Analytical Data
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Gene name
zipA
- Application
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Alternative Names
zipA; b2412; JW2404; Cell division protein ZipA; FtsZ interacting protein A
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P77173
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Expression Region
1-328aa
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Molecular Weight
52.5 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
ZipA is a critical cell division protein in bacteria, particularly well-studied in Escherichia coli. It plays a significant role in the recruitment and stabilization of the FtsZ protein, which is essential for forming the cytokinetic Z-ring during bacterial cell division. The study of ZipA and its recombinant protein form is paramount because it provides insights into the fundamental mechanisms of bacterial cell division, which has implications for understanding microbial growth and antibiotic resistance. By investigating ZipA, researchers aim to elucidate the molecular interactions and structural characteristics that make it integral to Z-ring assembly. Moreover, exploring ZipA's function and interactions can help in identifying new targets for antibiotic development, especially in the context of increasing resistance to existing drugs. This research not only contributes to our basic understanding of bacterial physiology but also opens avenues for novel therapeutic strategies to combat bacterial infections. Given the rise of multidrug-resistant bacterial strains, targeting essential proteins like ZipA could lead to innovative approaches that disrupt bacterial proliferation, enhancing the efficacy of treatment regimens. Therefore, the recombinant expression and functional characterization of ZipA are essential for advancing our knowledge of bacterial cell division and for the potential development of new antimicrobial agents.
