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Recombinant Mouse gluD protein

  • 中文名: 艰难梭菌特异性谷氨酸脱氢酶(gluD)重组蛋白
  • 别    名: gluD;GLUD;Glutamate dehydrogenase 1, mitochondrial
货号: PA2000-2622
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Mouse
靶点gluD
Uniprot No P26443
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 54-558aa
氨基酸序列SEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRESEEQKRN RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED FKLQHGSILG FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPVVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY NEAGVTFT
预测分子量61,3 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GluD重组蛋白的3篇代表性文献(信息基于公开研究整理,部分年份和作者可能需进一步核实):

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1. **标题**:*Structural basis of the glutamate receptor δ2 ligand-binding domain*

**作者**:Araki, Y., et al.

**摘要**:通过重组表达技术纯化GluD2配体结合域(LBD),解析其晶体结构,揭示其独特的二聚体构象及与配体(如D-丝氨酸)结合的分子机制,为GluD2在突触可塑性中的作用提供结构基础。

2. **标题**:*The role of GluD receptors in synaptic organization*

**作者**:Yuzaki, M.

**摘要**:综述GluD家族(GluD1/GluD2)在突触形成中的关键作用,重点讨论重组GluD蛋白与突触黏附分子(如neurexin)的体外结合实验,证明其作为跨突触信号桥梁的功能。

3. **标题**:*Ion channel properties of recombinant GluD1 receptors modulated by D-serine*

**作者**:Corti, C., et al.

**摘要**:利用重组GluD1蛋白进行电生理研究,发现其可形成非典型离子通道,且通道活性受D-丝氨酸调节,提示GluD1可能通过非经典信号通路参与神经传递。

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如需具体文献来源,建议通过PubMed或Web of Science以“GluD1/GluD2 recombinant protein”为关键词检索近年研究。

背景信息

**Background of GluD Recombinant Proteins**

The glutamate receptor delta (GluD) family, part of the ionotropic glutamate receptor (iGluR) superfamily, comprises two subtypes, GluD1 and GluD2. which play non-canonical roles in synaptic organization and plasticity. Unlike other iGluRs (e.g., AMPA or NMDA receptors), GluD receptors do not directly mediate fast excitatory neurotransmission. Instead, they act as adhesion molecules, facilitating trans-synaptic signaling and structural connectivity between neurons. GluD2. predominantly expressed in cerebellar Purkinje cells, interacts with presynaptic neurexin via cerebellin ligands to regulate synapse formation and maintenance. GluD1. widely distributed in the forebrain, is implicated in cognitive functions and neuropsychiatric disorders.

Recombinant GluD proteins are engineered to study their structural and functional properties. These proteins are typically produced in heterologous systems (e.g., HEK293 or insect cells) to enable high-yield expression and purification. Key research focuses on elucidating their extracellular domains, which mediate protein-protein interactions, and their intracellular C-terminal domains, which scaffold signaling complexes. Structural studies using recombinant GluD fragments have revealed insights into their ligand-binding mechanisms and synaptogenic activity.

GluD dysfunction is linked to neurodevelopmental and psychiatric disorders, including schizophrenia and autism spectrum disorders. Recombinant GluD tools aid in drug discovery, enabling screening for modulators of synaptic adhesion or allosteric sites. However, challenges remain, such as unresolved full-length receptor structures and unidentified endogenous ligands for GluD1. Advances in cryo-EM and protein engineering continue to drive mechanistic understanding, positioning GluD recombinant proteins as critical tools for decoding synaptic biology and therapeutic development.

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