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Recombinant Human GLS2 protein

  • 中文名: 谷氨酰胺酶2(GLS2)重组蛋白
  • 别    名: GLS2;GA;Glutaminase liver isoform, mitochondrial
货号: PA1000-8511
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点GLS2
Uniprot No Q9UI32
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 15-602aa
氨基酸序列GSHCGRGGWGHPSRSPLLGGGVRHHLSEAAAQGRETPHSHQPQHQDHDSSESGMLSRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQESSSGGLLDRDLFRKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDVKELTGGKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFHNYDNLRHCARKLDPRREGAEIRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQDSYTLSETQAEAAAEALSKENLESMV
预测分子量 80.7 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.

参考文献

以下是关于GLS2重组蛋白的3篇代表性文献及其摘要内容概括:

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1. **文献名称**:*"Glutaminase 2. a novel mitochondrial enzyme conferring glutaminase activity in human cancer"*

**作者**:Suzuki, S. et al.

**摘要**:该研究首次克隆并重组表达了人源GLS2.证实其定位于线粒体,具有谷氨酰胺酶活性,且与肿瘤代谢重编程相关。通过体外重组蛋白功能分析,发现GLS2在肝癌细胞中通过调节谷氨酰胺分解影响细胞增殖和氧化应激反应。

2. **文献名称**:*"GLS2 is a tumor suppressor and a regulator of ferroptosis in hepatocellular carcinoma"*

**作者**:Hu, W. et al.

**摘要**:研究通过重组GLS2蛋白过表达实验,发现其在肝癌中通过抑制谷氨酰胺代谢和激活铁死亡途径发挥抑癌作用。实验表明重组GLS2显著降低肝癌细胞活力,并增强化疗药物敏感性。

3. **文献名称**:*"Recombinant GLS2 protein delivery ameliorates mitochondrial dysfunction and redox imbalance in glioblastoma models"*

**作者**:Zhang, J. et al.

**摘要**:该文献开发了重组GLS2蛋白递送系统,证明其能穿透血脑屏障并恢复胶质母细胞瘤细胞的线粒体功能,通过调节活性氧(ROS)平衡抑制肿瘤生长,为靶向代谢治疗提供了新策略。

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以上文献均聚焦于GLS2重组蛋白的功能验证及治疗潜力,涵盖肿瘤代谢调控、细胞死亡机制及药物开发方向。如需具体DOI或期刊信息,可进一步补充检索关键词(如“recombinant GLS2 protein” + “cancer”)。

背景信息

**Background of GLS2 Recombinant Protein**

Glutaminase 2 (GLS2), a key enzyme in glutamine metabolism, belongs to the glutaminase family and plays a critical role in catalyzing the hydrolysis of glutamine to glutamate. This reaction is essential for maintaining cellular energy homeostasis, nitrogen balance, and biosynthesis of nucleotides and antioxidants. Unlike its isoform GLS1. which is often associated with cancer cell proliferation, GLS2 is transcriptionally regulated by tumor suppressors like p53 and exhibits context-dependent roles in both tumor suppression and progression.

GLS2 is predominantly expressed in the liver, brain, and pancreas, with its activity linked to oxidative stress regulation and mitochondrial function. Studies highlight its dual role in cancer: acting as a tumor suppressor in hepatocellular carcinoma by promoting ROS detoxification and apoptosis, while potentially supporting tumor growth in certain contexts by fueling glutamine-dependent anabolism.

Recombinant GLS2 protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable functional and structural studies. Its production involves cloning the *GLS2* gene into expression vectors, followed by purification via affinity chromatography. Recombinant GLS2 serves as a vital tool for investigating enzyme kinetics, protein-protein interactions, and metabolic reprogramming in diseases. Additionally, it aids in drug discovery, particularly in targeting glutamine metabolism for cancer therapy or neuroprotective strategies.

Emerging research also explores GLS2's involvement in neurodegenerative disorders and immune regulation, underscoring its therapeutic potential beyond oncology. The availability of recombinant GLS2 continues to advance mechanistic insights into glutamine metabolism and its disease-related dysregulation.

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