Analytical Data
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Gene name
lpxD
- Application
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Alternative Names
lpxD；UDP-3-O-acylglucosamine N-acyltransferase
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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
P0CD76
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Expression Region
1-354aa
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AA Sequence
MSQSTYSLEQLADFLKVEFQGNGATLLSGVEEIEEAKTAHITFLDNEKYAKHLKSSEAGAIIISRTQFQKYRDLNKNFLITSESPSLVFQKCLELFITPVDSGFPGIHPTAVIHPTAIIEDHVCIEPYAVVCQHAHVGSACHIGSGSVIGAYSTVGEHSYIHPRVVIRERVSIGKRVIIQPGAVIGSCGFGYVTSAFGQHKHLKHLGKVIIEDDVEIGANTTIDRGRFKHSVVREGSKIDNLVQIAHQVEVGQHSMIVAQAGIAGSTKIGNHVIIGGQAGITGHICIADHVIMMAQTGVTKSITSPGIYGGAPARPYQEIHRQVAKVRNLPRLEERIAALEKLVQKLEALSEQH
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Molecular Weight
38.4 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
Related Products
Protein Description
LpxD is a crucial enzyme in the biosynthesis of lipid A, an essential component of the outer membrane of Gram-negative bacteria. It catalyzes the transfer of acyl groups to UDP-GlcNAc, leading to the formation of the lipid A precursor. Given the importance of lipid A in maintaining bacterial integrity and serving as a target for the host immune system, LpxD has gained attention as a potential target for novel antibiotics. With the rise of antibiotic-resistant bacteria, understanding the structure and function of LpxD is vital for developing new therapeutic strategies. Researchers have focused on recombinant expression of LpxD to study its enzymatic activity and structure, allowing for the exploration of its mechanism and the identification of inhibitory compounds. Furthermore, structural studies through techniques like X-ray crystallography and cryo-electron microscopy have provided insights into the enzyme's active site and substrate interactions, paving the way for structure-based drug design. Overall, the study of recombinant LpxD not only enriches our understanding of bacterial lipid biosynthesis but also opens new avenues for combating antibiotic resistance through innovative antibiotic development.
