Analytical Data
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Gene name
ccdA
- Application
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Alternative Names
(Protein LetA)
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Species
Escherichia coli
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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
Q46995
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Expression Region
1-72aa
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Molecular Weight
15.6 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 recombinant ccdA protein is essential in understanding its role in bacterial cell division and the maintenance of plasmids. ccdA, often found in conjunction with the ccdB gene, functions as part of a toxin-antitoxin system critical for stabilizing plasmids within bacterial populations. When expressed, ccdB acts as a potent toxin, while ccdA serves to neutralize this toxicity, allowing the bacteria carrying the plasmid to survive under stressful conditions. The intricate balance between these two proteins ensures that plasmid-bearing cells can maintain their genetic material. Researchers have focused on characterizing the ccdA protein to explore its structure, function, and the mechanisms by which it protects bacterial cells. Additionally, understanding the interactions between ccdA and ccdB could provide insights into designing novel antibacterial strategies, as targeting such systems may disrupt plasmid maintenance. As resistance to antibiotics continues to rise, exploiting the intricacies of toxin-antitoxin systems like that of ccdA-ccdb becomes increasingly relevant, offering potential pathways for developing new therapeutics or improving existing antimicrobial treatments. This research not only enhances our knowledge of bacterial physiology but also has significant implications for biotechnology and medicine, highlighting the importance of recombinant protein studies in addressing contemporary challenges in microbial resistance.
