| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HERC1 |
| Uniprot No | Q15751 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 3975-4360aa |
| 氨基酸序列 | GMDEQIMSWATSRPEDWHLGGKCDVYLWGAGRHGQLAEAGRNVMVPAAAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQGFVVTQLVTSCGSDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGEEVVQMSCGFKHSAVVTSDGKLFTFGNGDYGRLGLGNTSNKKLPERVTALEGYQIGQVACGLNHTLAVSADGSMVWAFGDGDYGKLGLGNSTAKSSPQKIDVLCGIGIKKVACGTQFSVALTKDGHVYTFGQDRLIGLPEGRARNHNRPQQIPVLAGVIIEDVAVGAEHTLALASNGDVYAWGSNSEGQLGLGHTNHVREPTLVTGLQGKNVRQISAGRCHSAAWTA |
| 预测分子量 | 48.1 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HERC1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Structural and functional analysis of the HERC1 ubiquitin ligase*
**作者**：Rosa JL, et al.
**摘要**：本研究通过重组表达纯化了HERC1蛋白的HECT结构域，解析了其晶体结构，并证明其具有泛素连接酶活性。实验发现HERC1通过调控mTOR信号通路参与细胞生长调控。
2. **文献名称**：*HERC1 regulates cell migration and invasion in melanoma via ubiquitination of Annexin A2*
**作者**：Bian Y, et al.
**摘要**：利用重组HERC1蛋白进行体外泛素化实验，发现其通过泛素化修饰膜联蛋白A2(Annexin A2)影响黑色素瘤细胞的迁移和侵袭能力，为靶向治疗提供了潜在分子机制。
3. **文献名称**：*Generation and characterization of a stable HERC1 knockout cell line using recombinant CRISPR/Cas9*
**作者**：Zhang L, et al.
**摘要**：通过重组CRISPR/Cas9技术构建HERC1基因敲除细胞系，结合重组HERC1蛋白回补实验，证实HERC1缺失导致溶酶体功能异常和自噬通路紊乱，提示其在细胞稳态中的关键作用。
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(注：以上文献信息为模拟示例，实际引用需以具体论文内容为准。)
**Background of HERC1 Recombinant Protein**
HERC1 (HECT and RLD domain-containing E3 ubiquitin-protein ligase 1) is a member of the HERC protein family, characterized by the presence of a HECT (Homologous to E6-AP C-Terminus) domain and RCC1 (Regulator of Chromosome Condensation 1)-like domains (RLD). It functions as an E3 ubiquitin ligase, playing a critical role in the ubiquitin-proteasome system by tagging specific substrate proteins for degradation. HERC1 is involved in diverse cellular processes, including cell cycle regulation, intracellular signaling, and protein trafficking.
Structurally, HERC1 contains a N-terminal RLD domain, which interacts with small GTPases like Rab proteins, and a C-terminal HECT domain responsible for its ubiquitin ligase activity. This dual-domain architecture allows HERC1 to act as a scaffold, linking GTPase signaling to ubiquitination pathways. Dysregulation of HERC1 has been implicated in neurological disorders, such as autism spectrum disorders and intellectual disabilities, as well as cancers. For instance, mutations in *HERC1* are linked to neurodevelopmental defects in mice and humans, while its overexpression or loss correlates with tumor progression in certain cancers.
Recombinant HERC1 protein is engineered for *in vitro* studies to dissect its biochemical functions, substrate interactions, and enzymatic mechanisms. Produced via heterologous expression systems (e.g., bacteria, mammalian cells), it is purified for use in ubiquitination assays, protein interaction studies, and structural analyses. Research on recombinant HERC1 aids in understanding its role in diseases and exploring therapeutic strategies targeting ubiquitination pathways. Recent studies also highlight its involvement in mTOR signaling, suggesting broader implications in metabolic regulation and aging.
Overall, HERC1 recombinant protein serves as a vital tool for unraveling the complex roles of ubiquitination in health and disease.
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