Analytical Data
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基因名
Lysozyme C/LYZ
- Application
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别名
LYZ; Renal Amyloidosis; N-Acetylmuramide Glycanhydrolase; Muramidase; 1,4-beta-N-acetylmuramidase C
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P61626
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表达区间
Cys24~Gln144
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分子量
14kDa
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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
Lysozyme C (LYZ) is a highly conserved enzyme found in a variety of biological samples, known for its antimicrobial properties. It plays a crucial role in the innate immune system by hydrolyzing the peptidoglycan layer of bacterial cell walls, thus offering a first line of defense against infections. Due to its significant biological functions and potential applications in food preservation, pharmaceuticals, and biotechnology, the production of recombinant LYZ has garnered considerable interest. Advances in molecular cloning and expression systems have enabled the efficient production of LYZ in various host organisms, including bacteria, yeast, and mammalian cells. Research on recombinant LYZ focuses on optimizing expression conditions, improving enzyme stability, and enhancing its antimicrobial activity. Additionally, the structural and functional characterization of LYZ variants can provide insights into enzyme mechanisms and inform the design of more effective antimicrobial agents. The ongoing exploration of recombinant LYZ also highlights its potential as a therapeutic protein in treating microbial infections and as a complementary agent in antibiotic therapy, especially in light of rising antibiotic resistance. Overall, the study of recombinant LYZ represents a promising avenue for developing innovative solutions to combat infectious diseases and improve food safety.
