Analytical Data
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Gene name
tmpB
- Application
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Alternative Names
Antigen TmpB
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Species
Treponema phagedenis
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P29720
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Expression Region
22-384aa
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Molecular Weight
47.4 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 research on the tmpB recombinant protein stems from the need to understand and manipulate the functions of specific proteins involved in various biological processes. TmpB, a protein associated with certain bacterial species, has garnered interest due to its potential roles in pathogenicity, signaling pathways, and interactions with host organisms. Investigating tmpB at the molecular level allows scientists to elucidate its structure-function relationship, which is crucial for developing targeted treatments against bacterial infections. Moreover, the production of tmpB as a recombinant protein facilitates the study of its biochemical properties and functional mechanisms in vitro and in vivo. By utilizing techniques such as cloning, expression, and purification, researchers aim to generate sufficient quantities of tmpB for extensive characterization. This work not only contributes to the broader field of microbiology and protein science but also has significant implications for biotechnology, vaccine development, and therapeutic interventions. Understanding tmpB's role in bacterial physiology can pave the way for innovative strategies to combat antibiotic resistance and enhance our arsenal against bacterial diseases.
