| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EDEM2 |
| Uniprot No | Q9BV94 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-492aa |
| 氨基酸序列 | MPFRLLIPLG LLCALLPQHH GAPGPDGSAP DPAHYRERVK AMFYHAYDSY LENAFPFDEL RPLTCDGHD TWGSFSLTLI DALDTLLILG NVSEFQRVVE VLQDSVDFDI DVNASVFETN IRVVGGLLS AHLLSKKAGV EVEAGWPCSG PLLRMAEEAA RKLLPAFQTP TGMPYGTVNL LHGVNPGET PVTCTAGIGT FIVEFATLSS LTGDPVFEDV ARVALMRLWE SRSDIGLVGN HIDVLTGKW VAQDAGIGAG VDSYFEYLVK GAILLQDKKL MAMFLEYNKA IRNYTRFDDW YLWVQMYKG TVSMPVFQSL EAYWPGLQSL IGDIDNAMRT FLNYYTVWKQ FGGLPEFYNI PQGYTVEKR EGYPLRPELI ESAMYLYRAT GDPTLLELGR DAVESIEKIS KVECGFATIK DLRDHKLDN RMESFFLAET VKYLYLLFDP TNFIHNNGST FDAVITPYGE CILGAGGYIF NTEAHPIDP AALHCCQRLK |
| 预测分子量 | 54 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EDEM2重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step*
**作者**：Hirao, K., et al.
**摘要**：该研究揭示了EDEM2作为α-1.2-甘露糖苷酶，通过剪切错误折叠糖蛋白上的N-聚糖甘露糖残基(Man8至Man7)，启动内质网相关降解(ERAD)过程。实验通过重组EDEM2蛋白的体外酶活分析，证实其直接参与甘露糖修剪，并证明其功能依赖于ERAD复合物组分OS9/SEL1L。
2. **文献名称**：*A novel ER α-mannosidase-like protein accelerates ER-associated degradation*
**作者**：Mast, S.W., et al.
**摘要**：本研究首次报道EDEM2作为内质网定位的甘露糖苷酶样蛋白，通过重组蛋白表达和体外酶活实验，证明其能加速错误折叠蛋白的降解。研究还发现EDEM2与ERAD调控分子如ERManI存在功能互补，并通过基因敲除实验验证其在细胞ERAD通路中的必要性。
3. **文献名称**：*EDEM2 regulates ERAD by enhancing the interaction of ER chaperones with ERAD components*
**作者**：Shenkman, M., et al.
**摘要**：该研究利用重组EDEM2蛋白进行体外结合实验，发现EDEM2通过其MRH结构域与内质网分子伴侣(如BiP)及ERAD衔接蛋白(如Sel1L)相互作用，从而促进错误折叠蛋白从伴侣系统向降解机器的传递。研究进一步通过结构生物学手段解析了关键相互作用界面。
4. **文献名称**：*Recombinant EDEM2 production in mammalian cells enables functional characterization of its role in ER stress*
**作者**：Ninagawa, S., et al.
**摘要**：文章建立了哺乳动物细胞中重组EDEM2的高效表达纯化系统，并利用该蛋白进行功能分析，发现EDEM2在未折叠蛋白反应(UPR)中通过IRE1-XBP1通路被诱导表达，且其过表达可显著增强细胞对ER应激的耐受能力。
**Background of EDEM2 Recombinant Protein**
EDEM2 (ER-degradation enhancing alpha-mannosidase-like protein 2) is a key player in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, a quality control system that identifies and targets misfolded glycoproteins for proteasomal degradation. Structurally, EDEM2 belongs to the glycosyl hydrolase family 47 (GH47), sharing homology with α1.2-mannosidases but lacking enzymatic activity in some species. Instead, it acts as a lectin-like chaperone, recognizing high-mannose oligosaccharides on misfolded glycoproteins to initiate their ERAD-mediated disposal.
The ERAD process is critical for maintaining cellular proteostasis. EDEM2 accelerates the clearance of terminally misfolded proteins by extracting them from the calnexin/calreticulin folding cycle and transferring them to downstream ERAD components, such as OS-9. XTP3-B, and the SEL1L-HRD1 ubiquitin ligase complex. Unlike its homologs EDEM1 and EDEM3. EDEM2 is proposed to act earlier in the ERAD pathway, possibly by trimming specific mannose residues to expose degradation signals.
Recombinant EDEM2 protein is produced via heterologous expression systems (e.g., mammalian, insect, or bacterial cells) for functional studies. Its purification often involves affinity chromatography tags (e.g., His-tag) followed by biochemical validation (e.g., SDS-PAGE, Western blot). Research applications include in vitro reconstitution of ERAD steps, structural analysis of substrate recognition, and disease modeling (e.g., neurodegenerative disorders linked to protein misfolding).
EDEM2’s role in diseases like alpha-1 antitrypsin deficiency or neurodegeneration underscores its therapeutic potential. Studying recombinant EDEM2 enhances understanding of ERAD mechanisms and may inform strategies to modulate proteostasis in pathological conditions.
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