Analytical Data
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Gene name
lpxC
- Application
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Alternative Names
lpxC；asmB；envA；UDP-3-O-acyl-N-acetylglucosamine deacetylase
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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
P0A725
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Expression Region
1-305aa
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AA Sequence
MIKQRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVLAKQEAWEYVTFQDDAELPLAFKAPSAVLA
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Molecular Weight
49.8 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
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Protein Description
LPXC is a key enzyme in the bacterial fatty acid synthesis pathway, specifically involved in the biosynthesis of the essential lipid component, mycobacterial cell walls. It catalyzes the conversion of long-chain fatty acids into shorter fatty acyl-CoA derivatives, playing a crucial role in maintaining the integrity and functionality of the bacterial membrane. Given its significance in bacterial physiology and pathogenicity, LPXC has emerged as a target for antibiotic development, particularly against Mycobacterium tuberculosis, the causative agent of tuberculosis. Research on recombinant LPXC has provided insights into its enzymatic mechanisms, structural biology, and potential as an antibiotic target. By producing LPXC as a recombinant protein, scientists can study its biochemical properties in detail, evaluate its interactions with potential inhibitors, and explore its role in bacterial survival under various environmental stresses. Ultimately, LPXC represents a promising candidate for novel therapeutic strategies aimed at combating antibiotic resistance and improving treatment outcomes for bacterial infections.
