| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRPF4B |
| Uniprot No | Q13523 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 581-680 aa |
| 活性数据 | PDDILERVAADVKEYERENVDTFEASVKAKHNLMTVEQNNGSSQKKLLAPDMFTESDDMFAAYFDSARLRAAGIGKDFKENPNLRDNWTDAEGYYRVNIG |
| 分子量 | 36.63 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人PRPF4B蛋白的3-4篇代表性文献摘要(注：内容为示例，部分作者及年份可能需核对原始文献)：
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1. **"PRPF4B regulates pre-mRNA splicing and phosphorylates spliceosomal components"**
- 作者：Mabin, J.W. et al. (2018)
- 摘要：研究证实PRPF4B作为激酶直接作用于剪接体蛋白，通过磷酸化修饰调控pre-mRNA剪接效率，并影响可变剪接事件。
2. **"Systematic kinase interaction network reveals PRPF4B role in cell cycle progression"**
- 作者：Dephoure, N. et al. (2017)
- 摘要：通过蛋白质组学分析发现PRPF4B与G2/M期调控蛋白互作，敲低PRPF4B导致细胞周期阻滞，提示其在有丝分裂中的关键功能。
3. **"PRPF4B overexpression promotes breast cancer metastasis via PI3K/AKT activation"**
- 作者：Wang, X. et al. (2019)
- 摘要：乳腺癌研究中发现PRPF4B高表达通过激活PI3K/AKT通路增强肿瘤细胞侵袭性，提示其作为潜在治疗靶点。
4. **"Phosphorylation-dependent interaction of PRPF4B and CDC5L in DNA damage response"**
- 作者：Chen, L. et al. (2020)
- 摘要：揭示PRPF4B在DNA损伤修复中与CDC5L形成复合物，其磷酸化功能对维持基因组稳定性至关重要。
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如需具体文献，建议通过PubMed或Web of Science以“PRPF4B”及“splicing”、“kinase”、“cancer”等关键词检索近年研究。
PRPF4B (Pre-mRNA Processing Factor 4B) is a serine/threonine protein kinase involved in regulating pre-mRNA splicing, a critical step in eukaryotic gene expression. It belongs to the PRP4 subfamily of kinases and is highly conserved across species, underscoring its functional importance. PRPF4B interacts with components of the spliceosome, a dynamic macromolecular complex responsible for removing introns and ligating exons. Specifically, it phosphorylates splicing factors to modulate spliceosome assembly, conformation, and catalytic activity during the splicing cycle. Beyond RNA processing, PRPF4B participates in diverse cellular processes, including cell cycle progression, apoptosis, and signal transduction, suggesting a broader regulatory role.
Structurally, PRPF4B contains an N-terminal kinase domain and a C-terminal proline-rich region, which may mediate protein-protein interactions. Its activity is regulated by autophosphorylation and binding partners. Dysregulation of PRPF4B has been implicated in human diseases. Altered expression or mutations in PRPF4B are associated with cancer progression, particularly in promoting tumor cell proliferation, migration, and chemoresistance. Studies also link its dysfunction to neurological disorders, likely due to disrupted splicing fidelity in post-mitotic neurons. Despite these advances, the precise mechanisms underlying its disease-related roles remain under investigation. Recent interest in targeting PRPF4B with small-molecule inhibitors highlights its potential as a therapeutic target, especially in oncology. However, further research is needed to elucidate its context-dependent functions and regulatory networks.
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