纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | SRPK1 |
Uniprot No | Q96SB4 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-655aa |
氨基酸序列 | MERKVLALQA RKKRTKAKKD KAQRKSETQH RGSAPHSESD LPEQEEEILG SDDDEQEDPN DYCKGGYHLV KIGDLFNGRY HVIRKLGWGH FSTVWLSWDI QGKKFVAMKV VKSAEHYTET ALDEIRLLKS VRNSDPNDPN REMVVQLLDD FKISGVNGTH ICMVFEVLGH HLLKWIIKSN YQGLPLPCVK KIIQQVLQGL DYLHTKCRII HTDIKPENIL LSVNEQYIRR LAAEATEWQR SGAPPPSGSA VSTAPQPKPA DKMSKNKKKK LKKKQKRQAE LLEKRMQEIE EMEKESGPGQ KRPNKQEESE SPVERPLKEN PPNKMTQEKL EESSTIGQDQ TLMERDTEGG AAEINCNGVI EVINYTQNSN NETLRHKEDL HNANDCDVQN LNQESSFLSS QNGDSSTSQE TDSCTPITSE VSDTMVCQSS STVGQSFSEQ HISQLQESIR AEIPCEDEQE QEHNGPLDNK GKSTAGNFLV NPLEPKNAEK LKVKIADLGN ACWVHKHFTE DIQTRQYRSL EVLIGSGYNT PADIWSTACM AFELATGDYL FEPHSGEEYT RDEDHIALII ELLGKVPRKL IVAGKYSKEF FTKKGDLKHI TKLKPWGLFE VLVEKYEWSQ EEAAGFTDFL LPMLELIPEK RATAAECLRH PWLNS |
预测分子量 | 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SRPK1重组蛋白的3篇参考文献,内容涵盖重组蛋白制备、功能研究及结构分析:
1. **标题**:Structural Basis of SRPK1 Kinase Activity and Inhibition by Small Molecules
**作者**:Feng et al.
**摘要**:该研究利用大肠杆菌表达系统制备了重组人源SRPK1蛋白,并通过X射线晶体学解析了其三维结构。文章揭示了SRPK1与底物相互作用的机制,并筛选出小分子抑制剂,为癌症治疗提供了潜在靶点。
2. **标题**:Expression and Purification of Active SRPK1 Using a Baculovirus System
**作者**:Zhou et al.
**摘要**:作者通过昆虫细胞-杆状病毒系统高效表达了具有激酶活性的SRPK1重组蛋白,并优化了纯化条件。实验证明重组蛋白可磷酸化剪接因子SRSF1.验证了其在pre-mRNA剪接中的功能。
3. **标题**:SRPK1 Accelerates Tumor Angiogenesis via VEGF Splicing Regulation
**作者**:Amin et al.
**摘要**:研究通过哺乳动物细胞(HEK293)表达重组SRPK1.发现其通过调控VEGF剪接促进血管生成。体内实验表明,抑制SRPK1活性可减少肿瘤血管生成,提示其作为抗肿瘤靶点的潜力。
Serine/arginine-rich protein kinase 1 (SRPK1) is a conserved kinase that plays a critical role in regulating pre-mRNA splicing by phosphorylating serine/arginine (SR)-rich splicing factors. These SR proteins are essential for spliceosome assembly and alternative splicing decisions, influencing mRNA maturation and protein diversity. SRPK1’s activity is tightly linked to cellular processes such as cell cycle progression, signal transduction, and stress responses. Dysregulation of SRPK1 has been implicated in multiple diseases, including cancer, neurodegenerative disorders, and viral infections, making it a subject of growing research interest.
Recombinant SRPK1 proteins are engineered versions of the kinase produced in vitro using expression systems like *E. coli* or mammalian cell cultures. These proteins retain the enzymatic activity of native SRPK1 and are widely used to study phosphorylation mechanisms, screen kinase inhibitors, and analyze structural interactions. The recombinant form typically includes functional domains, such as the N-terminal kinase domain responsible for catalytic activity and the C-terminal spacer region that modulates substrate recognition. Purification tags (e.g., GST or His-tags) are often added to facilitate isolation and experimental workflows.
Research on recombinant SRPK1 has advanced our understanding of its role in pathological conditions. In cancer, SRPK1 overexpression correlates with enhanced angiogenesis, metastasis, and chemotherapy resistance by promoting pro-oncogenic splicing variants (e.g., VEGF isoforms). Inhibitors targeting SRPK1 kinase activity are being explored as potential therapeutics. Additionally, studies using recombinant SRPK1 have revealed its interaction with viral proteins, suggesting roles in viral replication. As a tool, recombinant SRPK1 bridges structural biology, drug discovery, and mechanistic studies, offering insights into both basic kinase function and therapeutic applications.
×