Analytical Data
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Gene name
tsaE
- Application
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Alternative Names
tsaE；yjeE；tRNA threonylcarbamoyladenosine biosynthesis Protein TsaE
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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
P0AF67
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Expression Region
1-153aa
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AA Sequence
MMNRVIPLPDEQATLDLGERVAKACDGATVIYLYGDLGAGKTTFSRGFLQALGHQGNVKSPTYTLVEPYTLDNLMVYHFDLYRLADPEELEFMGIRDYFANDAICLVEWPQQGTGVLPDPDVEIHIDYQAQGREARVSAVSSAGELLLARLAG
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Molecular Weight
16.9 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 tsaE recombinant protein has garnered significant attention due to its potential implications in microbial pathogenesis and immune response. TsaE, a protein encoded by the *Neisseria meningitidis* gene, plays a crucial role in the bacterium's survival and virulence. As a component of the outer membrane, TsaE is involved in various physiological processes, including nutrient uptake and the interaction with the host's immune system. Researchers have focused on recombinant expression systems to produce TsaE in a controlled environment, allowing for the investigation of its structure and function. The ability to isolate and characterize this protein will enhance our understanding of bacterial pathogenesis and could contribute to the development of novel vaccines or therapeutics against meningococcal infections. Moreover, understanding the immune response elicited by TsaE could provide insights into how the body recognizes and responds to bacterial infections. The exploration of tsaE also intersects with broader themes in microbiology and immunology, making it a valuable target for research aimed at addressing public health challenges posed by infectious diseases.
