Analytical Data
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Gene name
lpxK
- Application
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Alternative Names
lpxK；Probable tetraacyldisaccharide 4'-kinase. mitochondrial
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Species
E.coli
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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
C4ZQ41
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Expression Region
1-328aa
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AA Sequence
MIEKIWSGESPLWRLLLPLSWLYGLVSGAIRLCYKLKLKRAWRAPVPVVVVGNLTAGGNGKTPVVVWLVEQLQQRGIRVGVVSRGYGGKAESYPLLLSADTTTAQAGDEPVLIYQRTDAPVAVSPVRSDAVKAILAQHPDVQIIVTDDGLQHYRLARNVEIVVIDGVRRFGNGWWLPAGPMRERAGRLKSVDAVIVNGGVPRSGEIPMHLLPGQAVNLRTGTRCDVAQLEHVVAMAGIGHPPRFFATLKMCGVQPEKCVPLADHQSLNHADVSALVSAGQTLVMTEKDAVKCRAFAEENWWYLPVDAQLSGDEPAKLLTQLTLLASGN
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Molecular Weight
43.0 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
LPxK is a significant protein motif recognized for its role in bacterial pathogenesis and virulence, often associated with Lipoproteins and membrane proteins. Research on LPxK recombinant proteins has gained momentum due to their potential applications in vaccine development and immunological studies. The LPxK motif, typically characterized by the presence of leucine (L), proline (P), and lysine (K), serves as a crucial signal for post-translational modifications, impacting the protein's stability and function within bacterial membranes. Many pathogenic bacteria harness the LPxK motif to enhance their survival and evasion of the host immune response. Furthermore, as antibiotic resistance becomes a pressing global issue, understanding the mechanistic roles of LPxK proteins can contribute to the identification of new therapeutic targets. By employing recombinant DNA technology, researchers can produce LPxK proteins in vitro, enabling detailed functional analyses and structural studies. This work not only furthers our comprehension of bacterial virulence mechanisms but also holds promise for the development of innovative strategies to combat infectious diseases. The ongoing exploration into the biochemical properties and interactions of LPxK-containing proteins is expected to reveal insights that could aid in creating more effective vaccines and therapeutics, ultimately addressing the challenges posed by antibiotic resistance and emerging pathogens.
