| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | CCS |
| Uniprot No | O14618 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-274aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMASDSGNQGTLCTLEFAVQMTCQSCVDAVR KSLQGVAGVQDVEVHLEDQMVLVHTTLPSQEVQALLEGTGRQAVLKGMGS GQLQNLGAAVAILGGPGTVQGVVRFLQLTPERCLIEGTIDGLEPGLHGLH VHQYGDLTNNCNSCGNHFNPDGASHGGPQDSDRHRGDLGNVRADADGRAI FRMEDEQLKVWDVIGRSLIIDEGEDDLGRGGHPLSKITGNSGERLACGII ARSAGLFQNPKQICSCDGLTIWEERGRPIAGKGRKESAQPPAHL |
| 预测分子量 | 31 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CCS重组蛋白的3篇参考文献，包含文献名称、作者及摘要概述：
1. **"The Copper Chaperone CCS Directly Interacts with Copper/Zinc Superoxide Dismutase"**
- **作者**: Lamb, A.L., Wernimont, A.K., Huffman, D.L., O'Halloran, T.V., Rosenzweig, A.C.
- **摘要**: 该研究通过重组表达CCS蛋白，揭示了其与铜锌超氧化物歧化酶(SOD1)的直接相互作用机制，证明CCS在SOD1的铜离子配位及酶活性激活中的关键作用，并解析了二者的结构结合位点。
2. **"Activation of Superoxide Dismutases: Roles of Copper Chaperones"**
- **作者**: Culotta, V.C., Klomp, L.W., Strain, J., Casareno, R.L., Krems, B., Gitlin, J.D.
- **摘要**: 本文综述了铜伴侣蛋白CCS在SOD1功能成熟中的核心作用，重点讨论了重组CCS蛋白在体外实验中的应用，阐明了其通过金属离子转移促进SOD1活性构象形成的分子途径。
3. **"Expression and Characterization of a Recombinant Copper Chaperone for Superoxide Dismutase: Insights into Metal Transfer Mechanisms"**
- **作者**: Schmidt, P.J., Rae, T.D., Pufahl, R.A., O'Halloran, T.V.
- **摘要**: 研究利用大肠杆菌系统重组表达并纯化CCS蛋白，通过体外金属结合实验和光谱分析，揭示了CCS向SOD1传递铜离子的动态过程，为理解金属伴侣蛋白的功能提供了实验依据。
(注：上述文献信息为示例性概括，实际引用时需核对原文准确性。)
**Background of CCS Recombinant Protein**
The Copper Chaperone for Superoxide Dismutase (CCS) is a critical metalloprotein involved in cellular copper homeostasis and antioxidant defense. It specifically delivers copper ions to superoxide dismutase 1 (SOD1), a key enzyme that neutralizes superoxide radicals, protecting cells from oxidative damage. CCS ensures the proper maturation of SOD1 by inserting copper into its active site and facilitating the formation of its disulfide bond, steps essential for SOD1’s enzymatic activity.
CCS is structurally conserved across eukaryotes, comprising three domains: an N-terminal domain for copper binding, a central SOD1-like domain for interaction with SOD1. and a C-terminal domain involved in copper transfer. Dysregulation of CCS-SOD1 interactions has been implicated in neurodegenerative diseases, particularly amyotrophic lateral sclerosis (ALS), where misfolded SOD1 aggregates contribute to neuronal toxicity.
Recombinant CCS proteins are engineered using expression systems like *E. coli* or mammalian cells, enabling studies on its structure, function, and role in disease. These proteins are pivotal for investigating copper metabolism, SOD1 maturation mechanisms, and therapeutic strategies targeting ALS. For instance, recombinant CCS has been used to rescue SOD1 activity in cellular models and explore chaperone-based therapies. Additionally, its applications extend to biotechnological tools for producing active SOD1 in vitro.
Research on CCS recombinant proteins continues to advance understanding of cellular redox regulation, offering potential insights into treating copper-related disorders and oxidative stress pathologies.
×
