Analytical Data
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Gene name
nisZ
- Application
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Alternative Names
nisZ；Lantibiotic nisin-Z
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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
P29559
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Expression Region
1-57aa
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AA Sequence
MSTKDFNLDLVSVSKKDSGASPRITSISLCTPGCKTGALMGCNMKTATCNCSIHVSK
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Molecular Weight
5.9kDa
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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
NisZ is a key component of the nisin biosynthetic pathway, which is responsible for the production of nisin, a well-known antimicrobial peptide used as a food preservative. Nisin is produced by certain strains of Lactococcus lactis and exhibits strong activity against a wide range of Gram-positive bacteria, including pathogenic strains such as Listeria monocytogenes. The study of NisZ focuses on its role as a modifying enzyme in the post-translational modification of nisin, specifically in the incorporation of unusual amino acids that contribute to the peptide's bioactivity. Understanding the mechanism of action and structure-function relationship of NisZ is crucial, as it can provide insights into the biosynthesis of nisin and potentially enable the engineering of novel antimicrobial peptides with enhanced properties. Furthermore, with the increasing prevalence of antibiotic resistance, exploring alternative antimicrobial agents like nisin and its derivatives has become imperative. Research on NisZ thus not only contributes to the fundamental understanding of bacteriocin biosynthesis but also has significant implications for developing new strategies to combat bacterial infections and enhance food safety.
