Analytical Data
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Gene name
zipA
- Application
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Alternative Names
zipA；Cell division Protein ZipA
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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
P77173
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Expression Region
1-328aa
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AA Sequence
MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREYQDIIREVKDANA
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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
The study of the ZipA protein, a key component of the divisome in bacterial cell division, has garnered significant attention in recent years due to its crucial role in facilitating cytokinesis in prokaryotic organisms. ZipA is an integral membrane protein that interacts with the FtsZ protein, which forms a ring-like structure at the site of cell division, providing a scaffold for other essential proteins involved in septum formation. Understanding the structure and function of ZipA is essential, as it not only helps elucidate the fundamental mechanisms of bacterial cell division but also presents potential targets for novel antibacterial therapies. As antibiotic resistance becomes an increasing global health concern, targeting bacterial cell division pathways, including those involving ZipA, offers a promising avenue for developing new drugs. Research often involves recombinant expression of ZipA, followed by biochemical and structural analyses, to determine its interaction mechanisms with FtsZ and other divisome components. Such studies are crucial for developing drugs that can effectively disrupt bacterial proliferation by targeting these essential proteins.
