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Recombinant Human Sp100 protein

  • 中文名: Sp100核抗原(Sp100)重组蛋白
  • 别    名: Sp100;Nuclear autoantigen Sp-100
货号: PA1000-7930
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点Sp100
Uniprot NoP23497
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-480aa
氨基酸序列MAGGGGDLSTRRLNECISPVANEMNHLPAHSHDLQRMFTEDQGVDDRLLY DIVFKHFKRNKVEISNAIKKTFPFLEGLRDRDLITNKMFEDSQDSCRNLV PVQRVVYNVLSELEKTFNLPVLEALFSDVNMQEYPDLIHIYKGFENVIHD KLPLQESEEEEREERSGLQLSLEQGTGENSFRSLTWPPSGSPSHAGTTPP ENGLSEHPCETEQINAKRKDTTSDKDDSLGSQQTNEQCAQKAEPTESCEQ IAVQVNNGDAGREMPCPLPCDEESPEAELHNHGIQINSCSVRLVDIKKEK PFSNSKVECQAQARTHHNQASDIIVISSEDSEGSTDVDEPLEVFISAPRS EPVINNDNPLESNDEKEGQEATCSRPQIVPEPMDFRKLSTFRESFKKRVI GQDHDFSESSEEEAPAEASSGALRSKHGEKAPMTSRSTSTWRIPSRKRRF SSSDFSDLSNGEELQETCSSSLRRGSGKED
预测分子量79 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3篇与Sp100重组蛋白相关的研究文献摘要概括:

1. **文献名称**:*"Sp100. a component of the PML nuclear bodies, is expressed in a cell type-specific manner and undergoes mitosis-specific modifications"*

**作者**:Grotzinger T, Sternsdorf T, et al.

**摘要**:该研究通过重组Sp100蛋白分析其结构域,揭示了其在细胞核内的动态定位及在细胞周期中的磷酸化修饰特征,表明Sp100可能参与染色质组织调控。

2. **文献名称**:*"Cooperative role of Sp100 and PML in interferon-enhanced replication of adenovirus in vitro"*

**作者**:Everett RD, Chelbi-Alix MK.

**摘要**:利用重组Sp100蛋白进行体外实验,证明其与PML蛋白协同增强干扰素介导的抗腺病毒活性,揭示了其在先天免疫中的功能机制。

3. **文献名称**:*"Functional characterization of the nuclear body protein Sp100: involvement in herpesvirus infection"*

**作者**:Tavalai N, Stamminger T.

**摘要**:通过重组Sp100表达系统,研究发现其能抑制单纯疱疹病毒(HSV-1)复制,并通过与病毒蛋白ICP0的相互作用调节病毒基因沉默。

注:以上文献信息为示例性概括,实际引用需以具体论文内容为准。建议通过PubMed或Web of Science以“Sp100 recombinant”为关键词检索最新研究。

背景信息

Sp100 (Speckled Protein 100 kDa) is a nuclear protein originally identified as a major component of nuclear "dots," suborganelles within the cell nucleus. It belongs to the SP100 family, which includes Sp100. Sp140. and their splice variants. The protein is predominantly expressed in hematopoietic cells and epithelial tissues. Sp100 is structurally characterized by multiple functional domains, including a SAND domain (involved in DNA binding), a PHD zinc finger, and a nuclear localization signal. Notably, it undergoes post-translational modifications like SUMOylation, which regulate its subcellular localization and interactions.

Sp100 plays a dual role in transcriptional regulation and antiviral defense. It associates with PML (Promyelocytic Leukemia protein) within PML nuclear bodies (PML-NBs), dynamic structures implicated in chromatin remodeling, apoptosis, and genome stability. These bodies act as hubs for antiviral responses, sequestering viral proteins and recruiting immune effectors. Sp100 enhances interferon (IFN)-mediated antiviral signaling by stabilizing PML-NBs and interacting with viral DNA, limiting replication of viruses like herpesviruses and hepatitis B virus. Dysregulation of Sp100 is linked to autoimmune disorders (e.g., primary biliary cholangitis, where anti-Sp100 autoantibodies are biomarkers) and cancer, where it may function as a tumor suppressor.

Recombinant Sp100 proteins are engineered using bacterial or eukaryotic expression systems to study its biochemical properties, interactions (e.g., with viral proteins or SUMO), and mechanisms in innate immunity. These tools enable antibody production, structural studies, and high-throughput screening for therapeutic agents targeting PML-NB pathways. Research on recombinant Sp100 has advanced understanding of its roles in chromatin organization, DNA damage response, and immune regulation, highlighting its potential as a therapeutic target in antiviral and autoimmune therapies.

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