Analytical Data
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Gene name
entH
- Application
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Alternative Names
entH；C17orf56；ENTHD2；AP-4 complex accessory subunit Tepsin
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Species
Staphylococcus aureus
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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
P0A0M0
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Expression Region
25-241aa
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AA Sequence
EDLHDKSELTDLALANAYGQYNHPFIKENIKSDEISGEKDLIFRNQGDSGNDLRVKFATADLAQKFKNKNVDIYGASFYYKCEKISENISECLYGGTTLNSEKLAQERVIGANVWVDGIQKETELIRTNKKNVTLQELDIKIRKILSDKYKIYYKDSEISKGLIEFDMKTPRDYSFDIYDLKGENDYEIDKIYEDNKTLKSDDISHIDVNLYTKKKV
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Molecular Weight
27.1 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
EntH is a crucial protein in the biosynthesis of enterobactin, a high-affinity iron-chelating siderophore produced by various enteric bacteria, including Escherichia coli. This siderophore plays a significant role in iron acquisition, which is vital for bacterial survival in iron-limited environments, such as those found in the human host. Understanding the function and mechanism of EntH is essential, as it is involved in the modification and maturation of enterobactin, influencing the overall efficiency of iron uptake. The study of EntH can provide insights into bacterial pathogenesis, as iron acquisition is often linked to virulence. Additionally, investigating the structural and functional aspects of EntH may reveal novel targets for antimicrobial drug development, particularly in light of the increasing prevalence of antibiotic-resistant bacteria. Current research focuses on the characterization of EntH through recombinant protein technologies, allowing scientists to study its enzymatic activity, protein-protein interactions, and role in enterobactin biosynthesis in detail. By elucidating the mechanisms by which EntH operates, researchers hope to develop strategies to disrupt its function, thereby limiting bacterial growth and combating infections caused by enteric pathogens. Overall, the study of EntH not only enhances our understanding of microbial physiology but also offers potential avenues for therapeutic intervention in infectious diseases.
