Analytical Data
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基因名
Anionic trypsin
- Application
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别名
; Anionic trypsin; EC 3.4.21.4
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种属
Dog
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P06872
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表达区间
24-247aa
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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
Anionic trypsin, a serine protease primarily found in the pancreas, plays a pivotal role in protein digestion by cleaving peptide bonds at the carboxyl side of lysine and arginine residues. Its physiological significance extends beyond digestion, as it is involved in various biological processes, including cell signaling and immune responses. The recombinant production of anionic trypsin has gained attention due to its potential applications in biotechnology and pharmaceuticals. Traditional extraction from animal sources raises ethical concerns and poses risks of contamination, prompting researchers to explore alternative methods for obtaining this enzyme. Genetic engineering techniques enable the efficient production of anionic trypsin in microbial hosts, allowing for large-scale production while ensuring high purity and activity. Additionally, understanding the enzyme's structure-function relationship can lead to the design of specific inhibitors or activators, which may have therapeutic implications for diseases related to protease dysregulation. The research on recombinant anionic trypsin thus holds promise not only for advancing our understanding of proteolytic enzymes but also for developing novel biotechnological applications in diverse fields, including drug development and food processing.












