纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | PTH1R |
Uniprot No | Q03431 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 27-188aa |
氨基酸序列 | DADDVMTKEEQIFLLHRAQAQCEKRLKEVLQRPASIMESDKGWTSASTSG KPRKDKASGKLYPESEEDKEAPTGSRYRGRPCLPEWDHILCWPLGAPGEV VAVPCPDYIYDFNHKGHAYRRCDRNGSWELVPGHNRTWANYSECVKFLTN ETREREVFDRLG |
预测分子量 | 20 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. |
以下是关于PTH1R重组蛋白的3-4篇代表性文献的简要概括:
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1. **文献名称**: *Structure and dynamics of the active human parathyroid hormone receptor-1*
**作者**: Zhao LH, et al.
**摘要**: 通过冷冻电镜解析了人源PTH1R与甲状旁腺激素类似物结合的复合物结构,揭示了受体胞外结构域与配体结合的分子机制,并阐明了其跨膜结构域激活的构象变化。
2. **文献名称**: *PTH1R interaction with arrestin mediates biased signaling in bone development*
**作者**: Gidon A, et al.
**摘要**: 研究利用重组PTH1R蛋白和细胞模型,阐明了PTH1R通过选择性招募β-arrestin(而非G蛋白)传递信号,调控骨形成的偏置信号传导机制,为骨质疏松治疗提供新思路。
3. **文献名称**: *Allosteric modulation of PTH1R by a synthetic antibody*
**作者**: Ehrenmann J, et al.
**摘要**: 设计了一种合成抗体作为PTH1R的变构调节剂,通过重组受体蛋白实验证实其可增强PTH的结合能力并延长下游cAMP信号,为开发长效PTH类似物奠定基础。
4. **文献名称**: *Mechanism of PTH hypocalcemia in familial hypocalciuric hypercalcemia*
**作者**: Mannstadt M, et al.
**摘要**: 利用重组PTH1R突变体研究家族性低尿钙高钙血症(FHH)的致病机制,发现特定突变导致受体对钙离子的敏感性下降,进而引发病理表型。
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以上文献涵盖了PTH1R的结构解析、信号传导机制、药物开发及疾病相关性研究。如需具体文章链接或补充,可进一步说明。
**Background of PTH1R Recombinant Protein**
The parathyroid hormone receptor 1 (PTH1R) is a class B G protein-coupled receptor (GPCR) that plays a central role in regulating calcium and phosphate homeostasis, bone metabolism, and skeletal development. It mediates the biological effects of parathyroid hormone (PTH) and parathyroid hormone-related protein (PTHrP), two critical ligands involved in maintaining mineral ion balance and tissue development. PTH1R activation triggers intracellular signaling cascades, primarily via Gαs/cyclic AMP (cAMP) and Gαq/phospholipase C (PLC) pathways, influencing bone remodeling, renal calcium reabsorption, and vitamin D synthesis.
Recombinant PTH1R protein is engineered *in vitro* using expression systems like mammalian cells (e.g., CHO or HEK293) to produce functional receptor variants for research and therapeutic applications. Its structure includes a large extracellular domain (ECD) responsible for ligand binding and a transmembrane domain that facilitates signal transduction. Studies of recombinant PTH1R have elucidated mechanisms of ligand-receptor interaction, activation dynamics, and allosteric modulation, providing insights into GPCR signaling specificity.
PTH1R dysfunction is linked to diseases such as hypercalcemia, hypocalcemia, and skeletal disorders like Jansen’s metaphyseal chondrodysplasia. Recombinant PTH1R is pivotal in drug discovery, particularly for osteoporosis treatments. For example, teriparatide (a recombinant PTH fragment) acts as an agonist to stimulate bone formation, while antagonists are explored for hypercalcemia management. Structural studies of recombinant PTH1R-ligand complexes have guided the design of biased agonists with tailored signaling profiles to enhance therapeutic efficacy and reduce side effects.
Additionally, recombinant PTH1R serves as a tool for high-throughput screening of small molecules, antibody development, and mechanistic studies of receptor trafficking and desensitization. Its application extends to understanding endocrine disorders and developing precision therapies targeting mineral metabolism pathways. Ongoing research aims to optimize recombinant PTH1R stability and activity for clinical translation, reflecting its significance in both basic science and biomedical innovation.
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