Analytical Data
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Gene name
lpxK
- Application
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Alternative Names
Lipid A 4'-kinase
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Species
Escherichia coli
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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
C4ZQ41
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Expression Region
1-328aa
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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
Related Products
Protein Description
LpxK, or 1-Phosphatidyl-D-myo-inositol 4,5-bisphosphate kinase, is an essential enzyme involved in the biosynthesis of lipid A, a critical component of the outer membrane of Gram-negative bacteria. The enzyme phosphorylates lipid precursors, leading to the production of bisphosphorylated lipid A, which is vital for maintaining the structural integrity of the bacterial membrane. Given the role of lipid A in the virulence and pathogenicity of various bacteria, LpxK has emerged as a promising target for the development of novel antimicrobial agents. Research on recombinant LpxK proteins has gained momentum as it enables detailed studies of the enzyme's structure, function, and regulatory mechanisms. Through recombinant protein technologies, researchers can produce LpxK in heterologous systems, allowing for large-scale production and purification of the enzyme for biochemical assays and structural studies. Understanding LpxK's enzymatic activity and its interaction with lipid substrates is crucial for elucidating the biosynthetic pathways of lipid A and potentially identifying inhibitors that could disrupt bacterial membrane integrity. This research not only aids in the fight against antibiotic-resistant bacterial infections but also enhances our overall knowledge of bacterial biochemistry and membrane biology.
