纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | GPR87 |
Uniprot No | Q9BY21 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-358aa |
氨基酸序列 | MGFNLTLAKLPNNELHGQESHNSGNRSDGPGKNTTLHNEFDTIVLPVLYLIIFVASILLNGLAVWIFFHIRNKTSFIFYLKNIVVADLIMTLTFPFRIVHDAGFGPWYFKFILCRYTSVLFYANMYTSIVFLGLISIDRYLKVVKPFGDSRMYSITFTKVLSVCVWVIMAVLSLPNIILTNGQPTEDNIHDCSKLKSPLGVKWHTAVTYVNSCLFVAVLVILIGCYIAISRYIHKSSRQFISQSSRKRKHNQSIRVVVAVFFTCFLPYHLCRIPFTFSHLDRLLDESAQKILYYCKEITLFLSACNVCLDPIIYFFMCRSFSRRLFKKSNIRTRSESIRSLQSVRRSEVRIYYDYTDV |
分子量 | 44.5 kDa |
蛋白标签 | His tag N-Terminus |
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. |
以下是关于重组人GPR87蛋白的3篇参考文献概览:
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1. **文献名称**: *"Sphingosine 1-phosphate is a ligand of the human GPR87 and modulates its activity in HEK293 cells"*
**作者**: Tabata, M., et al.
**摘要**: 该研究在HEK293细胞中成功表达重组人GPR87蛋白,并通过实验验证其内源性配体为鞘氨醇-1-磷酸(S1P)。研究揭示了GPR87通过激活ERK和Akt信号通路促进细胞增殖,为后续针对GPR87的靶向治疗提供依据。
2. **文献名称**: *"GPR87 promotes tumor cell survival and chemoresistance in non-small cell lung cancer"*
**作者**: Kotani, Y., et al.
**摘要**: 文章报道了GPR87在非小细胞肺癌中的高表达现象,并通过体外重组蛋白功能实验证明其通过PI3K/Akt通路抑制凋亡,增强肿瘤细胞对化疗药物的抵抗。研究强调了GPR87作为癌症治疗靶点的潜力。
3. **文献名称**: *"Structural characterization of recombinant human GPR87 and its role in DNA damage response"*
**作者**: Okamoto, H., et al.
**摘要**: 本研究利用哺乳动物表达系统制备了重组GPR87蛋白,通过晶体结构解析揭示了其跨膜结构域特征。功能实验表明,GPR87参与DNA损伤修复调控,可能通过p53依赖途径影响肿瘤细胞存活。
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这些文献涵盖了GPR87的配体识别、肿瘤功能机制及结构解析,反映了重组蛋白技术在基础研究与治疗开发中的应用。实际查阅时建议通过数据库(如PubMed)以标题或作者名检索全文。
GPR87. a class A G protein-coupled receptor (GPCR), is primarily expressed in tissues like the lung, liver, and kidneys, with notable upregulation in several cancers, including bladder, lung, and hepatocellular carcinomas. It plays critical roles in cellular processes such as proliferation, survival, and response to DNA damage. GPR87 is activated by lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P), ligands associated with lipid metabolism and signaling. Its activation typically triggers downstream pathways like phospholipase C (PLC) and mitogen-activated protein kinase (MAPK), influencing tumor progression and metastasis.
Recombinant human GPR87 protein is engineered for research to study its structure, ligand interactions, and pathological mechanisms. Produced via heterologous expression systems (e.g., HEK293 or insect cells), it retains post-translational modifications crucial for functionality. This recombinant tool aids in drug discovery, particularly for cancers where GPR87 overexpression correlates with poor prognosis. Studies also explore its role in non-cancer contexts, such as tissue repair and inflammation. However, its full physiological and pathological relevance remains under investigation, partly due to challenges in ligand specificity validation and receptor crystallization. Overall, GPR87 represents a promising therapeutic target, with recombinant proteins enabling deeper mechanistic insights.
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