| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GGCT |
| Uniprot No | O75223 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-188aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMANSGCKDVTGPDEESFLYFAYGSNLLTER IHLRNPSAAFFCVARLQDFKLDFGNSQGKTSQTWHGGIATIFQSPGDEVW GVVWKMNKSNLNSLDEQEGVKSGMYVVIEVKVATQEGKEITCRSYLMTNY ESAPPSPQYKKIICMGAKENGLPLEYQEKLKAIEPNDYTGKVSEEIEDII KKGETQTL |
| 预测分子量 | 23 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GGCT(γ-谷氨酰环转移酶)重组蛋白的3篇代表性文献摘要示例：
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1. **文献名称**：*"Cloning, expression, and characterization of recombinant human gamma-glutamyl cyclotransferase"*
**作者**：Oakley AJ, et al.
**摘要**：本研究成功克隆了人源GGCT基因，并在大肠杆菌中实现了高效重组表达。通过亲和层析纯化获得高纯度蛋白，并证实其具有催化谷氨酰基环化反应的活性，为后续酶学机制研究奠定基础。
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2. **文献名称**：*"Crystal structure of GGCT reveals a novel enzyme mechanism in glutathione metabolism"*
**作者**：Yamada T, et al.
**摘要**：通过X射线晶体学首次解析了重组GGCT的三维结构，揭示了其独特的活性中心构象，并提出了一种新的底物识别与催化模型，为设计靶向GGCT的抑制剂提供结构依据。
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3. **文献名称**：*"GGCT overexpression promotes cancer cell proliferation via redox homeostasis"*
**作者**：Lieberman MW, et al.
**摘要**：利用重组GGCT蛋白进行功能研究，发现其在多种癌细胞中高表达，并通过调节谷胱甘肽代谢维持细胞内氧化还原稳态，提示GGCT可能成为癌症治疗的潜在靶点。
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注：以上文献信息为示例性概括，实际文献需通过PubMed/Web of Science等数据库检索确认。如需具体文献，建议提供更详细的研究方向(如疾病关联、结构或应用场景)。
GGCT (Gamma-Glutamyl Cyclotransferase) is a key enzyme involved in glutathione metabolism, playing a critical role in maintaining cellular redox homeostasis. It catalyzes the degradation of gamma-glutamyl dipeptides, converting them into 5-oxoproline and free amino acids, thereby recycling glutamate for glutathione synthesis. GGCT is ubiquitously expressed in human tissues and has been implicated in various physiological and pathological processes, including oxidative stress regulation, cell proliferation, and apoptosis.
The recombinant form of GGCT is engineered using molecular cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or mammalian cell systems to ensure proper folding and enzymatic activity. Recombinant GGCT proteins retain the native enzyme's functional properties, enabling researchers to study its biochemical mechanisms, substrate specificity, and interactions with inhibitors or modulators. Its high purity and consistency make it valuable for structural studies, such as X-ray crystallography, which have revealed insights into its catalytic site and conformational dynamics.
Recent studies highlight GGCT's potential as a therapeutic target, particularly in cancer. Overexpression of GGCT has been observed in multiple malignancies, correlating with tumor progression, chemoresistance, and poor prognosis. Inhibiting GGCT activity may disrupt glutathione metabolism in cancer cells, sensitizing them to oxidative damage. Additionally, recombinant GGCT serves as a tool for developing diagnostic biomarkers and screening anticancer compounds. Ongoing research continues to explore its role in neurodegenerative diseases and metabolic disorders, underscoring its broad biomedical relevance.
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