Analytical Data
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Gene name
lpxD
- Application
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Alternative Names
UDP-3-O-acylglucosamine N-acyltransferase(EC 2.3.1.-)
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Species
Burkholderia pseudomallei
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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
A3NAT7
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Expression Region
1-361aa
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Molecular Weight
44.2 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 lpxD recombinant protein is rooted in the exploration of lipid A biosynthesis, a crucial component of the outer membrane of Gram-negative bacteria. Lipid A serves as an anchor for lipopolysaccharides (LPS), which are fundamental for bacterial viability, cellular structure, and pathogenicity. LpxD, an enzyme that catalyzes the acylation of glucosamine in lipid A biosynthesis, is essential for the production of biologically active lipid A. Given its pivotal role, LpxD has been identified as a potential target for developing new antibacterial agents, particularly in response to the growing threat of antibiotic resistance. By creating recombinant forms of LpxD, researchers aim to better understand its structure-function relationships and enzymatic mechanisms. This research not only advances our knowledge of bacterial biology but also paves the way for novel therapeutic strategies that could inhibit LPS biosynthesis, thereby helping to combat resistant bacterial infections. Consequently, recombinant LpxD serves as a valuable tool in both fundamental and applied microbiological research.
