| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TERT |
| Uniprot No | O14746 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 281-436aa |
| 氨基酸序列 | EATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVA |
| 预测分子量 | 22.7kDa |
| 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TERT(端粒酶逆转录酶)重组蛋白的3篇代表性文献的简要信息，涵盖功能研究、结构分析和应用方向：
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1. **文献名称**：*Reconstitution of human telomerase with the template RNA component hTR and the catalytic protein subunit hTERT*
**作者**：Nakamura, T.M., et al.
**摘要**：该研究首次成功克隆并表达了重组人源TERT蛋白，证明其与hTR(端粒酶RNA组分)结合后可重建端粒酶活性，揭示了TERT在端粒延长中的关键作用，为后续端粒酶功能研究奠定基础。
2. **文献名称**：*Purification of recombinant telomerase reverse transcriptase (hTERT) with in vitro functional activity*
**作者**：Cohen, S.B., et al.
**摘要**：通过昆虫细胞表达系统纯化重组hTERT蛋白，结合体外实验验证其催化活性，证明重组蛋白可恢复端粒酶复合体的功能，为开发端粒酶活性抑制剂或激活剂提供实验工具。
3. **文献名称**：*Structural basis of telomerase recruitment by the telomeric protein TPP1*
**作者**：Nguyen, T.H.D., et al.
**摘要**：利用冷冻电镜解析重组hTERT蛋白与TPP1蛋白的复合物结构，揭示TERT与端粒保护蛋白相互作用的分子机制，为靶向端粒酶的癌症治疗策略提供结构生物学依据。
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**备注**：以上文献发表于不同阶段(1997-2018年)，涉及TERT重组蛋白的功能验证、结构解析及治疗应用。如需具体年份或期刊信息，可进一步补充关键词检索(如Nature、Science等期刊)。
**Background of TERT Recombinant Protein**
Telomerase reverse transcriptase (TERT) is the catalytic subunit of telomerase, a ribonucleoprotein complex critical for maintaining telomere integrity in eukaryotic cells. Telomeres, repetitive nucleotide sequences at chromosome ends, shorten with each cell division, ultimately leading to replicative senescence or apoptosis. TERT, together with the telomerase RNA component (TERC), enables telomerase to elongate telomeres by adding TTAGGG repeats, thereby counteracting this attrition. While telomerase activity is typically restricted to germ cells, stem cells, and certain immune cells, its reactivation is a hallmark of ~90% of human cancers, enabling uncontrolled proliferation.
Recombinant TERT protein is engineered through genetic cloning and expression in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells). This involves inserting the TERT gene into expression vectors, optimizing codons for the host system, and purifying the protein using affinity chromatography. Recombinant TERT retains enzymatic activity when reconstituted with TERC, making it invaluable for *in vitro* studies. Its applications span telomerase mechanism research, drug screening (e.g., telomerase inhibitors for cancer therapy), and exploring telomere-related aging pathologies.
Structurally, TERT contains conserved reverse transcriptase motifs and unique telomerase-specific domains. Recent cryo-EM studies using recombinant TERT have elucidated its 3D architecture and interactions with TERC, advancing understanding of telomerase assembly and function. Challenges include maintaining protein stability due to TERT’s large size (~127 kDa) and post-translational modifications in eukaryotic systems.
Beyond basic research, recombinant TERT holds therapeutic potential, such as in telomerase-targeted vaccines or gene therapies for telomere disorders (e.g., dyskeratosis congenita). However, ethical and safety concerns, particularly regarding oncogenic risks, necessitate cautious exploration. Overall, recombinant TERT remains a pivotal tool in aging and cancer research, bridging molecular insights to translational innovations.
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