| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DNCL2A |
| Uniprot No | Q9NP97 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-96aa |
| 氨基酸序列 | VVNTEGIPIKSTMDNPTTTQYASLMHSFILKARSTVRDIDPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE |
| 分子量 | 33.99 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DNCL2A蛋白的模拟参考文献(注：以下内容为虚构示例，仅供学术参考)：
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1. **文献名称**：*Expression and Purification of Recombinant Human DNCL2A in Escherichia coli*
**作者**：Smith A.L., et al.
**摘要**：本研究成功构建了重组人DNCL2A蛋白的原核表达系统，优化了诱导表达条件，并采用Ni-NTA层析法实现了高效纯化。Western blot分析验证了蛋白特异性，体外实验证实其具有ATP酶活性，为后续功能研究奠定了基础。
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2. **文献名称**：*Functional Characterization of DNCL2A in Microtubule Dynamics*
**作者**：Chen H., Li R., Wang Y.
**摘要**：通过siRNA敲低和过表达实验，发现DNCL2A通过调控微管稳定性参与细胞分裂进程。重组蛋白的体外结合实验表明其直接与α/β微管蛋白相互作用，并依赖其C端结构域介导动力学变化，提示其在有丝分裂中的关键作用。
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3. **文献名称**：*DNCL2A Interactome Reveals Novel Binding Partners in Neuronal Cells*
**作者**：García M., et al.
**摘要**：利用免疫共沉淀联合质谱分析，鉴定了重组人DNCL2A蛋白在神经元细胞中的新型相互作用蛋白，包括突触囊泡运输相关蛋白Synaptophysin-1.研究提示DNCL2A可能参与突触可塑性和神经退行性疾病的病理过程。
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4. **文献名称**：*Dysregulation of DNCL2A in Hepatocellular Carcinoma and Its Therapeutic Implications*
**作者**：Tanaka K., et al.
**摘要**：在肝细胞癌组织样本中发现DNCL2A表达显著下调。体外实验表明，重组DNCL2A蛋白能够抑制癌细胞增殖并诱导G2/M期阻滞，提示其作为肿瘤抑制因子和潜在治疗靶点的可能性。
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注：以上文献及内容均为模拟生成，实际研究中需以真实数据库(如PubMed)为准。
Recombinant human DCNL2A (Defective in Cullin Neddylation 2A) protein is a key regulator involved in the neddylation pathway, primarily facilitating the activation of Cullin-RING E3 ubiquitin ligases (CRLs). DCNL2A acts as a cofactor that recruits and positions NEDD8. a ubiquitin-like protein, onto Cullin proteins via its conserved N-terminal domain. This post-translational modification, termed neddylation, is essential for CRL complex assembly and activity, enabling targeted ubiquitination of substrate proteins for proteasomal degradation.
The DCNL2A gene encodes a 302-amino acid protein containing a coiled-coil region and a C-terminal domain critical for Cullin binding. Dysregulation of DCNL2A has been implicated in various cancers and developmental disorders due to its role in controlling protein homeostasis, cell cycle progression, and stress responses. Recombinant DCNL2A is typically produced in Escherichia coli or mammalian expression systems, maintaining structural and functional integrity for biochemical studies.
Its applications span mechanistic studies of CRL regulation, drug discovery targeting neddylation pathways, and structural analysis of protein-protein interactions. Recent research focuses on developing DCNL2A inhibitors as potential anticancer agents, leveraging its crucial role in tumorigenesis through hyperactivation of CRL-mediated proteostasis.
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