| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | YOD1 |
| Uniprot No | Q5VVQ6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-348aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMFGPAKGRHFGVHPAPGFPGGVSQQAA GTKAGPAGAWPVGSRTDTMWRLRCKAKDGTHVLQGLSSRTRVRELQGQIA AITGIAPGGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIIEEDQTRP RSSPAFTKRGASSYVRETLPVLTRTVVPADNSCLFTSVYYVVEGGVLNPA CAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEISI LSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDGIHYDPLQRNFPD PDTPPLTIFSSNDDIVLVQALELADEARRRRQFTDVNRFTLRCMVCQKGL TGQAEAREHAKETGHTNFGEV |
| 预测分子量 | 41 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YOD1重组蛋白的3-4条参考文献示例(注：以下内容为虚构，仅用于格式演示)：
1. **文献名称**：*YOD1-mediated deubiquitination promotes endoplasmic reticulum-associated degradation of misfolded proteins*
**作者**：Ernst, R., Ploegh, H.L., et al.
**摘要**：该研究利用重组YOD1蛋白，揭示了其在内质网相关降解(ERAD)中的关键作用。通过体外酶活实验，证明YOD1通过剪切K48连接的泛素链，协助错误折叠蛋白从内质网逆向转运至胞质，最终被蛋白酶体降解。
2. **文献名称**：*Structural basis of ubiquitin chain recognition and hydrolysis by YOD1 deubiquitinase*
**作者**：Christis, C., Schulman, B.A., et al.
**摘要**：通过重组表达纯化人源YOD1蛋白并进行晶体结构解析，研究发现其OTU结构域特异性结合K63和K48混合型泛素链，揭示了YOD1底物选择性的分子机制及催化活性调控的关键位点。
3. **文献名称**：*YOD1 regulates mitochondrial apoptosis by modulating the stability of pro-survival BCL-2 proteins*
**作者**：Buchanan, B.W., Youle, R.J., et al.
**摘要**：该研究使用重组YOD1蛋白进行体外泛素化/去泛素化分析，发现YOD1通过去泛素化BCL-2家族蛋白调控其稳定性，从而影响线粒体途径的细胞凋亡过程。
4. **文献名称**：*YOD1 interacts with p97/VCP to coordinate the processing of ubiquitinated substrates*
**作者**：Hörnstein, M., Meyer, H., et al.
**摘要**：通过重组蛋白互作实验，证明YOD1与ATP酶p97/VCP形成复合物，协同调控泛素化底物的去折叠与转运，为理解蛋白酶体依赖性蛋白质量控制提供了新机制。
(注：以上文献为模拟生成，实际研究中请参考真实发表的学术论文。)
YOD1. also known as ubiquitin thioesterase OTU1. is a deubiquitinating enzyme (DUB) belonging to the ovarian tumor (OTU) family of proteases. It plays a critical role in regulating cellular protein homeostasis, particularly in endoplasmic reticulum-associated degradation (ERAD), a quality control pathway that identifies and eliminates misfolded proteins in the endoplasmic reticulum (ER). YOD1 functions by cleaving ubiquitin chains attached to substrate proteins, facilitating their retrotranslocation to the cytosol for proteasomal degradation. Its activity is tightly linked to the AAA+ ATPase p97 (VCP), which coordinates substrate handling during ERAD. Structurally, YOD1 contains an N-terminal OTU domain responsible for catalytic activity and a C-terminal ubiquitin-associated (UBA) domain that mediates interactions with ubiquitin or ubiquitinated substrates.
Recombinant YOD1 protein is engineered for in vitro studies to dissect its enzymatic mechanisms, substrate specificity, and regulatory roles. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), it retains deubiquitinase activity and is widely used in biochemical assays, structural studies, and drug discovery. Researchers employ it to explore how YOD1 modulates ubiquitin signaling dynamics, particularly in stress responses, apoptosis, and autophagy. Dysregulation of YOD1 has been implicated in diseases such as neurodegeneration and cancer, making it a potential therapeutic target. For example, aberrant YOD1 activity may contribute to protein aggregation in Alzheimer’s or Parkinson’s disease, while its overexpression in certain cancers could promote cell survival. Current research focuses on identifying small-molecule inhibitors or activators to modulate YOD1 function, aiming to develop targeted therapies. The recombinant protein’s availability accelerates mechanistic insights into ERAD and broader ubiquitin-dependent processes, bridging molecular biology with translational medicine.
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