关键信息
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基因名
lytA
- 应用
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别名
N-acetylmuramoyl-L-alanine amidase
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种属
Staphylococcus aureus
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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
P24556
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表达区间
1-481aa
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分子量
57.8 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.
质检流程
相关产品
背景信息
LytA, a key autolysin enzyme in Streptococcus pneumoniae, plays a crucial role in bacterial cell wall metabolism and contributes to the bacterium's pathogenicity. Understanding LytA's structure and function is essential for developing new therapeutic strategies against pneumococcal infections, which remain a major public health concern despite the availability of vaccines. Research on LytA recombinant proteins has gained traction in recent years, as these proteins can be utilized to investigate the enzyme's active site, substrate specificity, and interaction with other cell wall components. Additionally, LytA recombinant proteins offer potential as vaccine candidates, as they may elicit protective immune responses. Studies have focused on the expression and purification of LytA in various systems, alongside the characterization of its enzymatic activity to uncover its biological significance. As antibiotic resistance continues to rise, targeting virulence factors like LytA presents a promising approach to developing alternative treatments. The ongoing research aims to provide insights into LytA's mechanism of action, paving the way for innovative interventions against Streptococcus pneumoniae and related pathogens.
