Analytical Data
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Gene name
dhaA
- Application
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Species
Agrobacterium fabrum
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Source
E. coli
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Tag
N- His & C- Myc
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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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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
The study of the dhaA recombinant protein, derived from the bacterium *Pseudomonas fluorescens*, has gained significance due to its potential applications in biocatalysis and industrial processes. The dhaA gene encodes for a dehydratase enzyme that catalyzes the conversion of 1,2-propanediol to acrylate, an important precursor in the production of polymers and specialty chemicals. With the increasing interest in sustainable chemistry, the demand for biotechnological methods to produce acrylate from renewable resources has surged. Its ability to operate under mild conditions and specific substrate selectivity makes the dhaA enzyme an attractive candidate for green chemistry applications. Genetic engineering techniques have enabled the efficient expression of the dhaA protein in various host systems, allowing researchers to investigate its enzymatic properties and optimize reaction conditions. Additionally, understanding the structure-function relationship of dhaA can facilitate the development of more effective enzyme variants through directed evolution approaches. Overall, the research surrounding dhaA recombinant protein not only contributes to the field of enzyme engineering but also plays a crucial role in addressing the environmental challenges posed by traditional petrochemical processes. Through advancements in this area, the potential for creating more sustainable and eco-friendly manufacturing processes is within reach, further emphasizing the importance of ongoing research in this field.
