| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BK |
| Uniprot No | P46663 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-353aa |
| 氨基酸序列 | MASSWPPLELQSSNQSQLFPQNATACDNAPEAWDLLHRVLPTFIISICFFGLLGNLFVLLVFLLPRRQLNVAEIYLANLAASDLVFVLGLPFWAENIWNQFNWPFGALLCRVINGVIKANLFISIFLVVAISQDRYRVLVHPMASRRQQRRRQARVTCVLIWVVGGLLSIPTFLLRSIQAVPDLNITACILLLPHEAWHFARIVELNILGFLLPLAAIVFFNYHILASLRTREEVSRTRCGGRKDSKTTALILTLVVAFLVCWAPYHFFAFLEFLFQVQAVRGCFWEDFIDLGLQLANFFAFTNSSLNPVIYVFVGRLFRTKVWELYKQCTPKSLAPISSSHRKEIFQLFWRN |
| 预测分子量 | 40,4 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BK重组蛋白的3-4篇参考文献及其简要摘要：
---
1. **文献名称**：*"Crystal Structure of the Human BK Channel Calcium-Binding Domain in Complex with Calcium and Calmodulin"*
**作者**：Yuan, P., Leonetti, M.D., Hsiung, Y., & MacKinnon, R.
**摘要**：该研究通过X射线晶体学解析了人源BK通道钙结合结构域与钙离子及钙调蛋白的复合物结构，揭示了BK通道通过钙离子依赖性构象变化调控通道活性的分子机制，为理解其电压和钙双重门控特性提供了结构基础。
---
2. **文献名称**：*"Voltage-dependent gating of BK channels: experimental analysis and theoretical models"*
**作者**：Horrigan, F.T., & Aldrich, R.W.
**摘要**：作者通过重组BK通道蛋白的电生理实验，结合数学模型，提出了BK通道电压依赖性的门控机制假说，揭示了其独特的电压传感结构域与孔道结构协同作用的动力学特征。
---
3. **文献名称**：*"Functional role of the β1-subunit in BK channel regulation revealed by a dominant-negative mutation"*
**作者**：Niu, X., Qian, X., & Magleby, K.L.
**摘要**：该研究利用重组BK通道与β1亚基共表达系统，发现β1亚基通过调节通道的钙敏感性和电压依赖性显著影响BK通道的激活特性，为靶向β亚基的药物设计提供了理论依据。
---
4. **文献名称**：*"Alternative splicing of the BK channel gene alters channel function and pharmacology"*
**作者**：Savalli, N., Kondratiev, A., & Toro, L.
**摘要**：通过重组表达不同剪接变体的BK通道蛋白，研究发现特定外显子的可变剪接显著改变通道的动力学特性及对毒素抑制剂(如iberiotoxin)的敏感性，提示剪接变体在组织特异性功能中的重要性。
---
以上文献涵盖了BK重组蛋白的结构解析、门控机制、亚基调控及剪接变体功能差异等研究方向，均以重组蛋白技术为核心实验手段。
**Background of BK Recombinant Protein**
BK recombinant protein refers to a bioengineered form of the BK virus large tumor antigen (LTAg), a key regulatory protein encoded by the polyomavirus BK (BKV). BKV is a member of the *Polyomaviridae* family, commonly latent in human populations, with primary infections typically occurring in childhood. Reactivation of BKV, particularly in immunocompromised individuals (e.g., organ transplant recipients), is linked to severe complications such as nephropathy and hemorrhagic cystitis.
The BK recombinant protein is produced using recombinant DNA technology, where the LTAg gene is cloned into expression vectors (e.g., bacterial, insect, or mammalian systems) to enable large-scale protein synthesis. LTAg plays a critical role in viral replication by binding to host cell DNA and modulating cellular machinery to promote viral DNA synthesis. Its interactions with tumor suppressor proteins (e.g., p53. pRb) also contribute to oncogenic potential, making it a subject of interest in virology and cancer research.
Researchers utilize BK recombinant protein to study viral pathogenesis, host immune responses, and mechanisms of viral latency/reactivation. It serves as a tool for developing diagnostic assays, antiviral therapies, and vaccines. Additionally, its ability to disrupt cell cycle regulation provides insights into cellular transformation processes.
Despite its utility, challenges remain in ensuring protein stability, proper post-translational modifications, and minimizing batch-to-batch variability during production. Ongoing studies aim to optimize expression systems and functional assays to enhance its applicability in both basic and clinical research.
In summary, BK recombinant protein is a vital resource for understanding BKV biology and its clinical implications, bridging virology, immunology, and oncology.
×
