纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MT1A |
Uniprot No | P04731 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-59aa |
氨基酸序列 | MDPNCSCATGGSCTCTGSCKCKECKCTSCKKSCCSCCPMSCAKCAQGCICKGASEKCSC |
预测分子量 | 32.9 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MT1A重组蛋白的参考文献示例(注:以下为假设性文献,供格式参考):
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1. **标题**: "Expression and Purification of Recombinant Human MT1A in E. coli for Metal Chelation Studies"
**作者**: Zhang Y, et al.
**摘要**: 本研究通过大肠杆菌表达系统成功制备重组人MT1A蛋白,优化了诱导条件及纯化流程,并证实其具有高亲和力的镉离子结合能力,为金属解毒机制研究提供工具。
2. **标题**: "Structural and Functional Analysis of Recombinant MT1A in Antioxidant Defense"
**作者**: Lee S, Kim J.
**摘要**: 通过圆二色谱和细胞实验,解析重组MT1A的二级结构,证明其通过清除自由基减轻氧化应激损伤,在HEK293细胞模型中显著提升抗氧化酶活性。
3. **标题**: "Recombinant MT1A Attenuates Cisplatin-Induced Nephrotoxicity via Heavy Metal Sequestration"
**作者**: Gupta R, et al.
**摘要**: 在小鼠模型中,重组MT1A蛋白有效降低顺铂导致的肾脏铂蓄积及病理损伤,提示其在化疗辅助解毒中的潜在治疗价值。
4. **标题**: "Development of a Novel MT1A Fusion Protein for Enhanced Stability and Bioavailability"
**作者**: Müller C, et al.
**摘要**: 设计并表达了一种MT1A-硫氧还蛋白融合蛋白,显著延长重组蛋白的半衰期,并验证其在体外金属螯合效率,为工业化生产奠定基础。
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以上文献摘要概括了MT1A重组蛋白的表达优化、结构功能研究、治疗应用及改良策略,覆盖基础研究与潜在应用方向。实际引用时建议通过学术数据库检索真实文献。
**Background of MT1A Recombinant Protein**
Metallothionein 1A (MT1A) is a small, cysteine-rich protein belonging to the metallothionein (MT) family, which plays critical roles in metal ion homeostasis, detoxification of heavy metals, and protection against oxidative stress. MT1A is encoded by the *MT1A* gene located on human chromosome 16 and is highly conserved across species. Its structure includes multiple cysteine residues (20 out of ~61 amino acids) arranged in characteristic motifs, enabling strong binding to divalent metal ions like zinc, copper, and cadmium. This metal-binding capacity underpins its involvement in regulating cellular metal distribution, scavenging reactive oxygen species (ROS), and mitigating metal toxicity.
Recombinant MT1A protein is produced using biotechnological platforms, such as *E. coli* or yeast expression systems, to ensure high purity and scalability. These systems allow precise control over post-translational modifications and metal-loading states, making recombinant MT1A valuable for research and industrial applications. The protein is often purified via affinity chromatography and validated using techniques like SDS-PAGE, Western blotting, and mass spectrometry to confirm integrity and functionality.
In biomedical research, MT1A recombinant protein is widely used to study mechanisms of metal-related diseases (e.g., neurodegenerative disorders, cancer) and oxidative stress pathways. It also serves as a tool in environmental toxicology to assess heavy metal detoxification processes. Additionally, its antioxidant properties have spurred interest in therapeutic applications, including potential use in treating metal overload conditions or as a protective agent against radiation or chemotherapy-induced cellular damage.
Despite its promise, challenges remain in optimizing recombinant production to maintain native folding and metal-binding activity. Ongoing studies aim to refine expression systems and explore engineered variants for enhanced stability or targeted functions, broadening MT1A's utility in both basic science and clinical contexts.
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