Analytical Data
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Gene name
lpxA
- Application
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Alternative Names
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase(UDP-N-acetylglucosamine acyltransferase)(EC 2.3.1.129)
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Species
strain 053442
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A9M3T0
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Expression Region
1-258aa
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Molecular Weight
34.2 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
LPxA is a crucial protein involved in various biological processes, particularly in microbial pathogenesis and host interaction. The focus on LPxA, which is characterized by its distinct LPxA motif, has intensified due to its role in influencing bacterial virulence and immune evasion. Understanding the structure and function of LPxA not only sheds light on microbial behavior but also opens avenues for the development of novel therapeutic strategies against bacterial infections. Researchers are particularly interested in recombinant LPxA proteins, as they allow for detailed studies of the protein's biochemical properties and its interactions with host cells. The ability to produce LPxA in a laboratory setting through recombinant DNA technology enables the elucidation of its functional roles and its potential as a target for vaccine development or antibiotic design. The ongoing research aims to explore LPxA's mechanisms of action and its implications in disease, ultimately contributing to our understanding of host-pathogen dynamics. As a result, LPxA has emerged as a significant subject of study for microbiologists and immunologists, highlighting its potential impact on public health and disease management.
