Analytical Data
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基因名
NEU
- Application
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别名
NEU1; SIAL1; Sialidase 1; Lysosomal Sialidase; Acetylneuraminyl hydrolase; G9 sialidase; N-acetyl-alpha-neuraminidase 1
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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
Q99519
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表达区间
Ala141~His286
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分子量
26kDa
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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 NEU (Neuraminidase) recombinant proteins has garnered significant attention due to their crucial role in various biological processes and potential therapeutic applications. NEU enzymes, primarily known for their function in the cleavage of sialic acid residues from glycoproteins and glycolipids, are pivotal in modulating cell signaling, immune responses, and pathogen interactions. Research into NEU recombinant proteins is essential for understanding the biochemical pathways and mechanisms involved in diseases, particularly in the context of viral infections such as influenza and SARS-CoV-2, where viral neuraminidases are critical for viral release and spread. The ability to produce NEU proteins recombinantly allows for detailed structural and functional studies, paving the way for the development of novel antiviral drugs and vaccines. Additionally, NEU proteins hold promise in biotechnological applications, ranging from the enhancement of drug delivery systems to the modification of glycosylation patterns in therapeutic proteins. As research progresses, the insights gained from NEU recombinant proteins may lead to breakthroughs in both basic science and clinical medicine, highlighting their importance in health and disease management.
