Analytical Data
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基因名
acm
- Application
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别名
1,4-beta-N-acetylmuramidase M1
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种属
Streptomyces globisporus
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表达系统
E. coli
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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
P25310
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表达区间
78-294aa
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分子量
30.6 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 study of acyl-CoA-binding proteins (ACBP) and their restructured variants has gained significant attention in recent years due to their essential roles in lipid metabolism and cellular energy homeostasis. ACBP is known to facilitate the transport of acyl-CoA esters, which are vital intermediates in fatty acid metabolism, thereby influencing various physiological processes including energy production, signaling pathways, and membrane synthesis. Restructuring these proteins through techniques such as site-directed mutagenesis or protein engineering aims to enhance their stability, binding affinity, and specificity for different acyl-CoA substrates. This can lead to a better understanding of the molecular mechanisms underlying lipid-related diseases, including obesity, diabetes, and cardiovascular disorders. Furthermore, engineered ACBP variants could serve as valuable tools in metabolic engineering and synthetic biology, potentially aiding in the development of novel therapeutic strategies. As research progresses, the implications of ACBP manipulation extend beyond basic biology, presenting opportunities for biotechnological applications in health and disease management.
