| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHAC2 |
| Uniprot No | Q8WUX2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-184aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMWVFGYG SLIWKVDFPY QDKLVGYITN YSRRFWQGST DHRGVPGKPG RVVTLVEDPA GCVWGVAYRL PVGKEEEVKA YLDFREKGGY RTTTVIFYPK DPTTKPFSVL LYIGTCDNPD YLGPAPLEDI AEQIFNAAGP SGRNTEYLFE LANSIRNLVP EEADEHLFAL EKLVKERLEG KQNLNCI |
| 预测分子量 | 23 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CHAC2重组蛋白的模拟参考文献示例(实际文献需通过学术数据库验证)：
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1. **文献名称**: *"Expression and Functional Analysis of Recombinant CHAC2 in Glutathione Metabolism"*
**作者**: Zhang Y. et al. (2016)
**摘要**: 本研究利用大肠杆菌系统成功表达并纯化了CHAC2重组蛋白，证实其具有谷胱甘肽特异性γ-谷氨酰环转移酶活性，揭示了其在氧化应激条件下调控细胞内谷胱甘肽水平的作用机制。
2. **文献名称**: *"CHAC2 Recombinant Protein Induces Apoptosis via ER Stress Pathway in Cancer Cells"*
**作者**: Chen L. et al. (2018)
**摘要**: 通过哺乳动物细胞表达系统制备CHAC2重组蛋白，发现其通过内质网应激通路触发肿瘤细胞凋亡，为靶向谷胱甘肽代谢的抗癌治疗提供了实验依据。
3. **文献名称**: *"Structural Characterization of Human CHAC2 by X-ray Crystallography"*
**作者**: Kim S. et al. (2020)
**摘要**: 首次解析了重组CHAC2蛋白的晶体结构，明确了其底物结合域和催化活性中心的关键氨基酸残基，为开发小分子调节剂奠定结构基础。
4. **文献名称**: *"CHAC2 Recombinant Protein: Applications in Neurodegenerative Disease Models"*
**作者**: Gupta R. et al. (2021)
**摘要**: 综述了CHAC2重组蛋白在阿尔茨海默病等神经退行性疾病模型中的应用，强调其通过调节谷胱甘肽稳态缓解神经元氧化损伤的潜力。
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**注意**：以上文献信息为模拟示例，实际研究请通过 **PubMed/Google Scholar** 等平台以关键词“CHAC2 recombinant protein”检索真实文献。
CHAC2 (Cation Transport Regulator-like Protein 2) is a member of the CHAC protein family, which is evolutionarily conserved and implicated in cellular redox homeostasis. It shares structural homology with CHAC1. a well-characterized glutathione (GSH)-degrading enzyme that catalyzes the cleavage of GSH into 5-oxoproline and cysteinylglycine via its γ-glutamylcyclotransferase activity. While CHAC1 is primarily associated with endoplasmic reticulum (ER) stress-induced apoptosis and GSH metabolism, CHAC2 is less studied but believed to play complementary or distinct roles in redox regulation.
CHAC2 is encoded by the *CHAC2* gene located on human chromosome 2. Structurally, it contains a conserved N-terminal thioredoxin-like domain and a C-terminal γ-glutamylcyclotransferase domain, suggesting potential enzymatic activity in GSH degradation or related pathways. Unlike CHAC1. which is stress-inducible, CHAC2 exhibits constitutive expression in tissues like the liver, kidney, and heart, hinting at housekeeping functions in basal redox balance. Studies suggest its involvement in mitigating oxidative damage, modulating mitochondrial function, and influencing cell survival under stress conditions.
Recombinant CHAC2 protein is typically produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) for functional studies. Purification methods often employ affinity tags (e.g., His-tag) followed by chromatography. Its applications include enzymatic assays to validate GSH degradation activity, structural analysis via crystallography or cryo-EM, and exploring its role in diseases linked to oxidative stress, such as neurodegenerative disorders, cancer, or cardiovascular pathologies. Research on CHAC2 remains nascent, but its potential as a therapeutic target or biomarker in redox-related diseases continues to drive interest.
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