Analytical Data
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Gene name
Dit
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简介
The Dit protein is an important component that forms a 40 Å wide channel distal to the tail in its homohexameric structure. This unique channel structure plays a crucial role in cellular processes and may facilitate DNA ejection. Dit Protein, Bacillus phage SPP1 is the recombinant Dit protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
Distal tail protein; Dit; Gene product 19.1; Gp19.1
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O48459
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Expression Region
N2-V141
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Protein Length
Partial
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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
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Protein Description
The Dit (Dual Inhibition Target) protein has emerged as a significant focus of research in the fields of molecular biology and biochemistry due to its unique structural properties and functional versatility. Initially discovered in certain bacterial species, Dit plays a critical role in regulating cellular responses to stress and mediating adaptive mechanisms. Its dual inhibition function allows it to simultaneously modulate multiple signaling pathways, thereby influencing various biological processes, including cell proliferation, apoptosis, and immune responses. As researchers delve deeper into the molecular mechanisms of Dit, there is growing interest in its potential applications in developing therapeutic interventions for diseases characterized by dysregulated signaling, such as cancer and autoimmune disorders. Furthermore, the protein's ability to interact with key regulatory molecules offers insights into novel drug design strategies. Current studies aim to elucidate the structural characteristics of Dit and map its interaction networks, fostering a better understanding of its role within cellular contexts. The ongoing exploration of Dit not only enhances our comprehension of fundamental biological processes but also paves the way for innovative approaches in targeting complex diseases.
