Analytical Data
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Gene name
mazF
- Application
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Alternative Names
mazF；chpA；chpAK；Endoribonuclease toxin MazF
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Species
Human
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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
P0AE70
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Expression Region
1-111aa
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AA Sequence
MVSRYVPDMGDLIWVDFDPTKGSEQAGHRPAVVLSPFMYNNKTGMCLCVPCTTQSKGYPFEVVLSGQERDGVALADQVKSIAWRARGATKKGTVAPEELQLIKAKINVLIG
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Molecular Weight
13.6 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
MazF is an endoribonuclease discovered in Escherichia coli and is part of the mazEF toxin-antitoxin system, which plays a crucial role in bacterial response to stress and regulation of cell death. This system is particularly interesting because MazF acts by cleaving mRNA, leading to growth inhibition, which helps the bacteria survive adverse conditions. The study of MazF has garnered attention not only for its regulatory functions in bacterial physiology but also for its potential biotechnological applications, including the development of novel antimicrobial agents. Furthermore, as antibiotic resistance becomes a growing global concern, understanding the mechanisms of MazF and its interactions within the cellular environment could pave the way for innovative therapeutic strategies. Researchers have focused on the structural and functional characterization of MazF to elucidate its enzymatic activity and specificity towards RNA substrates. By utilizing advanced techniques like X-ray crystallography and NMR spectroscopy, insights into its catalytic mechanisms have been gained, providing valuable information for the design of inhibitors that could modulate its activity. Overall, the exploration of MazF represents a promising avenue for both fundamental microbiological research and practical applications in combating antibiotic-resistant pathogens.
