. Research has shown that DhaA exhibits a unique substrate specificity and catalytic mechanism, making it an interesting target for biochemical studies. Additionally, the recombinant expression of DhaA facilitates the investigation of its properties and functions in a controlled environment, allowing for detailed kinetic and structural analyses. By producing and characterizing recombinant DhaA, researchers aim to uncover the molecular mechanisms underlying its activity, which can lead to broader insights into microbial sulfur metabolism and its environmental impacts. Understanding DhaA's role could also pave the way for biotechnological applications, particularly in the fields of bioremediation and bioengineering, where manipulating sulfur-related pathways can enhance ecosystem health or carbon sequestration processes. Overall, the study of DhaA not only contributes to our knowledge of marine chemistry but also informs potential strategies for addressing climate change challenges.
