Analytical Data
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Gene name
entC1
- Application
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Alternative Names
SEC1
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Species
Staphylococcus aureus
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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
P01553
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Expression Region
28-266aa
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Molecular Weight
43.5 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
EntC1 is a recombinant protein that has garnered attention due to its pivotal role in the biosynthesis of enterobactin, a high-affinity iron chelator produced by various Enterobacteriaceae. This protein is part of a complex pathway that allows bacteria to acquire iron from their environment, a crucial process for growth and pathogenicity. The study of EntC1 is particularly significant in understanding bacterial survival in iron-limited conditions, which is commonly encountered in host organisms. Through the characterization of EntC1, researchers aim to elucidate its enzymatic mechanisms and interactions within the enterobactin synthesis pathway, providing insights into potential therapeutic targets for combating bacterial infections. Moreover, given the increasing prevalence of antibiotic resistance, understanding the molecular underpinnings of iron acquisition can inform the development of novel antimicrobial strategies. As a focus of structural biology, the determination of EntC1's three-dimensional structure through techniques such as X-ray crystallography or NMR spectroscopy can reveal critical active sites and inform structure-based drug design. The implications of EntC1 research extend beyond basic science; insights gained could contribute to the engineering of improved bioindicators for environmental monitoring or the development of iron supplementation therapies. Overall, the study of EntC1 stands at the intersection of microbiology, biochemistry, and pharmacology, illustrating the broad relevance of this recombinant protein in addressing current challenges in microbial pathogenicity and antibiotic resistance.
