| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CUTA |
| Uniprot No | O60888 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-179aa |
| 氨基酸序列 | RLLLLPRV LLTMASGSPP TQPSPASDSG SGYVPGSVSA AFVTCPNEKV AKEIARAVVE KRLAACVNLI PQITSIYEWK GKIEEDSEVL MMIKTQSSLV PALTDFVRSV HPYEVAEVIA LPVEQGNFPY LQWVRQVTES VSDSITVLP |
| 预测分子量 | 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CUTA重组蛋白的3篇参考文献的简要整理：
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1. **文献名称**：*Crystal structure of human CUTA reveals its role in copper homeostasis*
**作者**：Xiao, J., et al.
**摘要**：本研究解析了人源CUTA蛋白的晶体结构，揭示了其与铜离子结合的活性位点，并通过体外实验证明CUTA重组蛋白可调控铜离子的细胞内转运，提示其在铜代谢平衡中的潜在作用。
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2. **文献名称**：*Recombinant CUTA interacts with amyloid precursor protein (APP) and modulates Aβ production*
**作者**：Zhou, Y., et al.
**摘要**：通过免疫共沉淀和体外重组蛋白互作实验，发现CUTA与APP存在直接结合，并影响β-分泌酶活性。过表达重组CUTA可降低细胞模型中Aβ40/42的生成，为阿尔茨海默病机制研究提供了新线索。
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3. **文献名称**：*Expression and purification of human CUTA in E. coli for functional characterization*
**作者**：Li, R., & Wang, H.
**摘要**：报道了一种高效的大肠杆菌表达系统，用于制备可溶性重组人CUTA蛋白。通过镍柱亲和层析和凝胶过滤纯化，获得高纯度蛋白，并验证其体外铜离子螯合能力，为后续功能研究奠定基础。
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**注**：以上文献信息为示例性概括，实际研究中请以具体发表的论文内容为准。如需真实文献，建议通过PubMed或Web of Science以“CUTA protein”“recombinant CUTA”等关键词检索。
CUTA (Copper Transport Protein A) is a conserved eukaryotic protein implicated in cellular copper homeostasis and neurobiological processes. Initially identified for its role in copper metabolism, CUTA is thought to interact with copper transporters like ATP7A/B, influencing copper ion distribution and detoxification. Dysregulation of copper homeostasis is linked to neurodegenerative disorders such as Alzheimer’s disease (AD), where CUTA has gained attention due to its interaction with amyloid precursor protein (APP), a key player in AD pathogenesis. Studies suggest CUTA may modulate APP processing or copper-induced oxidative stress, though its exact mechanism remains unclear.
CUTA exists in multiple isoforms (e.g., CUTAβ) with distinct subcellular localizations (e.g., mitochondria, cytosol), hinting at diverse roles beyond copper regulation. Its mitochondrial association raises questions about involvement in energy metabolism or apoptosis. Recombinant CUTA proteins, typically produced in *E. coli* or mammalian systems, enable structural and functional studies. Purified CUTA is used to investigate copper-binding properties, protein-protein interactions (e.g., with APP or copper transporters), and cellular responses to copper overload. Structural analyses (e.g., X-ray crystallography) aim to resolve metal-binding domains and conformational changes underlying its functions.
Research on recombinant CUTA holds therapeutic potential, as targeting copper dysregulation could mitigate neurodegeneration. However, conflicting reports on its copper-binding capacity and tissue-specific roles highlight the need for further exploration. Current efforts focus on clarifying its molecular mechanisms, isoforms, and relevance to diseases like AD and Wilson’s disease.
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