| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSP40 |
| Uniprot No | P25685 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-340aa |
| 氨基酸序列 | MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI |
| 预测分子量 | 65.0kDa |
| 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HSP40重组蛋白的虚构参考文献示例，内容基于典型研究方向概括：
1. **《Structural and functional analysis of recombinant human HSP40 (DNAJA1) co-chaperone activity》**
- **作者**: Cheetham, M.E., Caplan, A.J.
- **摘要**: 研究重组人源HSP40(DNAJA1)的蛋白结构及其与HSP70的协同作用，阐明其在帮助错误折叠蛋白质重折叠中的分子机制。
2. **《Recombinant HSP40 suppresses amyloid-β aggregation in Alzheimer’s disease models》**
- **作者**: Lu, Z., Wang, X., et al.
- **摘要**: 利用重组HSP40蛋白在细胞模型中抑制β-淀粉样蛋白聚集，证明其通过增强HSP70活性减缓神经退行性疾病进程。
3. **《Prokaryotic expression and purification of HSP40 for in vitro chaperone assays》**
- **作者**: Yamamoto, T., Tanaka, K.
- **摘要**: 描述在大肠杆菌系统中高效表达和纯化重组HSP40的方法，并验证其在体外分子伴侣活性检测中的应用。
4. **《HSP40 recombinant protein enhances thermotolerance in plant cells via ROS scavenging》**
- **作者**: Li, H., Chen, R.
- **摘要**: 发现重组HSP40通过清除活性氧(ROS)提升植物细胞耐热性，为农业抗逆基因工程提供新靶点。
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注：以上文献为示例，实际引用需检索PubMed或Google Scholar获取真实发表论文。
**Background of HSP40 Recombinant Proteins**
Heat shock protein 40 (HSP40), also known as DNAJ proteins, belongs to a conserved family of molecular chaperones that play critical roles in protein homeostasis. These proteins are named for their ability to respond to cellular stress, such as heat shock, by stabilizing nascent polypeptides, preventing aggregation, and facilitating proper protein folding. HSP40 functions as a co-chaperone for HSP70 ATPases, where it binds client proteins via its J-domain and stimulates HSP70’s ATPase activity to regulate substrate recognition and folding cycles.
Recombinant HSP40 proteins are engineered versions produced through genetic cloning and expression in systems like *E. coli*, yeast, or mammalian cells. This allows large-scale production of highly pure, functional HSP40 for research and therapeutic applications. The recombinant form retains key domains, including the J-domain for HSP70 interaction, a glycine/phenylalanine-rich region, and a substrate-binding domain, enabling studies on its chaperone mechanisms.
Research on recombinant HSP40 spans multiple fields. In cancer biology, HSP40 overexpression is linked to tumor progression and drug resistance, making it a potential therapeutic target. In neurodegenerative diseases like Alzheimer’s or Parkinson’s, HSP40 assists in mitigating protein misfolding and aggregation. Additionally, recombinant HSP40 is used to study bacterial and viral infections, as pathogens often hijack host chaperones for replication.
The development of HSP40 recombinant proteins has advanced drug discovery, enabling high-throughput screening for chaperone modulators. It also supports structural studies (e.g., X-ray crystallography) to elucidate interaction networks. Challenges remain in understanding tissue-specific isoforms and post-translational modifications, which recombinant systems aim to address. Overall, HSP40 recombinant tools are indispensable for decoding proteostasis mechanisms and developing targeted therapies.
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