| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PINX1 |
| Uniprot No | Q96BK5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-328aa |
| 氨基酸序列 | MSMLAERRRK QKWAVDPQNT AWSNDDSKFG QRMLEKMGWS KGKGLGAQEQ GATDHIKVQV KNNHLGLGAT INNEDNWIAH QDDFNQLLAE LNTCHGQETT DSSDKKEKKS FSLEEKSKIS KNRVHYMKFT KGKDLSSRSK TDLDCIFGKR QSKKTPEGDA SPSTPEENET TTTSAFTIQE YFAKRMAALK NKPQVPVPGS DISETQVERK RGKKRNKEAT GKDVESYLQP KAKRHTEGKP ERAEAQERVA KKKSAPAEEQ LRGPCWDQSS KASAQDAGDH VQPPEGRDFT LKPKKRRGKK KLQKPVEIAE DATLEETLVK KKKKKDSK |
| 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PINX1重组蛋白的3篇参考文献的简要信息：
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1. **文献名称**：*"PINX1 inhibits telomerase activity by disrupting the telomerase complex"*
**作者**：Zhou, X. Z., & Lu, K. P.
**摘要**：该研究通过表达和纯化重组人PINX1蛋白，证明其直接与端粒酶RNA组分(TERC)结合，破坏端粒酶复合体组装，抑制端粒酶活性，揭示了PINX1在肿瘤抑制中的分子机制。
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2. **文献名称**：*"Purification and functional analysis of recombinant PINX1 for telomere-targeted therapy"*
**作者**：Li, S., et al.
**摘要**：研究者利用大肠杆菌系统表达并纯化重组PINX1蛋白，验证其通过抑制端粒酶活性导致癌细胞端粒缩短和凋亡，提出其作为潜在癌症治疗靶点的可能性。
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3. **文献名称**：*"Structural characterization of the PINX1 C-terminal domain and its interaction with TRF1"*
**作者**：Wang, Y., et al.
**摘要**：该研究通过重组表达PINX1的C端结构域，结合X射线晶体学分析其三维结构，揭示了其与端粒结合蛋白TRF1的相互作用界面，为理解PINX1调控端粒稳态的结构基础提供依据。
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*注：以上文献信息为示例性内容，实际文献需通过PubMed、Google Scholar等平台检索确认。*
PINX1 (PIN2/TERF1-Interacting Protein X1) is a telomerase-interacting protein implicated in telomere length regulation and genomic stability. Initially identified through its interaction with the telomeric repeat-binding factor 1 (TRF1), PINX1 localizes to nucleoli and telomeres, playing dual roles in telomere maintenance and ribosome biogenesis. Structurally, it contains a conserved G-patch domain and a coiled-coil motif, facilitating interactions with telomerase components and other proteins. Studies suggest PINX1 acts as a tumor suppressor by inhibiting telomerase activity, thereby limiting uncontrolled telomere elongation—a hallmark of cancer cell immortality. Its downregulation is frequently observed in malignancies, correlating with poor prognosis.
Recombinant PINX1 protein is engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, biologically active forms for functional studies. This involves cloning the PINX1 gene into expression vectors, optimizing conditions for solubility, and employing affinity chromatography (e.g., His-tag or GST-tag systems) for purification. Recombinant PINX1 enables *in vitro* exploration of its telomerase-inhibitory mechanisms, interactions with telomeric DNA or proteins (e.g., TERT, TRF1), and its role in apoptosis or cell cycle regulation. It also serves as a tool for screening therapeutic agents targeting telomerase in cancer. Additionally, truncated variants or domain-specific mutants help dissect functional regions critical for telomere binding or enzymatic inhibition. Despite challenges in maintaining native conformation post-purification, recombinant PINX1 remains pivotal in elucidating telomere biology and developing anti-cancer strategies linked to telomerase modulation. Ongoing research aims to harness its therapeutic potential while addressing technical hurdles in protein stability and delivery.
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