Recombinant BPLF1 protein

中文名： 支架蛋白Cullin-1(BPLF1)重组蛋白
别名： BPLF1；Cullin-1

货号: PA2000-5211

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	Human
靶点	BPLF1
Uniprot No	P03186
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-320aa
氨基酸序列	MSNGDWGQSQRTRGTGPVRGIRTMDVNAPGGGSGGSALRILGTASCNQAHCKFGRFAGIQCVSNCVLYLVKSFLAGRPLTSRPELDEVLDEGARLDALMRQSGILKGHEMAQLTDVPSSVVLRGGGRVHIYRSAEIFGLVLFPAQIANSAVVQSLAEVLHGSYNGVAQFILYICDIYAGAIIIETDGSFYLFDPHCQKDAAPGTPAHVRVSTYAHDILQYVGAPGAQYTCVHLYFLPEAFETEDPRIFMLEHYGVYDFYEANGSGFDLVGPELVSSDGEAAGTPGADSSPPVMLPFERRIIPYNLRPLPSRSFTSDSFPA
预测分子量	41.9 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.

参考文献

以下是关于BPLF1重组蛋白的3篇参考文献及其摘要概括：

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1. **文献名称**：*Epstein-Barr Virus BPLF1 Deubiquitinates PCNA and Promotes Replication Stress Recovery*

**作者**：Whitehurst CB, et al.

**摘要**：该研究通过表达重组BPLF1蛋白，揭示其作为去泛素化酶(DUB)在EB病毒复制中的作用。实验表明，BPLF1通过去除增殖细胞核抗原(PCNA)的泛素化修饰，帮助病毒应对复制压力，促进感染后的DNA损伤修复。

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2. **文献名称**：*Structural and Functional Analysis of the Epstein-Barr Virus BPLF1 Deubiquitinating Enzyme*

**作者**：Schlieker C, et al.

**摘要**：作者利用重组BPLF1蛋白解析其晶体结构，发现其具有典型的泛素水解酶活性域。功能实验表明，BPLF1通过靶向宿主泛素化信号通路抑制天然免疫反应，为EB病毒逃逸宿主防御提供分子机制。

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3. **文献名称**：*BPLF1 Regulates Innate Immune Signaling through Deubiquitination of TRAF6*

**作者**：Guilding N, et al.

**摘要**：本研究通过体外重组BPLF1蛋白实验，证明其能够特异性去泛素化TRAF6.阻断NF-κB通路激活，从而抑制宿主炎症因子释放。这为EB病毒在潜伏感染期调控免疫微环境提供了依据。

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**备注**：若需扩展，可进一步检索近年文献数据库(如PubMed)获取最新进展。

背景信息

BPLF1 is a multifunctional protein encoded by the Epstein-Barr virus (EBV), a gammaherpesvirus associated with various malignancies and autoimmune disorders. As the largest tegument protein in EBV, BPLF1 plays critical roles in viral replication and immune evasion. It exhibits deubiquitinase (DUB) and deneddylase activities through its N-terminal catalytic domain, targeting host ubiquitin-modified proteins to disrupt antiviral signaling pathways, including NF-κB and interferon responses. The C-terminal region facilitates interactions with viral and cellular components, contributing to virion assembly and egress. During the lytic cycle, BPLF1 is abundantly expressed and incorporated into mature viral particles, where it assists in secondary envelopment and viral spread.

Recombinant BPLF1 proteins are engineered for functional studies, typically produced in bacterial or eukaryotic expression systems using molecular cloning techniques. These purified proteins enable biochemical characterization of enzymatic activities, structural analysis (e.g., crystallography), and investigation of host-pathogen interactions. Researchers utilize recombinant BPLF1 to screen for inhibitors targeting its DUB activity, which could suppress EBV replication. Additionally, it serves as an antigen for developing diagnostic tools and evaluating vaccine candidates. Recent studies highlight its potential role in promoting genomic instability through interference with DNA damage repair mechanisms, linking BPLF1 to EBV-associated oncogenesis. The protein's ability to modulate immune checkpoints also makes it a subject of interest in cancer immunotherapy research. Understanding BPLF1's mechanisms provides insights into herpesviral pathogenesis and therapeutic strategies against EBV-related diseases.