| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UCHL1 |
| Uniprot No | P09936 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-220aa |
| 氨基酸序列 | QLKPMEINPEMLNKVLSRLGVAGQWRFVDVLGLEEESLGSVPAPACALLL LFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVAN NQDKLGFEDGSVLKQFLSETEKMSPEDRAKCFEKNEAIQAAHDAVAQEGQ CRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDTLLKDAAKVC REFTEREQGEVRFSAVALC |
| 预测分子量 | 26 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UCHL1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Expression, purification, and characterization of recombinant human UCHL1"*
**作者**：Liu Y. et al.
**摘要**：该研究报道了人源UCHL1重组蛋白在大肠杆菌中的高效表达和纯化方法，并验证了其水解泛素C端酯酶活性，为后续功能研究提供了基础材料。
2. **文献名称**：*"Structural basis for the dual enzyme activity of UCHL1 in ubiquitin processing"*
**作者**：Das C. et al.
**摘要**：通过X射线晶体学解析了重组UCHL1的分子结构，揭示了其同时具备水解酶与泛素连接酶活性的构象机制，解释了UCHL1在神经退行性疾病中的潜在作用。
3. **文献名称**：*"UCHL1 inhibition suppresses breast cancer progression via destabilizing EGFR"*
**作者**：Hussain S. et al.
**摘要**：研究利用重组UCHL1蛋白进行体外实验，发现其通过调控EGFR蛋白稳定性影响乳腺癌细胞增殖，提示UCHL1可能成为癌症治疗的靶点。
(注：以上文献为示例，实际引用时需核实具体信息。)
UCHL1 (ubiquitin carboxyl-terminal hydrolase L1), also known as PARK5. is a deubiquitinating enzyme belonging to the ubiquitin-specific protease family. It plays a critical role in the ubiquitin-proteasome system by hydrolyzing polyubiquitin chains or ubiquitin precursors, thereby regulating protein degradation, cellular homeostasis, and stress response. UCHL1 is predominantly expressed in neurons and testis, with high abundance in the brain, where it constitutes ~1-2% of total soluble proteins. Its enzymatic activity and non-catalytic functions are linked to synaptic plasticity, axonal transport, and mitochondrial dynamics.
Mutations or dysregulation of UCHL1 have been implicated in neurodegenerative disorders. The I93M mutation causes early-onset Parkinson’s disease (PD), while the S18Y polymorphism may confer PD resistance. Aberrant UCHL1 expression is also observed in Alzheimer’s disease, traumatic brain injury, and certain cancers, acting as either an oncogene or tumor suppressor depending on context. Its dual roles—promoting ubiquitin recycling while stabilizing specific substrates—highlight complex regulatory mechanisms.
Recombinant UCHL1 proteins are engineered using expression systems like E. coli or mammalian cells, often with tags (e.g., His, GST) for purification. These tools enable studies on enzyme kinetics, structure-function relationships (e.g., catalytic triad Cys90-His161-Asp176), and interactions with pathogenic proteins (α-synuclein, tau). Pharmaceutical interest focuses on developing UCHL1 inhibitors/modulators for neurodegeneration or cancer therapy. However, challenges persist in understanding its cell-type-specific roles and designing blood-brain barrier-penetrant compounds. As a potential biomarker, UCHL1 levels in biofluids are being explored for neurological disease diagnostics.
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