Analytical Data
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Gene name
zapA
- Application
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Alternative Names
zapA；ygfE；Cell division Protein ZapA
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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
P0ADS2
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Expression Region
1-109aa
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AA Sequence
MSAQPVDIQI FGRSLRVNCP PDQRDALNQA ADDLNQRLQD LKERTRVTNT EQLVFIAALN ISYELAQEKA KTRDYAASME QRIRMLQQTI EQALLEQGRI TEKTNQNFE
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Molecular Weight
12.5 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
ZapA is a crucial protein involved in bacterial cell division, particularly in Escherichia coli. It plays a vital role in the dynamic assembly of the septal ring, which is essential for proper cytokinesis. The protein is known to localize to the Z-ring during the early stages of cell division, where it interacts with other key division proteins, such as FtsZ and FtsA, to facilitate the constriction process. Given its significant role in bacterial proliferation, ZapA has garnered attention as a potential target for antibiotic development. As antibiotic resistance becomes an increasingly pressing global health issue, understanding the structural and functional characteristics of ZapA can provide insights into novel therapeutic strategies. Researchers have focused on the recombinant expression and purification of ZapA to study its biophysical properties, interaction partners, and the mechanisms by which it contributes to cell division. By utilizing techniques such as X-ray crystallography and cryo-electron microscopy, scientists aim to elucidate the molecular details of ZapA's function and its assembly dynamics. This research not only enhances our fundamental understanding of bacterial cell division but also opens avenues for the design of new antimicrobial agents that specifically disrupt the function of ZapA and other related proteins in pathogenic bacteria.
