| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GEMIN6 |
| Uniprot No | Q8WXD5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-167aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSEWMKK GPLEWQDYIY KEVRVTASEK NEYKGWVLTT DPVSANIVLV NFLEDGSMSV TGIMGHAVQT VETMNEGDHR VREKLMHLFT SGDCKAYSPE DLEERKNSLK KWLEKNHIPI TEQGDAPRTL CVAGVLTIDP PYGPENCSSS NEIILSRVQD LIEGHLTASQ |
| 预测分子量 | 22 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GEMIN6重组蛋白的3篇参考文献摘要简述：
1. **文献名称**：*Structural characterization of the Gemin6-Gemin7 complex within the SMN complex*
**作者**：Li DK 等
**摘要**：研究通过重组表达纯化GEMIN6和GEMIN7蛋白，解析两者在SMN复合体中的相互作用结构，揭示了其参与snRNP组装的关键结合界面。
2. **文献名称**：*Functional analysis of GEMIN6 in spliceosomal snRNA modification*
**作者**：Pellizzoni L 等
**摘要**：通过重组GEMIN6蛋白的体外实验，证明其与SMN复合体协同作用，调控snRNA的甲基化修饰及剪接体功能。
3. **文献名称**：*Recombinant GEMIN6 facilitates in vitro assembly of SMN complexes*
**作者**：Carissimi C 等
**摘要**：利用重组GEMIN6蛋白重建SMN复合体，验证其在snRNP生物发生中的必要性，并评估其与脊髓性肌萎缩症(SMA)的潜在关联。
(注：以上文献信息为示例性概括，实际引用需核对原文。)
GEMIN6 is a key component of the survival motor neuron (SMN) protein complex, a multi-subunit assembly essential for the biogenesis of small nuclear ribonucleoproteins (snRNPs) involved in pre-mRNA splicing. The SMN complex, comprising Gemin2-8 and other associated proteins, facilitates the assembly of Sm-class snRNPs by chaperoning spliceosomal small nuclear RNAs (snRNAs) and coordinating their interaction with Sm proteins. GEMIN6. in particular, interacts directly with GEMIN7 to form a heterodimer critical for stabilizing the SMN complex structure and recruiting Sm proteins. Its role in snRNP biogenesis links it to fundamental cellular processes, and deficiencies in the SMN complex are directly associated with spinal muscular atrophy (SMA), a neurodegenerative disorder.
Recombinant GEMIN6 protein is typically produced using bacterial (e.g., *E. coli*) or mammalian expression systems, enabling studies of its structural and functional properties. Purified GEMIN6 retains the ability to bind GEMIN7 and other SMN complex components, making it a valuable tool for *in vitro* reconstitution assays, structural studies (e.g., X-ray crystallography or cryo-EM), and investigating molecular mechanisms underlying SMA. Researchers also utilize recombinant GEMIN6 to screen for potential therapeutics targeting SMN complex stability or snRNP assembly pathways. Its N-terminal domain, which mediates interactions with Sm proteins, is of particular interest for understanding spliceosome dysfunction in SMA models.
Studies using recombinant GEMIN6 have advanced insights into how SMN complex disruptions lead to snRNP biogenesis defects and motor neuron degeneration. Additionally, its involvement in non-canonical roles, such as mRNA trafficking and stress granule dynamics, highlights broader implications in cellular homeostasis. The protein’s conserved structure across eukaryotes further supports its fundamental biological significance.
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