Analytical Data
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基因名
ARG
- Application
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别名
ARG1; Arginase I; Liver Arginase
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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
P05089
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表达区间
Met1~Lys322
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分子量
37kDa
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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
ARG (Arginine-rich protein) recombinant proteins have drawn significant attention in recent years due to their diverse biological functions and potential applications in various fields, including therapeutics and biotechnology. These proteins, characterized by their high arginine content, play crucial roles in cellular processes such as gene regulation, cell signaling, and protein interactions. Research has shown that ARG proteins can influence the stability and activity of other proteins, as well as modulate the immune response. Their unique structural characteristics facilitate the interaction with nucleic acids, making them valuable tools in gene delivery systems and molecular biology studies. Advances in recombinant DNA technology have enabled the production of these proteins in large quantities, allowing for detailed studies of their structure-function relationships. Additionally, ARG proteins have shown promise in drug delivery and as novel therapeutic agents, particularly in targeting cancer cells and combating infectious diseases. As the understanding of ARG proteins continues to evolve, their potential applications in personalized medicine and targeted therapies are becoming increasingly evident, underscoring the importance of continued research in this field. This growing interest in ARG recombinant proteins not only enhances our understanding of fundamental biological mechanisms but also paves the way for innovative solutions to complex health challenges.












