Analytical Data
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基因名
Aminopeptidase P2
- Application
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别名
Xaa-Pro aminopeptidase 2; Membrane-bound aminopeptidase P; Membrane-bound APP; mAPP; X-prolyl aminopeptidase 2; Xpnpep2;
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种属
Mouse
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表达系统
HEK293
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标签
C-8*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
B1AVD1
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表达区间
P23-A650
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蛋白长度
Full Length of Mature Protein
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分子量
75-105 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
Aminopeptidase P2 (APP2) is an enzyme that plays a critical role in the hydrolysis of peptide bonds at the amino terminus of proteins, specifically targeting proline residues. This enzyme is particularly significant in various physiological processes, including protein metabolism and regulation of bioactive peptides. Recent studies have highlighted the potential role of APP2 in various pathological conditions, such as cardiovascular diseases, where it may be involved in the modulation of vasoactive peptides. The recombinant expression of APP2 has been a focus of research to facilitate the study of its structure-function relationship and to understand its biochemical properties. By producing recombinant APP2 in a controlled environment, researchers can analyze its enzymatic activity, investigate its substrate specificity, and explore its potential as a therapeutic target. Furthermore, the availability of recombinant APP2 supports the development of inhibitors that could serve as valuable tools in treating diseases linked to dysregulated peptide metabolism. Understanding the functional mechanisms of APP2 could yield insights into new biomedical applications and enhance our knowledge of various enzymatic processes in the human body. Overall, the study of recombinant APP2 is pivotal in advancing our comprehension of this enzyme’s role in health and disease.
