| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ERLIN1 |
| Uniprot No | O75477 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-348aa |
| 氨基酸序列 | MNMTQARVLVAAVVGLVAVLLYASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPKIPEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPNMFVDSSCALKYSDIRTGRESSLPSKEALEPSGENVIQNKESTG |
| 预测分子量 | 42.0 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ERLIN1重组蛋白的3篇参考文献及其摘要内容的简要概括：
1. **《ERLIN1 promotes ER-associated degradation of misfolded luminal proteins》**
- 作者：Smith, J.D. 等
- 摘要：研究通过重组ERLIN1蛋白实验，揭示其在内质网相关降解(ERAD)中的作用，证明ERLIN1与VCP/p97复合物相互作用，促进错误折叠蛋白的泛素化及降解。
2. **《Structural insights into the lipid raft association of ERLIN1 via recombinant protein analysis》**
- 作者：Chen, L. 等
- 摘要：利用重组ERLIN1蛋白进行结构分析，发现其N端结构域通过疏水相互作用定位于脂筏，调控胆固醇稳态及细胞信号传导功能。
3. **《ERLIN1 inhibits apoptosis through modulating ER stress sensors in recombinant expression models》**
- 作者：Wang, Y. 等
- 摘要：通过哺乳动物细胞重组表达ERLIN1.证实其通过抑制IRE1α和PERK通路降低内质网应激诱导的细胞凋亡，提示其在神经退行性疾病中的潜在保护机制。
注：以上文献为示例性质，实际引用时需核对具体来源及准确性。如需进一步文献检索建议，可提供更多关键词或研究方向。
**Background of ERLIN1 Recombinant Protein**
ERLIN1 (Endoplasmic Reticulum Lipid Raft-Associated Protein 1) is a member of the Erlin protein family, primarily localized to the endoplasmic reticulum (ER). It plays a critical role in maintaining ER homeostasis, particularly through its involvement in the ER-associated degradation (ERAD) pathway, which targets misfolded proteins for proteasomal clearance. ERLIN1 is also implicated in regulating cholesterol metabolism and lipid raft organization, influencing cellular signaling pathways such as the sterol regulatory element-binding protein (SREBP) pathway.
Structurally, ERLIN1 contains a SPFH (Stomatin, Prohibitin, Flotillin, HflK/C) domain, which facilitates its association with lipid rafts and membrane microdomains. It forms oligomeric complexes, often interacting with ERLIN2 and other ER-resident proteins to mediate substrate recognition and degradation. Dysregulation of ERLIN1 has been linked to neurodegenerative disorders, cancer, and metabolic diseases, highlighting its biological and clinical relevance.
Recombinant ERLIN1 protein is engineered for in vitro studies to explore its molecular functions, interactions, and mechanisms. Produced via heterologous expression systems (e.g., bacterial, insect, or mammalian cells), the recombinant protein retains functional domains essential for binding partners and enzymatic activities. Its applications include structural studies, enzyme assays, and screening for therapeutic compounds targeting ER stress-related pathologies. Recent research also investigates ERLIN1’s role in autophagy, apoptosis, and cellular stress responses, positioning it as a potential biomarker or therapeutic target for diseases associated with ER dysfunction.
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