Analytical Data
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Gene name
zapD
- Application
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Alternative Names
zapD；yacF；Cell division Protein ZapD
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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
P36680
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Expression Region
1-247aa
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AA Sequence
MQTQVLFEHPLNEKMRTWLRIEFLIQQLTVNLPIVDHAGALHFFRNVSELLDVFERGEVRTELLKELDRQQRKLQTWIGVPGVDQSRIEALIQQLKAAGSVLISAPRIGQFLREDRLIALVRQRLSIPGGCCSFDLPTLHIWLHLPQAQRDSQVETWIASLNPLTQALTMVLDLIRQSAPFRKQTSLNGFYQDNGGDADLLRLNLSLDSQLYPQISGHKSRFAIRFMPLDTENGQVPERLDFELACC
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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 key protein involved in the regulation of bacterial cell division, specifically in the context of the highly studied model organism Escherichia coli. Research into ZapD has gained traction due to its essential role in mediating the assembly and stability of the divisome, the protein complex that orchestrates cytokinesis. It is known to interact with other crucial proteins such as FtsZ, which is central to the formation of the Z-ring during cell division. The study of ZapD is particularly significant because alterations in its function can lead to abnormal cell division processes, potentially resulting in increased cell size or filamentation, which can have implications for bacterial growth and antibiotic resistance. Furthermore, understanding the biochemical properties and structural dynamics of ZapD could open new avenues for therapeutic interventions against bacterial pathogens, particularly in an era where antibiotic resistance poses a significant challenge. Recent advances in recombinant protein technologies have enabled the production and purification of ZapD for detailed functional and structural analyses, providing insights into its role in the divisome and offering potential targets for drug design. Overall, the study of ZapD not only enhances our basic understanding of bacterial division mechanisms but also paves the way for innovative strategies to combat bacterial infections.
