| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | CDC48 |
| Uniprot No | P54774 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 653-807aa |
| 氨基酸序列 | DEDSRHQIFKACLRKSPIAKNVDLRALARHTQGFSGADITEICQRACKYAIRENIEKDIERERKSRENPEAMDEDTVDDEVAEIKAAHFEESMKFARRSVSDADIRKYQAFAQTLQQSRGFGSEFRFPESGDRTTTGSDPFAASAGGADEDDLYS |
| 预测分子量 | 33.5 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CDC48(p97/VCP)重组蛋白的3篇代表性文献摘要：
1. **标题**：*Crystal structure of the AAA+ ATPase p97 reveals structural insights into a versatile adaptor protein*
**作者**：DeLaBarre, B., Brunger, A.T.
**摘要**：该研究解析了重组人源p97蛋白的晶体结构，揭示了其六聚体AAA+ ATP酶结构域构象变化，阐明了其通过ATP水解驱动底物解折叠的分子机制，为理解其与适配蛋白的互作提供了结构基础。
2. **标题**：*Distinct roles for the AAA ATPase NSF in regulated exocytosis and in the maintenance of vesicle pools in synaptic terminals*
**作者**：Morgan, J.R., Zhao, X., et al.
**摘要**：通过重组CDC48同源蛋白NSF的研究，揭示了其在突触囊泡融合中的关键作用，证明其ATP酶活性对SNARE复合体的解离和囊泡循环至关重要，并建立了体外重组系统验证功能。
3. **标题**：*The AAA ATPase Cdc48/p97 functions as a processive protein remodeling machine*
**作者**：Bodnar, N.O., Rapoport, T.A.
**摘要**：利用重组酵母Cdc48蛋白进行单分子实验，证明其通过连续ATP水解驱动泛素化底物的定向解折叠，并揭示了其与辅因子Ufd1-Npl4复合物协同工作的分子机制。
*注：实际文献需通过PubMed/Google Scholar检索最新成果。上述摘要基于领域经典研究方向概括，作者与标题为示意性内容，建议通过关键词“CDC48/p97 recombinant structural analysis/mechanism”查阅具体文献。*
**Background of CDC48 Recombinant Protein**
CDC48. also known as p97 or VCP (Valosin-Containing Protein) in mammals, is a highly conserved AAA+ (ATPases Associated with Diverse Cellular Activities) ATPase critical for multiple cellular processes. It plays a central role in ubiquitin-dependent protein quality control, endoplasmic reticulum-associated degradation (ERAD), membrane fusion, and cell cycle regulation. Structurally, CDC48 forms a hexameric ring-shaped complex, with each subunit containing two AAA+ ATPase domains (D1 and D2) and an N-terminal domain that recruits cofactors and substrates.
The protein functions as a molecular "segregase," using ATP hydrolysis to disassemble protein complexes or extract ubiquitinated substrates from membranes or macromolecular structures. This activity is tightly regulated by adaptor proteins, such as UFD1-NPL4 or PNGase, which determine substrate specificity and functional outcomes. Dysregulation of CDC48/p97 is linked to neurodegenerative diseases (e.g., IBMPFD, ALS), cancer, and viral infection mechanisms.
Recombinant CDC48 proteins are engineered for in vitro studies to dissect its biochemical mechanisms, interactions, and structural dynamics. These proteins are typically expressed in systems like *E. coli* or insect cells, purified via affinity tags (e.g., His-tag), and validated for ATPase activity. Recombinant variants, including disease-associated mutants (e.g., R155H, A232E), enable research into pathological mechanisms. Applications range from reconstituting ubiquitin-proteasome system components to screening therapeutic inhibitors targeting its ATPase activity.
Overall, CDC48 recombinant tools are indispensable for advancing understanding of cellular proteostasis and developing therapies for CDC48-related disorders.
×
