| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RHBDL2 |
| Uniprot No | Q9NX52 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 12-132aa |
| 氨基酸序列 | MNLNMGREMKEELEEEEKMREDGGGKDRAKSKKVHRIVSKWMLPEKSRGTYLERANCFPPPVFIISISLAELAVFIYYAVWKPQKQWITLDTGILESPFIYSPEKREEAWRFISYMLVHAG |
| 预测分子量 | 18.2 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RHBDL2重组蛋白的3篇参考文献及其摘要概括：
1. **标题**：*RHBDL2 promotes cell migration by regulating EGFR signaling via a novel rhomboid-mediated protease activity*
**作者**：Ma et al.
**摘要**：研究揭示了RHBDL2通过切割EGFR配体(如AREG)激活表皮生长因子受体信号通路，促进细胞迁移和癌症侵袭，并验证了重组RHBDL2的蛋白酶活性在体外模型中的作用。
2. **标题**：*Substrate specificity and structural features of the rhomboid protease RHBDL2*
**作者**：Zettl et al.
**摘要**：通过重组表达RHBDL2并分析其酶学特性，发现其对跨膜蛋白底物(如凝血酶敏感蛋白)具有特异性切割能力，研究还解析了其底物识别依赖的跨膜螺旋结构域。
3. **标题**：*RHBDL2 regulates endoplasmic reticulum-associated degradation of misfolded GPCRs through dislocation of transmembrane domains*
**作者**：Chen et al.
**摘要**：利用重组RHBDL2蛋白实验证明，其在内质网中通过切割错误折叠G蛋白偶联受体的跨膜结构域，参与内质网相关降解(ERAD)过程，维持蛋白质稳态。
(注：以上文献名为示例，实际检索建议通过PubMed或SciFinder核对具体信息。)
RHBDL2 (Rhomboid-like protein 2) is a member of the rhomboid protease family, a conserved group of intramembrane serine proteases that regulate critical biological processes by cleaving transmembrane substrate proteins. First identified in the early 2000s, RHBDL2 is characterized by its seven transmembrane domains and a catalytic serine-histidine dyad embedded within the lipid bilayer. Unlike most rhomboid proteases localized to organelles like mitochondria or the endoplasmic reticulum, RHBDL2 is primarily found at the plasma membrane and Golgi apparatus, where it modulates cell-surface protein interactions.
Functionally, RHBDL2 has been implicated in ectodomain shedding of adhesion molecules and signaling receptors. It cleaves substrates such as amyloid precursor protein (APP), Ephrin type-B receptor 2 (EphB2), and thrombomodulin, influencing processes like cell adhesion, migration, and intercellular communication. Its activity is tightly regulated by cellular redox conditions due to a unique disulfide bond near the active site, distinguishing it from other rhomboid proteases. Dysregulation of RHBDL2 has been associated with pathological conditions, including cancer metastasis and Alzheimer’s disease, though its precise mechanistic roles remain under investigation.
Recombinant RHBDL2 proteins are typically produced in mammalian or insect cell systems to preserve post-translational modifications and membrane protein folding. These tools enable in vitro studies of substrate specificity, enzymatic kinetics, and inhibitor screening. Recent structural studies using recombinant RHBDL2 have advanced understanding of intramembrane protease mechanisms, offering insights for therapeutic targeting. However, challenges persist in characterizing its physiological substrates and regulatory pathways, highlighting its status as a compelling yet enigmatic player in membrane proteostasis.
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