Analytical Data
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Gene name
ftsZ
- Application
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Alternative Names
ftsZ；Cell division Protein FtsZ
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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
P0A9A7
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Expression Region
1-383aa
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AA Sequence
MFEPMELTNDAVIKVIGVGGGGGNAVEHMVRERIEGVEFFAVNTDAQALR KTAVGQTIQIGSGITKGLGAGANPEVGRNAADEDRDALRAALEGADMVFI AAGMGGGTGTGAAPVVAEVAKDLGILTVAVVTKPFNFEGKKRMAFAEQGI TELSKHVDSLITIPNDKLLKVLGRGISLLDAFGAANDVLKGAVQGIAELI TRPGLMNVDFADVRTVMSEMGYAMMGSGVASGEDRAEEAAEMAISSPLLE DIDLSGARGVLVNITAGFDLRLDEFETVGNTIRAFASDNATVVIGTSLDP DMNDELRVTVVATGIGMDKRPEITLVTNKQVQQPVMDRYQQHGMAPLTQE QKPVAKVVNDNAPQTAKEPDYLDIPAFLRKQAD
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Molecular Weight
56 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
FtsZ is a key protein involved in bacterial cell division, serving as a homolog of tubulin in eukaryotes. It plays a critical role in forming the Z-ring at the future site of division, recruiting other proteins necessary for cell wall synthesis and ultimately facilitating cytokinesis. Research on FtsZ has garnered significant interest due to its essential function in bacterial proliferation and its potential as a target for novel antibiotic development. The understanding of FtsZ dynamics, assembly, and regulation not only provides insights into the fundamental mechanisms of bacterial cell division but also highlights its evolutionary significance as a precursor to the cytoskeletal structures found in higher organisms. Recent studies employing recombinant FtsZ have expanded our knowledge of its structure-function relationships, allowing researchers to investigate the effects of various post-translational modifications and regulatory proteins on its activity. Additionally, the development of in vitro assays has enabled detailed investigations of the polymerization kinetics and interactions of FtsZ with other cell division components. Given the rising issue of antibiotic resistance, characterizing the properties and mechanisms of FtsZ offers a promising avenue for discovering new therapeutic strategies to combat bacterial infections. As such, the ongoing exploration of FtsZ and its role in the bacterial life cycle not only enriches our understanding of bacterial biology but also has important implications for public health and the development of innovative treatments.
