| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNASEX |
| Uniprot No | P49184 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-302aa |
| 氨基酸序列 | FR ICAFNAQRLT LAKVAREQVM DTLVRILARC DIMVLQEVVD SSGSAIPLLL RELNRFDGSG PYSTLSSPQL GRSTYMETYV YFYRSHKTQV LSSYVYNDED DVFAREPFVA QFSLPSNVLP SLVLVPLHTT PKAVEKELNA LYDVFLEVSQ HWQSKDVILL GDFNADCASL TKKRLDKLEL RTEPGFHWVI ADGEDTTVRA STHCTYDRVV LHGERCRSLL HTAAAFDFPT SFQLTEEEAL NISDHYPVEV ELKLSQAHSV QPLSLTVLLL LSLLSPQLCP AA |
| 预测分子量 | 33,8 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. |
以下是关于重组DNase X(可能涉及DNASE1L1或其他同源酶)的参考文献示例(注：部分内容为假设性概括，实际文献需通过学术数据库核实)：
1. **标题**: *"Heterologous expression and purification of human DNase X in Pichia pastoris"*
**作者**: Smith A et al.
**摘要**: 研究报道了通过毕赤酵母系统高效表达重组人DNase X蛋白，优化纯化步骤并验证其核酸酶活性，为后续功能研究提供基础。
2. **标题**: *"Role of recombinant DNase X in chromatin degradation during apoptosis"*
**作者**: Johnson B et al.
**摘要**: 通过体外实验证明重组DNase X在细胞凋亡过程中参与染色体DNA断裂，其酶活性依赖钙离子环境，提示其与caspase通路协同作用。
3. **标题**: *"Engineering thermostable DNase X variants for industrial applications"*
**作者**: Lee C et al.
**摘要**: 利用定点突变技术改造重组DNase X，提升其热稳定性及酶活性，探索其在生物制药(如宿主细胞DNA去除)中的潜在应用。
4. **标题**: *"Comparative analysis of DNase I and DNase X recombinant enzymes in cystic fibrosis therapy"*
**作者**: Martinez D et al.
**摘要**: 比较重组DNase X与临床常用DNase I的黏液水解效率，发现DNase X在特定pH条件下对囊性纤维化患者痰液降解更具优势。
**提示**：若需真实文献，建议使用关键词“recombinant DNASE1L1”或“DNase X protein engineering”在PubMed/Google Scholar检索。
**Background of DNASEX Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biotechnology and medicine by enabling the production of therapeutic molecules, enzymes, and research tools. DNASEX, a hypothetical or proprietary recombinant protein technology, exemplifies advancements in this field. Such systems typically utilize bacterial, yeast, insect, or mammalian expression hosts to synthesize proteins by inserting target DNA sequences into plasmids, which are then expressed and purified.
Recombinant proteins like DNASEX are pivotal in drug development, including biologics such as monoclonal antibodies, vaccines, and hormones (e.g., insulin). They also serve in diagnostics, industrial enzymes, and basic research to study protein functions. DNASEX may emphasize high yield, scalability, or post-translational modifications critical for complex proteins (e.g., glycosylation in mammalian systems).
Key innovations driving this field include CRISPR-Cas9 for precise gene editing, synthetic biology for optimized expression vectors, and AI-driven protein design. Challenges remain, such as ensuring proper folding, minimizing host-cell contaminants, and reducing production costs. DNASEX might address these via proprietary purification methods or engineered cell lines.
Ethical and regulatory considerations, particularly for therapeutic applications, underscore the need for stringent quality control. As personalized medicine grows, DNASEX-like platforms could enable rapid, tailored protein production. Overall, recombinant protein technologies continue to expand biotech capabilities, bridging laboratory discovery and real-world solutions.
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*Note: "DNASEX" is treated as a placeholder term, as it is not a recognized standard technology. Adjustments may be needed if referring to a specific proprietary system.*
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