Analytical Data
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Gene name
yncE
- Application
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Alternative Names
yncE；Uncharacterized Protein YncE
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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
P76116
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Expression Region
31-353aa
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AA Sequence
AEEMLRKAVGKGAYEMAYSQQENALWLATSQSRKLDKGGVVYRLDPVTLEVTQAIHNDLKPFGATINNTTQTLWFGNTVNSAVTAIDAKTGEVKGRLVLDDRKRTEEVRPLQPRELVADDATNTVYISGIGKESVIWVVDGGNIKLKTAIQNTGKMSTGLALDSEGKRLYTTNADGELITIDTADNKILSRKKLLDDGKEHFFINISLDTARQRAFITDSKAAEVLVVDTRNGNILAKVAAPESLAVLFNPARNEAYVTHRQAGKVSVIDAKSYKVVKTFDTPTHPNSLALSADGKTLYVSVKQKSTKQQEATQPDDVIRIAL
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Molecular Weight
36.3 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 study of the yncE recombinant protein is rooted in its potential significance in understanding bacterial physiology and pathogenesis. YncE, a protein found in Escherichia coli, has garnered attention due to its involvement in various cellular processes, including stress response and virulence. As antibiotic resistance becomes a pressing global health issue, unraveling the molecular mechanisms behind bacterial survival strategies has become crucial. Research into yncE aims to characterize its structure, function, and interaction with other cellular components, which may reveal insights into the regulatory networks that sustain bacterial life under adverse conditions. Moreover, examining the roles of such proteins can aid in identifying novel therapeutic targets, contributing to the development of innovative strategies to combat bacterial infections. By utilizing recombinant DNA technology to produce yncE in a controlled environment, scientists can study its properties in detail, paving the way for potential applications in biotechnology and medicine. Overall, the investigation of yncE is not only essential for basic research in microbiology but also holds promise for advancing our approach to tackling antibiotic-resistant pathogens.
