Analytical Data
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Gene name
fbpC
- Application
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Alternative Names
fbpC；Fe(3+) ions import ATP-binding Protein FbpC
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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
P9WQN8
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Expression Region
46-340aa
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AA Sequence
AFSRPGLPVEYLQVPSASMGRDIKVQFQGGGPHAVYLLDGLRAQDDYNGWDINTPAFEEYYQSGLSVIMPVGGQSSFYTDWYQPSQSNGQNYTYKWETFLTREMPAWLQANKGVSPTGNAAVGLSMSGGSALILAAYYPQQFPYAASLSGFLNPSEGWWPTLIGLAMNDSGGYNANSMWGPSSDPAWKRNDPMVQIPRLVANNTRIWVYCGNGTPSDLGGDNIPAKFLEGLTLRTNQTFRDTYAADGGRNGVFNFPPNGTHSWPYWNEQLVAMKADIQHVLNGATPPAAPAAPAA
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Molecular Weight
36.1 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
Related Products
Protein Description
FBPc (FtsZ-binding protein C) is a critical component in bacterial cell division, playing a pivotal role in the regulation of peptidoglycan synthesis and maintaining cell shape. Its function is closely associated with the bacterial cytoskeleton and the dynamic assembly of the Z-ring, which is essential for cytokinesis. Research on FBPc recombinant protein has garnered interest due to its potential implications in understanding bacterial growth and division mechanisms, as well as its prospective applications in antibiotic development. The emergence of antibiotic resistance has prompted the scientific community to explore novel targets for drug development, and FBPc represents a promising candidate. By elucidating the structural and functional properties of FBPc, researchers aim to uncover its precise role in the bacterial cell cycle and its interactions with other key proteins involved in cell division. Techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy are often employed to determine the protein’s structure, while in vitro assays are utilized to investigate its functional interactions. The recombinant production of FBPc not only facilitates these studies but also enables the exploration of its potential as a target for novel antimicrobial agents. Furthermore, understanding the regulatory mechanisms involving FBPc could lead to breakthroughs in designing innovative strategies to combat bacterial infections, thereby addressing a significant public health challenge.
