Analytical Data
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Gene name
entB
- Application
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Alternative Names
entB；T-cell-specific surface glycoProtein CD28
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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
P0ADI4
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Expression Region
1-285aa
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AA Sequence
MAIPKLQAYA LPESHDIPQN KVDWAFEPQR AALLIHDMQD YFVSFWGENC PMMEQVIANI AALRDYCKQH NIPVYYTAQP KEQSDEDRAL LNDMWGPGLT RSPEQQKVVD RLTPDADDTV LVKWRYSAFH RSPLEQMLKE SGRNQLIITG VYAHIGCMTT ATDAFMRDIK PFMVADALAD FSRDEHLMSL KYVAGRSGRV VMTEELLPAP IPASKAALRE VILPLLDESD EPFDDDNLID YGLDSVRMMA LAARWRKVHG DIDFVMLAKN PTIDAWWKLL SREVK
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Molecular Weight
32.5 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
EntB is a non-ribosomal peptide synthetase (NRPS) that plays a crucial role in the biosynthesis of the siderophore enterobactin, which is produced by various pathogenic bacteria, including Escherichia coli. Siderophores are high-affinity iron-chelating compounds that enable bacteria to sequester iron from their environment, which is vital for their growth and virulence, particularly in iron-depleted conditions such as those found in host organisms. The study of EntB is significant because understanding its structure and function can provide insights into the mechanisms of iron uptake in pathogenic bacteria, potentially leading to new antimicrobial strategies. Additionally, the reconstitution of EntB as a recombinant protein allows for detailed biochemical and structural characterization, facilitating the elucidation of its enzymatic activity and interactions with other components of the enterobactin biosynthetic pathway. Elucidating the functional properties of recombinant EntB can also aid in the development of inhibitors that target this pathway, providing a novel approach to combating infections caused by enteric pathogens. Given the increasing resistance to conventional antibiotics, research on EntB and its associated biosynthetic mechanisms is vital for identifying new targets for drug development, highlighting the broader implications of this work in the field of microbial pathogenesis and therapeutic innovation.
