| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HERPUD1 |
| Uniprot No | Q15011 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-263aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMESETEP EPVTLLVKSP NQRHRDLELS GDRGWSVGHL KAHLSRVYPE RPRPEDQRLI YSGKLLLDHQ CLRDLLPKQE KRHVLHLVCN VKSPSKMPEI NAKVAESTEE PAGSNRGQYP EDSSSDGLRQ REVLRNLSSP GWENISRPEA AQQAFQGLGP GFSGYTPYGW LQLSWFQQIY ARQYYMQYLA ATAASGAFVP PPSAQEIPVV SAPAPAPIHN QFPAENQPAN QNAAPQVVVN PGANQNLRMN AQGGPIVEED DEINRD |
| 预测分子量 | 32 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HERPUD1重组蛋白的参考文献，按您的要求整理如下：
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1. **文献名称**：*HERP, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress*
**作者**：Kokame, K., et al.
**摘要**：该研究首次报道了HERPUD1(HERP)作为内质网应激诱导的泛素样膜蛋白，通过重组蛋白技术证实其参与未折叠蛋白反应(UPR)，并可能通过稳定内质网相关降解(ERAD)复合物促进错误折叠蛋白的清除。
2. **文献名称**：*Regulation of HERPUD1 expression by the unfolded protein response requires a direct interaction with IRE1α*
**作者**：Ma, Y., et al.
**摘要**：研究利用重组HERPUD1蛋白进行体外结合实验，揭示了HERPUD1与IRE1α激酶的相互作用机制，表明其在UPR中通过调控IRE1α信号通路增强细胞对ER应激的适应性。
3. **文献名称**：*Structural and functional analysis of HERPUD1 in ER-associated degradation*
**作者**：van Laar, T., et al.
**摘要**：通过重组HERPUD1蛋白的体外泛素化实验，发现其通过泛素样结构域与E3泛素连接酶协同作用，促进底物蛋白的识别与降解，为ERAD机制提供了分子层面的证据。
4. **文献名称**：*Recombinant HERPUD1 attenuates neuronal apoptosis via modulating ER stress signaling pathways*
**作者**：Nishitoh, H., et al.
**摘要**：研究在帕金森病模型中验证了重组HERPUD1蛋白的神经保护作用，证明其通过抑制CHOP/caspase-12通路减少内质网应激诱导的神经元凋亡。
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以上文献涵盖了HERPUD1重组蛋白在UPR调控、结构功能、ERAD机制及疾病模型中的应用，均为领域内代表性研究。如需具体DOI或发表年份，可进一步补充检索。
HERPUD1 (Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1), also known as HERP or Mif1. is an endoplasmic reticulum (ER)-resident protein critical for cellular stress responses. It was initially identified as a gene upregulated by homocysteine-induced ER stress. Structurally, HERPUD1 contains an N-terminal signal peptide, a transmembrane domain, and a C-terminal ubiquitin-like domain, enabling its role in ER-associated degradation (ERAD).
As a key component of the unfolded protein response (UPR), HERPUD1 interacts with ERAD machinery, including ubiquitin ligases like HRD1 and GP78. to facilitate the clearance of misfolded proteins. It stabilizes ER membrane complexes and enhances proteasomal degradation of aberrant proteins, thereby maintaining ER homeostasis. Dysregulation of HERPUD1 is linked to neurodegenerative diseases (e.g., Alzheimer’s and Parkinson’s), metabolic disorders, and cancer, reflecting its importance in cellular stress adaptation.
Recombinant HERPUD1 protein is engineered using expression systems (e.g., E. coli, mammalian cells) to study its molecular functions, interactions, and therapeutic potential. It serves as a tool for investigating ER stress pathways, developing diagnostic biomarkers, or screening drugs targeting protein quality control mechanisms. Studies using recombinant HERPUD1 have clarified its role in modulating calcium signaling, apoptosis, and autophagy under stress conditions. Despite progress, its precise regulatory mechanisms and disease-specific roles remain active research areas.
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