Analytical Data
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Gene name
patZ
- Application
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Alternative Names
(Protein lysine acetyltransferase)
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P76594
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Expression Region
724-886aa
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Molecular Weight
26.3 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
The patZ gene, derived from the plasmid pAD1 of Enterococcus faecalis, encodes a peptide with antimicrobial activity against several Gram-positive bacteria. Research on patZ recombinant protein has gained momentum due to its potential applications in combating antibiotic resistance, a major global health concern. The increasing prevalence of multidrug-resistant bacterial strains necessitates the discovery of novel antimicrobial agents, and patZ presents an exciting candidate due to its unique mechanism of action, which targets bacterial cell walls. Initial studies indicate that patZ exhibits a strong inhibitory effect on the growth of pathogens like Staphylococcus aureus and Listeria monocytogenes. By cloning and expressing patZ in suitable host systems such as Escherichia coli, researchers aim to produce the recombinant protein in larger quantities for further investigation. Detailed characterization of the recombinant patZ, including its stability, activity, and interaction with bacterial targets, is crucial for understanding its therapeutic potential. Furthermore, examining the structure-activity relationship of patZ could lead to the development of enhanced derivatives with improved efficacy. Given the urgent need for new antimicrobial strategies, the ongoing research into patZ and its recombinant protein form represents a promising avenue for the development of novel antibacterial therapies.
