| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SYMPK |
| Uniprot No | Q92797 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1274aa |
| 氨基酸序列 | MASGSGDSVTRRSVASQFFTQEEGPGIDGMTTSERVVDLLNQAALITNDSKITVLKQVQELIINKDPTLLDNFLDEIIAFQADKSIEVRKFVIGFIEEACKRDIELLLKLIANLNMLLRDENVNVVKKAILTMTQLYKVALQWMVKSRVISELQEACWDMVSAMAGDIILLLDSDNDGIRTHAIKFVEGLIVTLSPRMADSEIPRRQEHDISLDRIPRDHPYIQYNVLWEEGKAALEQLLKFMVHPAISSINLTTALGSLANIARQRPMFMSEVIQAYETLHANLPPTLAKSQVSSVRKNLKLHLLSVLKHPASLEFQAQITTLLVDLGTPQAEIARNMPSSKDTRKRPRDDSDSTLKKMKLEPNLGEDDEDKDLEPGPSGTSKASAQISGQSDTDITAEFLQPLLTPDNVANLVLISMVYLPEAMPASFQAIYTPVESAGTEAQIKHLARLMATQMTAAGLGPGVEQTKQCKEEPKEEKVVKTESVLIKRRLSAQGQAISVVGSLSSMSPLEEEAPQAKRRPEPIIPVTQPRLAGAGGRKKIFRLSDVLKPLTDAQVEAMKLGAVKRILRAEKAVACSGAAQVRIKILASLVTQFNSGLKAEVLSFILEDVRARLDLAFAWLYQEYNAYLAAGASGSLDKYEDCLIRLLSGLQEKPDQKDGIFTKVVLEAPLITESALEVVRKYCEDESRTYLGMSTLRDLIFKRPSRQFQYLHVLLDLSSHEKDKVRSQALLFIKRMYEKEQLREYVEKFALNYLQLLVHPNPPSVLFGADKDTEVAAPWTEETVKQCLYLYLALLPQNHKLIHELAAVYTEAIADIKRTVLRVIEQPIRGMGMNSPELLLLVENCPKGAETLVTRCLHSLTDKVPPSPELVKRVRDLYHKRLPDVRFLIPVLNGLEKKEVIQALPKLIKLNPIVVKEVFNRLLGTQHGEGNSALSPLNPGELLIALHNIDSVKCDMKSIIKATNLCFAERNVYTSEVLAVVMQQLMEQSPLPMLLMRTVIQSLTMYPRLGGFVMNILSRLIMKQVWKYPKVWEGFIKCCQRTKPQSFQVILQLPPQQLGAVFDKCPELREPLLAHVRSFTPHQQAHIPNSIMTILEASGKQEPEAKEAPAGPLEEDDLEPLTLAPAPAPRPPQDLIGLRLAQEKALKRQLEEEQKLKPGGVGAPSSSSPSPSPSARPGPPPSEEAMDFREEGPECETPGIFISMDDDSGLTEAALLDSSLEGPLPKETAAGGLTLKEERSPQTLAPVGEDAMKTPSPAAEDAREPEAKGNS |
| 预测分子量 | 141,1 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SYMPK重组蛋白的3篇文献示例(注：文献为虚构示例，仅供参考)：
1. **文献名称**：*Structural and functional insights into SYMPK-mediated mRNA polyadenylation*
**作者**：Chen L, et al.
**摘要**：本研究利用重组SYMPK蛋白解析其与CPSF复合体的相互作用机制，揭示了SYMPK在哺乳动物细胞mRNA 3'端加工中的关键结构域，为靶向转录后调控的疾病治疗提供理论依据。
2. **文献名称**：*Recombinant SYMPK enhances in vitro transcription termination efficiency*
**作者**：Wang X, et al.
**摘要**：通过体外重建实验，证明重组SYMPK蛋白可通过结合RNA聚合酶II调控转录终止，其磷酸化修饰对功能活性具有显著影响，为基因表达调控研究提供新模型。
3. **文献名称**：*SYMPK knockdown and recombinant rescue in epithelial junction formation*
**作者**：Müller R, et al.
**摘要**：利用重组SYMPK蛋白恢复缺失细胞模型的细胞间连接功能，证实SYMPK不仅参与mRNA加工，还通过调控紧密连接蛋白维持上皮细胞极性，提示其在癌症转移中的潜在作用。
(注：以上文献及摘要均为模拟内容，实际研究中请查阅真实数据库如PubMed获取准确信息。)
SYMPK (Symplekin) is a multifunctional scaffold protein implicated in eukaryotic RNA processing and transcriptional regulation. Initially identified as a component of the mammalian polyadenylation complex, it plays a critical role in mRNA 3′-end formation by bridging cleavage and polyadenylation specificity factor (CPSF) and cleavage stimulation factor (CstF). Structurally, SYMPK contains conserved N-terminal helices and a C-terminal domain that facilitates protein-protein interactions. Beyond mRNA maturation, SYMPK localizes to the cytoplasm and nucleus, participating in histone mRNA 3′-end processing and serving as a transcriptional coactivator in Wnt/β-catenin signaling pathways. Its dysregulation has been linked to cancers, developmental defects, and immune disorders.
Recombinant SYMPK protein is engineered for in vitro studies to dissect its molecular mechanisms. Typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., HEK293 cells), the recombinant protein retains functional domains necessary for binding CPSF, CstF, or other partners. Purification often involves affinity tags (e.g., His-tag, GST) followed by chromatography. Researchers utilize recombinant SYMPK to reconstitute polyadenylation complexes, map interaction interfaces, or screen inhibitors targeting its oncogenic roles. It also aids structural studies (e.g., crystallography, cryo-EM) to resolve its conformational dynamics during RNA processing. Additionally, SYMPK variants are explored as biomarkers in cancer diagnostics. Its recombinant form thus serves as a versatile tool for both basic research and therapeutic development.
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