Analytical Data
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Gene name
entE
- Application
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Alternative Names
entE；Ganglioside-induced differentiation-associated Protein 1
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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
P12993
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Expression Region
28-257aa
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AA Sequence
SEEINEKDLRKKSELQRNALSNLRQIYYYNEKAITENKESDDQFLENTLLFKGFFTGHPWYNDLLVDLGSKDATNKYKGKKVDLYGAYYGYQCAGGTPNKTACMYGGVTLHDNNRLTEEKKVPINLWIDGKQTTVPIDKVKTSKKEVTVQELDLQARHYLHGKFGLYNSDSFGGKVQRGLIVFHSSEGSTVSYDLFDAQGQYPDTLLRIYRDNKTINSENLHIDLYLYTT
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Molecular Weight
32.1 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
Related Products
Protein Description
The entE gene encodes a protein involved in the biosynthesis of enterobactin, a high-affinity siderophore produced by many bacteria, particularly in the Enterobacteriaceae family. Enterobactin plays a crucial role in iron acquisition, which is vital for bacterial growth and survival in iron-limited environments, such as the mammalian host. The study of entE and its recombinant protein is significant for understanding microbial pathogenesis and developing new antimicrobial strategies, particularly as iron availability can influence virulence. Researchers have focused on the entE gene due to its potential applications in biotechnology and medicine. By recombinantly expressing and purifying the entE protein, scientists aim to elucidate its structure and function, particularly in relation to enterobactin synthesis. This research could pave the way for novel therapies against bacterial infections, especially those caused by antibiotic-resistant strains. Furthermore, understanding entE protein interactions and mechanisms can offer insights into the fundamental processes of bacterial iron metabolism, highlighting the complexities of microbial life and its adaptations to host environments. The ongoing investigation into entE recombined proteins thus represents a valuable intersection of microbiology, biochemistry, and medical research, with the potential to significantly impact public health and therapeutic approaches.
