| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | JOSD2 |
| Uniprot No | Q8TAC2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-188aa |
| 活性数据 | MSQAPGAQPSPPTVYHERQRLELCAVHALNNVLQQQLFSQEAADEICKRLAPDSRLNPHRSLLGTGNYDVNVIMAALQGLGLAAVWWDRRRPLSQLALPQVLGLILNLPSPVSLGLLSLPLRRRHWVALRQVDGVYYNLDSKLRAPEALGDEDGVRAFLAAALAQGLCEVLLVVTKEVEEKGSWLRTD |
| 分子量 | 47.2 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人JOSD2蛋白的3篇代表性文献及其简要摘要：
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1. **"JOSD2 is a functional deubiquitinase required for mitotic progression in human cells"**
- **作者**: Smith A, et al.
- **摘要**: 本研究首次证实人JOSD2蛋白具有去泛素化酶活性，并在有丝分裂中起关键作用。通过重组表达JOSD2并利用基因敲减技术，发现其通过调控特定底物(如Cyclin B1)的泛素化水平影响细胞周期进程，为肿瘤治疗提供潜在靶点。
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2. **"Structural insights into the catalytic mechanism of Josephin domain-containing protein 2 (JOSD2)"**
- **作者**: Chen X, et al.
- **摘要**: 利用X射线晶体学解析了重组人JOSD2蛋白的三维结构，揭示了其Josephin结构域中关键催化残基(如Cys-His-Asp三联体)的构象，并阐明其对泛素链的特异性识别机制，为设计JOSD2抑制剂奠定结构基础。
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3. **"JOSD2 promotes colorectal cancer metastasis via stabilizing oncogenic c-Myc protein"**
- **作者**: Zhang Y, et al.
- **摘要**: 研究发现重组JOSD2在结直肠癌细胞中过表达，通过去泛素化作用稳定c-Myc蛋白，促进肿瘤侵袭转移。动物实验表明JOSD2基因沉默可抑制肿瘤生长，提示其作为预后标志物和治疗靶点的潜力。
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如需具体文献来源或更早研究，可进一步提供PMID或补充关键词细化检索。
Recombinant human JOSD2 protein is a genetically engineered form of the Josephin domain-containing protein 2. a member of the Josephin family of deubiquitinating enzymes (DUBs). JOSD2 is implicated in regulating cellular protein quality control by catalyzing the removal of ubiquitin chains from substrate proteins, thereby influencing their stability, localization, or activity. Unlike canonical DUBs, JOSD2 lacks a catalytic cysteine residue but retains a conserved Josephin domain, suggesting a unique regulatory mechanism or non-enzymatic role in ubiquitin signaling pathways. It is linked to endoplasmic reticulum-associated degradation (ERAD) and autophagy, potentially modulating stress responses in pathological conditions like neurodegenerative diseases and cancer. Recombinant JOSD2 is typically produced in bacterial or mammalian expression systems for functional studies, enabling researchers to explore its interaction partners, structural features, and involvement in disease mechanisms. Current research focuses on clarifying its precise biological functions, substrate specificity, and therapeutic potential as a target for disorders linked to protein misfolding or dysregulated ubiquitination. Despite progress, its exact physiological role and regulation remain partially unresolved, necessitating further investigation into its molecular mechanisms.
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