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Recombinant Human SLC1A7 Protein

  • 中文名: 重组人(SLC1A7)蛋白
  • 别    名: AAAT; EAA5_HUMAN; EAAT5; Excitatory amino acid transporter 5 (retinal glutamate transporter); Excitatory amino acid transporter 5; FLJ36602; Retinal glutamate transporter; Slc1a7; Solute carrier family 1 (glutamate transporter) member 7; Solute carrier fa
货号: PAX2000-11357
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点SLC1A7
Uniprot NoO00341
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间0
活性数据MVPHAILARGRDVCRRNGLLILSVLSVIVGCLLGFFLRTRRLSPQEISYFQFPGELLMRMLKMMILPLVVSSLMSGLASLDAKTSSRLGVLTVAYYLWTTFMAVIVGIFMVSIIHPGSAAQKETTEQSGKPIMSSADALLDLIRNMFPANLVEATFKQYRTKTTPVVKSPKVAPEEAPPRRILIYGVQEENGSHVQNFALDLTPPPEVVYKSEPGTSDGMNVLGIVFFSATMGIMLGRMGDSGAPLVSFCQCLNESVMKIVAVAVWYFPFGIVFLIAGKILEMDDPRAVGKKLGFYSVTVVCGLVLHGLFILPLLYFFITKKNPIVFIRGILQALLIALATSSSSATLPITFKCLLENNHIDRRIARFVLPVGATINMDGTALYEAVAAIFIAQVNNYELDFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWALDRFRTMINVLGDALAAGIMAHICRKDFARDTGTEKLLPCETKPVSLQEIVAAQQNGCVKSVAEASELTLGPTCPHHVPVQVERDEELPAASLNHCTIQISELETNV
分子量61.6 kDa
蛋白标签GST-tag at N-terminal
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

以下为关于重组人SLC1A7(EAAT5)蛋白的参考文献示例(部分内容经概括整理,供参考):

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1. **"Cloning and functional characterization of human EAAT5 (SLC1A7) glutamate transporter"**

*Froy, O., et al. (2002)*

该研究克隆了人SLC1A7基因,并在HEK293细胞中重组表达其蛋白。结果表明,SLC1A7(EAAT5)在视网膜中高表达,同时具有谷氨酸转运和谷氨酸门控阴离子通道的双重功能,提示其在视觉信号调节中的作用。

2. **"Structural insights into the SLC1 transporter family: Implications for substrate specificity"**

*El Mestikawy, S., et al. (2015)*

本文通过生物信息学分析和重组蛋白纯化,对比了SLC1A家族成员的跨膜结构域差异,发现SLC1A7的底物结合口袋独特,可能与天冬氨酸选择性相关,为设计靶向药物提供依据。

3. **"Electrophysiological characterization of recombinant human EAAT5 in Xenopus oocytes"**

*Picaud, S., et al. (2006)*

利用非洲爪蟾卵母细胞系统表达重组SLC1A7蛋白,证实其在谷氨酸存在时触发阴离子电流,并揭示了其与视网膜双极细胞突触反馈调控的关联性。

4. **"Functional reconstitution of SLC1A7 in proteoliposomes reveals pH-dependent transport kinetics"**

*Vandenberg, R.J., et al. (2018)*

研究通过将重组SLC1A7蛋白重构至脂质体中,定量分析其谷氨酸转运活性与pH的关系,发现其在中性条件下活性最高,而在酸性微环境下抑制显著。

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**注**:以上文献摘要基于真实研究领域的代表性内容整理,具体标题/作者/年份为模拟示例。建议通过PubMed或Google Scholar以关键词 **"SLC1A7"、"EAAT5"、"recombinant"** 检索最新文献。


背景信息

The solute carrier family 1 member 7 (SLC1A7), also known as excitatory amino acid transporter 5 (EAAT5), is a transmembrane protein primarily involved in the uptake of the neurotransmitter L-glutamate. Belonging to the SLC1 family of sodium-dependent transporters, it plays a critical role in regulating extracellular glutamate concentrations, thereby maintaining synaptic transmission and preventing excitotoxicity. SLC1A7 is predominantly expressed in the retina, where it localizes to photoreceptor and bipolar cell terminals, and to a lesser extent in certain brain regions. Structurally, it contains eight transmembrane domains with intracellular N- and C-termini, and functions through a co-transport mechanism coupled with sodium and proton gradients.

As a high-affinity glutamate transporter, SLC1A7 contributes to visual signal processing by modulating photoreceptor synaptic activity. Unlike other EAATs, it exhibits an anion channel activity that modulates cellular excitability independently of transport. Its dual functionality suggests a unique regulatory role in neuronal signaling. Dysregulation of SLC1A7 has been implicated in retinal degenerative disorders and neurological conditions linked to glutamate imbalance. Recombinant SLC1A7 protein, produced via heterologous expression systems (e.g., HEK293 cells), serves as a valuable tool for studying transport kinetics, ligand interactions, and potential therapeutic targets for glutamate-related pathologies. Recent studies also explore its structural dynamics using cryo-EM to elucidate mechanisms underlying substrate specificity and ion coupling.


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