Analytical Data
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基因名
patZ
- Application
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别名
(Protein lysine acetyltransferase)
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种属
Escherichia coli
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表达系统
E. coli
-
标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P76594
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表达区间
724-886aa
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分子量
26.3 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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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.












