Analytical Data
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Gene name
hldE
- Application
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Alternative Names
Including the following 2 domains: D-beta-D-heptose 7-phosphate kinase (EC:2.7.1.167) Alternative name(s): D-beta-D-heptose 7-phosphotransferase D-glycero-beta-D-manno-heptose-7-phosphate kinase D-beta-D-heptose 1-phosphate adenylyltransferase (EC:2.7.7.70) Alternative name(s): D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P76658
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Expression Region
1-477aa
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Molecular Weight
67.1 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
The hldE gene, a crucial component of the bacterial cellular machinery, encodes for an enzyme involved in the biosynthesis of specific metabolites, which play significant roles in bacterial physiology and pathogenesis. Recent studies have highlighted the importance of hldE in the context of bacterial virulence and biofilm formation, making it a potential target for novel antimicrobial strategies. Researchers have been particularly interested in producing recombinant hldE protein to elucidate its structural and functional properties. This recombinant protein can provide insights into the enzyme's catalytic mechanisms and interactions with other cellular components, thereby aiding in the understanding of its role in pathogenic bacteria. Furthermore, characterizing hldE and its protein product can facilitate the development of inhibitors that disrupt its function, offering new avenues for treating bacterial infections. The exploration of hldE also opens up possibilities for leveraging its enzymatic activity in biotechnological applications, such as the development of biosensors or biotransformation processes. Understanding the intricacies of hldE presents a significant opportunity for both basic research and applied sciences, illustrating the interdisciplinary nature of contemporary microbiological research.
