| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SSU72 |
| Uniprot No | Q9NP77 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-194aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMPSSPLRVAVVCSSNQNRSMEAHNILS KRGFSVRSFGTGTHVKLPGPAPDKPNVYDFKTTYDQMYNDLLRKDKELYT QNGILHMLDRNKRIKPRPERFQNCKDLFDLILTCEERVYDQVVEDLNSRE QETCQPVHVVNVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQ EFEEKSGRTFLHTVCFY |
| 预测分子量 | 25 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SSU72重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*SSU72 mediates RNA polymerase II transcription through its phosphatase activity*
**作者**：Jeronimo C. et al. (2018)
**摘要**：该研究揭示了SSU72作为磷酸酶调控RNA聚合酶II(RNAPII)C端域(CTD)的磷酸化状态，通过重组蛋白实验证明其通过去磷酸化Ser5-P促进转录延伸和终止，并解析了其与转录复合物的相互作用机制。
2. **文献名称**：*Structural basis of SSU72 phosphatase activity in transcription termination and cancer*
**作者**：Zhang H. et al. (2020)
**摘要**：利用重组SSU72蛋白进行结构生物学分析，发现其独特的磷酸酶活性位点构象，阐明其在转录终止中的功能，并揭示某些癌症相关突变通过破坏SSU72的结构影响RNA加工过程。
3. **文献名称**：*SSU72 interacts with polycomb repressive complex 2 to regulate cellular senescence*
**作者**：Li Y. et al. (2021)
**摘要**：通过重组SSU72蛋白与表观调控复合物的体外结合实验，证明SSU72通过去磷酸化H3K36me3标记与多梳抑制复合物(PRC2)互作，调控细胞衰老相关基因的表达及端粒稳定性。
(注：以上文献为示例，实际引用需根据具体研究补充完整信息。)
**Background of SSU72 Recombinant Protein**
SSU72 is a conserved protein phosphatase implicated in diverse cellular processes, primarily linked to transcription regulation and RNA polymerase II (RNAP II) activity. Initially identified in yeast as a suppressor of splicing defects, SSU72 was later found to play a critical role in the transcription cycle by dephosphorylating the C-terminal domain (CTD) of RNAP II, a post-translational modification essential for transitioning between transcriptional initiation, elongation, and termination phases. This phosphatase activity positions SSU72 as a key modulator of gene expression, influencing mRNA processing, chromatin remodeling, and transcription-coupled DNA repair.
The recombinant form of SSU72 is engineered for functional studies, leveraging heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce purified, bioactive protein. Recombinant SSU72 retains enzymatic activity, enabling researchers to dissect its role in transcription dynamics, particularly its interaction with components of the mRNA capping and termination machinery. Structural analyses reveal that SSU72 adopts a dual-specificity phosphatase fold, with a unique substrate-binding pocket that accommodates phosphorylated serine residues in the RNAP II CTD.
Interest in SSU72 extends to its potential involvement in disease. Dysregulation of SSU72 has been associated with developmental defects, cancer, and neurodegenerative disorders, likely due to disrupted transcriptional fidelity. For example, SSU72 overexpression or mutations may alter cell cycle progression or stress responses, contributing to oncogenesis. Recombinant SSU72 proteins are thus valuable tools for drug screening, aiming to target transcription-related pathologies.
Current research focuses on elucidating SSU72’s regulatory networks, including its interplay with other phosphatases (e.g., FCP1) and transcription elongation factors. The development of recombinant SSU72 has accelerated mechanistic studies, offering insights into its bifunctional roles—acting both as a phosphatase and a putative transcription factor—and its broader impact on cellular homeostasis.
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