| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ASPRV1 |
| Uniprot No | Q53RT3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 191-326aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSSMGKGYYLKGKIGKVPVRFLVDSGAQV SVVHPNLWEEVTDGDLDTLQPFENVVKVANGAEMKILGVWDTAVSLGKLK LKAQFLVANASAEEAIIGTDVLQDHNAILDFEHRTCTLKGKKFRLLPVGG SLEDEFDLE |
| 预测分子量 | 17 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于ASPRV1重组蛋白的3篇参考文献概览，基于现有研究领域推测其相关内容：
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1. **文献名称**：*ASPRV1 is a novel regulator of epidermal differentiation*
**作者**：Smith J, et al.
**摘要**：本研究通过重组ASPRV1蛋白体外实验，发现其在天冬氨酸蛋白酶活性中起关键作用，参与皮肤屏障相关蛋白的水解调控。重组蛋白在HEK293细胞中表达并纯化后，证实其可特异性切割角蛋白结构蛋白，提示其在表皮分化中的功能。
2. **文献名称**：*Characterization of recombinant human ASPRV1 enzymatic activity*
**作者**：Li X, Wang Y.
**摘要**：作者利用大肠杆菌系统表达ASPRV1重组蛋白，分析其酶动力学参数及pH依赖性。结果表明，ASPRV1在酸性环境下对合成底物显示高催化效率，暗示其可能在溶酶体或皮肤酸性微环境中发挥生理作用。
3. **文献名称**：*ASPRV1 deficiency disrupts stratum corneum integrity via impaired protease activation*
**作者**：Tanaka K, et al.
**摘要**：通过构建ASPRV1敲除小鼠模型，结合重组蛋白回补实验，发现ASPRV1重组蛋白可恢复表皮中丝聚蛋白(filaggrin)的加工缺陷，证明其在维持角质层结构完整性中的必要性。
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**备注**：以上文献为示例性内容，实际研究中可能需通过PubMed或Google Scholar以“ASPRV1 recombinant protein”等关键词检索最新文献。若研究较少，建议扩展至“aspartic proteases in skin”或“retroviral-like proteases”相关主题。
**Background of ASPRV1 Recombinant Protein**
ASPRV1 (Aspartic Peptidase Retroviral-like 1), also known as Retroviral-like Aspartic Protease 1. is a human gene encoding a protease enzyme belonging to the aspartic peptidase family. This enzyme shares structural and functional similarities with retroviral proteases, particularly in its catalytic mechanism involving two conserved aspartic acid residues. ASPRV1 is implicated in proteolytic processing, a critical post-translational modification step that regulates protein activity, localization, and interactions. Although its precise physiological role remains under investigation, ASPRV1 is hypothesized to participate in processes such as extracellular matrix remodeling, immune response modulation, and cellular signaling.
The recombinant ASPRV1 protein is produced using biotechnological methods, typically via heterologous expression in systems like *E. coli* or mammalian cell cultures, followed by purification to ensure high specificity and activity. Recombinant forms enable detailed biochemical and functional studies, allowing researchers to explore substrate specificity, enzymatic kinetics, and inhibitor interactions. Its study holds therapeutic relevance, as dysregulation of proteases like ASPRV1 has been linked to pathologies including cancer metastasis, inflammatory disorders, and neurodegenerative diseases. Additionally, ASPRV1's retroviral-like features provide insights into evolutionary connections between endogenous human proteases and viral enzymes, potentially informing antiviral drug design.
As a research tool, ASPRV1 recombinant protein supports drug discovery pipelines and structural biology efforts, such as X-ray crystallography or cryo-EM, to elucidate its 3D architecture and catalytic mechanisms. Ongoing research aims to clarify its endogenous substrates and regulatory pathways, advancing its potential as a diagnostic or therapeutic target.
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