Analytical Data
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Gene name
dxr
- Application
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Alternative Names
dxr；1-deoxy-D-xylulose 5-phosphate reductoisomerase. apicoplastic
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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
P45568
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Expression Region
1-398aa
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AA Sequence
MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS
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Molecular Weight
48.4 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
The research on DXR (deoxyxylulose phosphate reductoisomerase) recombinant proteins is primarily driven by their crucial role in the non-mevalonate pathway of isoprenoid biosynthesis, which is essential in many organisms, including bacteria, algae, and higher plants, but absent in animals. This pathway presents a unique target for antibiotic and herbicide development, as inhibiting DXR can selectively kill pathogenic microbes or weed species without affecting human cells. The recombinant expression of DXR proteins enables researchers to study their structural and functional properties in vitro, facilitating the exploration of their mechanisms and interactions with potential inhibitors. Advances in molecular cloning and protein engineering techniques have allowed for the production of various DXR variants, enhancing our understanding of substrate specificity and catalytic efficiency. Moreover, the characterization of these recombinant proteins can further provide insights into the evolutionary divergence of metabolic pathways among different organisms. As a result, investigating DXR recombinant proteins not only contributes to fundamental biochemical knowledge but also has significant implications for developing novel therapeutic agents in the fight against antibiotic resistance and enhancing agricultural sustainability.
