Analytical Data
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基因名
lytM
- Application
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别名
Autolysin LytM
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种属
Staphylococcus aureus
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表达系统
E. coli
-
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
O33599
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表达区间
26-316aa
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分子量
35.9 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
LytM protein, a member of the large family of metalloproteases, plays a critical role in various biological processes, including bacterial cell wall degradation and regulation of protein turnover. The significance of LytM proteins has garnered attention in the context of bacterial pathogenesis, where they facilitate the breakdown of peptidoglycan, thereby enabling bacteria to alter their cell shape or escape immune responses. This capability makes LytM an attractive target for the development of novel antimicrobial strategies aimed at combating antibiotic-resistant infections. Researchers have been investigating the structure-function relationship of LytM proteins to elucidate their enzymatic mechanisms and identify potential inhibitors. Advances in protein engineering techniques and high-throughput screening methods have further accelerated the exploration of LytM, leading to promising findings that may pave the way for new therapeutic interventions. Understanding the role of LytM in various organisms not only enhances our knowledge of microbial physiology but also provides insights into evolutionary adaptations that have allowed some bacteria to thrive in hostile environments. Consequently, the study of LytM proteins carries significant implications for both basic science and clinical applications in the fight against infectious diseases.












