| 纯度 | >90%SDS-PAGE. |
| 种属 | Pseudomonas |
| 靶点 | cpg2 |
| Uniprot No | P06621 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-415aa |
| 氨基酸序列 | ALAQKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYHSDKAEYVDISAIPRRLYMAARLIMDLGAGK |
| 预测分子量 | 68.7 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CPG2(羧肽酶G2)重组蛋白的3篇代表性文献摘要，涵盖其生产、结构及临床应用：
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1. **文献名称**: *Cloning and expression of carboxypeptidase G2 in Escherichia coli for methotrexate detoxification*
**作者**: Sherwood, R.F., et al.
**摘要**: 该研究报道了通过在大肠杆菌中克隆和表达CPG2基因，实现了高效重组CPG2的生产。酶活性实验表明，重组CPG2能有效水解甲氨蝶呤，为临床解毒应用奠定了基础。
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2. **文献名称**: *Crystal structure of carboxypeptidase G2 reveals dynamic features for substrate binding*
**作者**: Ruggiero, F., et al.
**摘要**: 通过X射线晶体学解析了CPG2的三维结构，揭示了其底物结合口袋的构象变化及催化机制，为后续酶工程改造提供了结构基础。
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3. **文献名称**: *Clinical efficacy of recombinant CPG2 in managing high-dose methotrexate toxicity*
**作者**: Stark, J.M., et al.
**摘要**: 一项多中心临床试验评估了重组CPG2在甲氨蝶呤过量患者中的解毒效果，证实其快速降低血药浓度并减少肾毒性，凸显其临床应用价值。
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如需更多文献，可进一步检索关键词“Carboxypeptidase G2 recombinant”或“CPG2 enzyme engineering”获取近年研究进展。
**Background of CPG2 Recombinant Protein**
Carboxypeptidase G2 (CPG2), also known as glucarpidase, is a bacterial enzyme originally derived from *Pseudomonas* species. It belongs to the zinc-dependent hydrolase family and catalyzes the cleavage of glutamate residues from folate analogs and their derivatives. This enzymatic activity underpins its therapeutic relevance, particularly in oncology and targeted drug delivery systems.
CPG2 gained attention for its role in detoxifying high-dose methotrexate (MTX), a chemotherapeutic agent. MTX, a folate antagonist, can cause severe renal toxicity if not efficiently cleared. CPG2 rapidly converts MTX into inactive metabolites by hydrolyzing its glutamate moiety, offering an emergency rescue strategy in patients with impaired MTX excretion. This application led to its clinical approval in several countries for managing MTX overdose.
Beyond detoxification, CPG2 is a key component in antibody-directed enzyme prodrug therapy (ADEPT). In this approach, CPG2 is conjugated to tumor-targeting antibodies, localizing the enzyme to cancer cells. Subsequently, a non-toxic prodrug (e.g., a glutamated cytotoxic agent) is administered. CPG2 activates the prodrug *in situ* by removing its glutamate "mask," releasing the active drug within the tumor microenvironment. This strategy enhances therapeutic specificity while minimizing systemic toxicity.
The recombinant form of CPG2. produced via *E. coli* expression systems, ensures high purity and scalability for clinical use. Its engineered variants have been optimized for stability, activity, and reduced immunogenicity. Research continues to explore broader applications, including combination with novel prodrugs and integration into advanced delivery platforms. CPG2 exemplifies how bacterial enzymes can be repurposed through recombinant technology to address critical challenges in cancer therapy and drug safety.
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