Analytical Data
-
Gene name
nisZ
- Application
-
Species
Lactococcus lactis
-
Source
E. coli
-
Tag
N- His-KSI
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P29559
-
Expression Region
24-57aa
-
Molecular Weight
18.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 membrane-associated protein that plays a critical role in the biosynthesis of nisin, a naturally occurring antimicrobial peptide produced by certain lactic acid bacteria. The interest in NisZ stems from its involvement in the post-translational modification of the nisin precursor, which is essential for the peptide's antimicrobial activity. Nisin has gained significant attention due to its ability to inhibit a wide range of Gram-positive bacteria, including foodborne pathogens and spoilage organisms, making it an attractive candidate for use as a natural food preservative. The growing trend toward clean-label products has further fueled interest in exploring nisin and its production mechanisms. Research on NisZ encompasses various aspects, including its structure, function, and interaction with other proteins involved in nisin maturation. Understanding the biochemical pathways and molecular interactions facilitated by NisZ is vital for optimizing nisin production in industrial settings and potentially developing novel antimicrobial agents. Advances in this field may lead to innovative approaches to combat antibiotic resistance and enhance food safety.
