Analytical Data
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基因名
Animal-Free Enterokinase
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简介
Enterokinase proteins play a key role in initiating the activation of pancreatic proteolytic enzymes, including trypsin, chymotrypsin, and carboxypeptidase A. Its catalytic function converts trypsinogen to trypsin, triggering the cascade activation of chymotrypsinogen, procarboxypeptidase, and tropoelastin. Animal-Free Enterokinase Protein, Bovine (His) is the recombinant bovine-derived Enterokinase, expressed by P. pastoris, with C-His labeled tag. The total length of Animal-Free Enterokinase Protein, Bovine (His) is 235 a.a..
- Application
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别名
Enteropeptidase; Enterokinase; Serine protease 7; Transmembrane protease serine 15; Enteropeptidase; ENTK; PRSS7
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种属
Bovine
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表达系统
P. pastoris
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标签
C-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P98072-1
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表达区间
I801-H1035
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蛋白长度
Full Length of Enteropeptidase catalytic light chain
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分子量
40 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
Animal-Free Enterokinase is a recombinant protein that has gained attention due to the growing demand for safer and more ethical bioprocessing solutions in biotechnology and pharmaceuticals. Traditional enterokinase, an enzyme crucial for activating digestive proenzymes, is typically derived from animal sources, particularly bovine or porcine tissues. However, these sources pose several issues, including the risk of viral contamination, ethical concerns regarding animal welfare, and batch-to-batch variability in enzyme activity. In response to these challenges, researchers have turned to recombinant DNA technology to produce enterokinase in a controlled environment, using microbial or yeast expression systems that completely eliminate the need for animal-derived components. This approach not only enhances the safety profile of the enzyme but also ensures consistent quality and high purity, making it suitable for use in various applications, such as protein purification and the production of therapeutic proteins. The development of animal-free enterokinase contributes to a more sustainable and ethical biotechnology industry, addressing both consumer concerns and regulatory demands for animal-free products. This innovation aligns with the broader trend towards plant-based and synthetic alternatives in the life sciences, aiming to reduce dependence on animal sources while maintaining the efficacy and reliability of biotechnological products. As research advances in this area, the potential for animal-free enterokinase to become a standard tool in laboratories worldwide is becoming increasingly recognized.
