Analytical Data
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Gene name
zapD
- Application
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Alternative Names
(Z ring-associated protein D)
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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
P36680
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Expression Region
1-247aa
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Molecular Weight
35.7 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
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Protein Description
ZapD is a crucial protein involved in bacterial cell division and plays a significant role in the regulation of membrane dynamics. It guides the assembly of the cell division machinery, particularly in the bacterium *Escherichia coli*, where it interacts with other key proteins to ensure proper cytokinesis. Research on ZapD has gained attention due to its unique functions, such as its involvement in the stabilization of the Z-ring, which is essential for separating the daughter cells during division. Proposed mechanisms suggest that ZapD may help in maintaining the structural integrity of the Z-ring by binding to components like FtsZ, thus influencing the spatial distribution of the divisive apparatus. Understanding ZapD's structure and function can offer insights into bacterial growth and division, potentially leading to novel antimicrobial strategies. Furthermore, studies on its recombinant forms can provide valuable information about the protein's interactions, conformational changes, and overall role within the cell cycle. As antibiotic resistance continues to pose a significant challenge in clinical settings, targeting components of the bacterial division process, such as ZapD, presents a promising avenue for developing new therapeutic approaches. These investigations not only enhance our fundamental knowledge of bacterial biology but also pave the way for innovative solutions to combat infectious diseases.
