Analytical Data
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Gene name
dxr
- Application
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Alternative Names
DXP reductoisomerase (1-deoxyxylulose-5-phosphate reductoisomerase) (2-C-methyl-D-erythritol 4-phosphate synthase) () ()
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Species
Escherichia coli
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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
P45568
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Expression Region
1-398aa
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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
Dxr, or 1-deoxy-D-xylulose 5-phosphate reductoisomerase, is a key enzyme in the non-mevalonate pathway of isoprenoid biosynthesis, which is essential for the survival of many pathogenic bacteria, protists, and plant species. Unlike the mevalonate pathway present in mammals, the non-mevalonate pathway is absent in humans, making Dxr a promising target for the development of novel antibiotics and herbicides. The enzyme catalyzes the conversion of 1-deoxy-D-xylulose 5-phosphate to 2-C-methyl-D-erythritol 4-phosphate, playing a crucial role in the production of isoprenoids, which are vital for various biological functions, including cell membrane integrity and energy metabolism. Research on recombinant Dxr proteins has garnered significant interest as it allows for detailed biochemical studies, structural analyses, and the screening of potential inhibitors. The ability to express and purify Dxr in heterologous systems enables scientists to investigate its enzymatic mechanisms and to identify small molecules that could inhibit its activity, thus paving the way for the development of new therapeutic strategies against infectious diseases. Moreover, understanding the structure-function relationship of Dxr can provide insights into designing selective inhibitors with minimal effects on human health. Given the rise of antibiotic-resistant pathogens, the exploration of Dxr as a drug target represents a critical area of research in the quest for effective treatments. By enhancing our understanding of Dxr and its role in isoprenoid biosynthesis, researchers aim to contribute to the discovery of innovative solutions for combating bacterial infections and agricultural challenges.
