| 纯度 | >80%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ELP5 |
| Uniprot No | Q8TE02 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-316aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMTPSEGA RAGTGRELEM LDSLLALGGL VLLRDSVEWE GRSLLKALVK KSALCGEQVH ILGCEVSEEE FREGFDSDIN NRLVYHDFFR DPLNWSKTEE AFPGGPLGAL RAMCKRTDPV PVTIALDSLS WLLLRLPCTT LCQVLHAVSH QDSCPGDSSS VGKVSVLGLL HEELHGPGPV GALSSLAQTE VTLGGTMGQA SAHILCRRPR QRPTDQTQWF SILPDFSLDL QEGPSVESQP YSDPHIPPVD PTTHLTFNLH LSKKEREARD SLILPFQFSS EKQQALLRPR PGQATSHIFY EPDAYDDLDQ EDPDDDLDI |
| 预测分子量 | 37 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ELP5重组蛋白的3篇代表性参考文献(注：以下为假设文献示例，实际文献需通过数据库检索验证)：
---
1. **标题**: *Structural and functional analysis of the Elongator complex subunit ELP5*
**作者**: Winkler GS, et al.
**摘要**: 本研究解析了ELP5作为Elongator复合体核心亚基的结构特征，通过重组表达纯化人源ELP5蛋白，结合晶体学分析发现其与ELP3的相互作用界面，并验证其在组蛋白乙酰化修饰及神经发育中的调控作用。
---
2. **标题**: *Recombinant ELP5 expression in E. coli and its role in tRNA modification*
**作者**: Chen L, et al.
**摘要**: 报道了利用大肠杆菌系统高效表达并纯化重组ELP5蛋白的优化方法，通过体外酶活实验证实ELP5与ELP2/ELP3协同催化tRNA wobble尿苷的硫醇化修饰，为研究其分子机制提供工具。
---
3. **标题**: *ELP5 deficiency links to neurodegenerative disorders via impaired synaptic plasticity*
**作者**: Nelissen H, et al.
**摘要**: 通过构建ELP5条件性敲除小鼠模型，发现ELP5缺失导致神经元中Elongator复合体功能异常，引发tRNA修饰缺陷和蛋白质翻译效率下降，最终加剧阿尔茨海默病模型小鼠的认知障碍。
---
如需具体文献，建议在PubMed或Web of Science中以“ELP5 recombinant”、“ELP5 Elongator complex”为关键词检索。
**Background of ELP5 Recombinant Protein**
Elastin-like polypeptides (ELPs) are synthetic biopolymers inspired by the natural elastin protein, known for their unique temperature-responsive behavior and biocompatibility. ELP5. a specific member of this family, is engineered through recombinant DNA technology, where repetitive peptide sequences (typically Val-Pro-Gly-Xaa-Gly motifs, with Xaa as a variable amino acid) are encoded into host organisms like *Escherichia coli* or yeast. This design allows ELP5 to undergo reversible phase separation in response to environmental triggers such as temperature or ionic strength, a property termed "inverse temperature transition."
ELP5 has gained attention in biomedical research due to its tunable physicochemical properties. Its modular structure enables customization for applications like drug delivery, tissue engineering, and diagnostic platforms. For instance, ELP5 can be functionalized with bioactive domains (e.g., cell-binding peptides or therapeutic proteins) to enhance targeting or therapeutic efficacy. Its ability to self-assemble into nanoparticles or hydrogels further expands its utility in controlled-release systems.
A key advantage of ELP5 lies in its scalable production. Recombinant expression ensures high purity and batch consistency, while the phase transition property simplifies purification via a cost-effective "thermal cycling" method. Additionally, ELP5's biodegradability and low immunogenicity make it suitable for *in vivo* applications. Recent studies explore its role in cancer therapy (e.g., delivering chemotherapeutics) and regenerative medicine (e.g., scaffolds for cell growth). Overall, ELP5 exemplifies the fusion of protein engineering and material science, offering versatile solutions for emerging challenges in healthcare and biotechnology.
×
