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Recombinant Human GRM2 Protein

  • 中文名: 重组人GRM2蛋白
  • 别    名: AMPA selective glutamate receptor 2; GLUR2; GLURB; Glutamate metabotropic receptor 2; Glutamate receptor homolog; Glutamate receptor metabotropic 2; GPRC1B; GRM2; GRM2_HUMAN; Metabotropic glutamate receptor 2
货号: PA2000-8115
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点GRM2
Uniprot NoQ14416
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-872aa
氨基酸序列MGSLLALLALLLLWGAVAEGPAKKVLTLEGDLVLGGLFPVHQKGGPAEDCGPVNEHRGIQRLEAMLFALDRINRDPHLLPGVRLGAHILDSCSKDTHALEQALDFVRASLSRGADGSRHICPDGSYATHGDAPTAITGVIGGSYSDVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFFQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFELEARARNICVATSEKVGRAMSRAAFEGVVRALLQKPSARVAVLFTRSEDARELLAASQRLNASFTWVASDGWGALESVVAGSEGAAEGAITIELASYPISDFASYFQSLDPWNNSRNPWFREFWEQRFRCSFRQRDCAAHSLRAVPFEQESKIMFVVNAVYAMAHALHNMHRALCPNTTRLCDAMRPVNGRRLYKDFVLNVKFDAPFRPADTHNEVRFDRFGDGIGRYNIFTYLRAGSGRYRYQKVGYWAEGLTLDTSLIPWASPSAGPLPASRCSEPCLQNEVKSVQPGEVCCWLCIPCQPYEYRLDEFTCADCGLGYWPNASLTGCFELPQEYIRWGDAWAVGPVTIACLGALATLFVLGVFVRHNATPVVKASGRELCYILLGGVFLCYCMTFIFIAKPSTAVCTLRRLGLGTAFSVCYSALLTKTNRIARIFGGAREGAQRPRFISPASQVAICLALISGQLLIVVAWLVVEAPGTGKETAPERREVVTLRCNHRDASMLGSLAYNVLLIALCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCVSVSLSGSVVLGCLFAPKLHIILFQPQKNVVSHRAPTSRFGSAAARASSSLGQGSGSQFVPTVCNGREVVDSTTSSL
分子量95.6 kDa
蛋白标签GST-tag at N-terminal
缓冲液0
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

以下是关于重组人GRM2蛋白的模拟参考文献示例(仅供格式参考,实际文献需通过学术数据库检索):

1. **"Expression and Functional Characterization of Recombinant Human Metabotropic Glutamate Receptor 2 (GRM2) in Mammalian Cells"**

*Authors: Tanaka K, et al.*

摘要:本研究通过HEK293细胞系统成功表达重组人GRM2蛋白,验证其与G蛋白偶联的信号传导活性,为靶向GRM2的药物筛选提供了实验模型。

2. **"Cryo-EM Structure of Human GRM2 in Complex with an Allosteric Modulator"**

*Authors: Wang L, et al.*

摘要:利用冷冻电镜技术解析了重组人GRM2蛋白与其变构调节剂结合的高分辨率结构,揭示了跨膜结构域的构象变化机制。

3. **"Optimization of GRM2 Protein Production in Baculovirus-Insect Cell System for Neuropharmacology Studies"**

*Authors: Müller R, et al.*

摘要:在昆虫细胞中优化重组人GRM2的表达和纯化工艺,获得了高纯度蛋白用于配体结合实验和神经退行性疾病相关药理学研究。

4. **"Role of GRM2 in Glutamate-Mediated Synaptic Plasticity: Insights from Recombinant Protein Models"**

*Authors: Chen X, et al.*

摘要:通过重组人GRM2的功能分析,证明其在突触可塑性和神经保护中的作用,支持其在精神分裂症治疗中的潜在应用。

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**注意**:以上文献为示例,具体研究请通过PubMed、Google Scholar等平台检索关键词(如“recombinant human GRM2”“GRM2 expression”)获取真实文献。


背景信息

The metabotropic glutamate receptor 2 (GRM2 or mGluR2) is a class C G protein-coupled receptor (GPCR) predominantly expressed in the central nervous system. It plays a critical role in modulating synaptic transmission and neuronal excitability by responding to glutamate, the primary excitatory neurotransmitter. Activation of mGluR2 via glutamate binding triggers downstream signaling pathways, primarily through Gi/o proteins, leading to inhibition of adenylate cyclase and reduced cAMP levels. This receptor is implicated in neuropsychiatric and neurodegenerative disorders, including anxiety, schizophrenia, and Parkinson’s disease, making it a therapeutic target.

Recombinant human GRM2 protein is engineered in vitro using heterologous expression systems (e.g., mammalian cells, baculovirus-infected insect cells) to produce a purified, functional form of the receptor for research. Its structure often includes extracellular ligand-binding domains and transmembrane regions to mimic native conformation. Studies using recombinant GRM2 aim to elucidate ligand-receptor interactions, allosteric modulation, and signaling mechanisms. Additionally, it serves as a tool for high-throughput drug screening and development of selective agonists/antagonists to regulate glutamatergic signaling. Advances in cryo-EM and crystallography have further leveraged recombinant GRM2 to resolve its 3D structure, enabling structure-based drug design. Current research focuses on balancing receptor activation to treat neurological conditions without disrupting homeostasis.


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