| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DBC1 |
| Uniprot No | O60477 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-320aa |
| 氨基酸序列 | MNWRFVGLLYFLFIWGRISVQPSHQEPAGTDQHVSKEFDWLISDRGPFHHSRSYLSFVERHRQGFTTRYKIYREFARWKVRNTAIERRDLVRHPVPLMPEFQRSIRLLGRRPTTQQFIDTIIKKYGTHLLISATLGGEEALTMYMDKSRLDRKSGNATQSVEALHQLASSYFVDRDGTMRRLHEIQISTGAIKVTETRTGPLGCNSYDNLDSVSSVLLQSTESKLHLQGLQIIFPQYLQEKFVQSALSYIMCNGEGEYLCQNSQCRCQCAEEFPQCNCPITDIQIMEYTLANMAKSWAEAYKDLENSGRESHSVPLHEWP |
| 分子量 | 60.94 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DBC1蛋白的3篇代表性文献及其摘要内容(基于已有研究推测，非真实文献，供参考)：
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1. **文献名称**：*"Structural basis for DBC1-mediated regulation of SIRT1 deacetylase activity"*
**作者**：Li, Y. et al.
**摘要**：本研究利用重组人DBC1蛋白和SIRT1进行体外互作实验，发现DBC1通过直接结合抑制SIRT1的去乙酰化酶活性。通过晶体结构解析，揭示了DBC1的N端结构域与SIRT1催化核心的结合机制，为代谢相关疾病治疗提供了分子基础。
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2. **文献名称**：*"Efficient production of recombinant human DBC1 in insect cells for functional assays"*
**作者**：Zhang, H. et al.
**摘要**：报道了在昆虫细胞-杆状病毒系统中高效表达重组人DBC1蛋白，并通过多步层析纯化获得高纯度蛋白。功能验证显示，重组DBC1可体外结合p53并调控其稳定性，证明其在癌症研究中的应用潜力。
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3. **文献名称**：*"DBC1 acts as a tumor suppressor via modulating HDAC3 activity in colorectal cancer"*
**作者**：Wang, J. et al.
**摘要**：利用重组DBC1蛋白验证其与HDAC3的相互作用，发现DBC1通过抑制HDAC3去乙酰化活性，激活抑癌基因表达。研究揭示了DBC1在结直肠癌中的表观遗传调控机制。
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(注：若需真实文献，建议在PubMed或Web of Science以关键词“recombinant DBC1 protein”或“DBC1 purification”检索近年研究。)
DBC1 (Deleted in Breast Cancer 1), also known as CCAR2 or KIAA1967. is a nuclear protein initially identified as a putative tumor suppressor due to its genomic deletion in breast cancer. Later studies revealed its dual role in cancer progression, acting as both an oncogene and tumor suppressor depending on cellular context. DBC1 plays critical roles in epigenetic regulation, DNA repair, apoptosis, and metabolic pathways by interacting with key regulators such as SIRT1. HDAC3. SUV39H1. and BRCA1. Its N-terminal domain contains nuclear localization signals, while the central coiled-coil region and C-terminal SSF motif mediate protein-protein interactions.
Recombinant human DBC1 protein is engineered via molecular cloning, typically expressed in *E. coli* or eukaryotic systems for functional studies. This purified protein enables researchers to investigate DBC1's biochemical properties, enzymatic activities, and binding partners *in vitro*. It has become essential for studying DBC1's role in modulating deacetylase activities (e.g., SIRT1 inhibition affecting p53 activation), DNA damage response via PARP1 interaction, and circadian rhythm regulation through interactions with CLOCK proteins. Dysregulation of DBC1 is linked to cancers, neurodegenerative diseases, and metabolic disorders, making recombinant DBC1 valuable for drug discovery and mechanistic studies. Recent applications include screening small-molecule inhibitors targeting DBC1-mediated pathways and exploring its role in cellular senescence.
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