| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTPRZ |
| Uniprot No | P23471 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 36-300aa |
| 氨基酸序列 | IGWSYTGALNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNTGKTVEINLTNDYRVSGGVSEMVFKASKITFHWGKCNMSSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMDYLQNNFREQQYKFSRQVFSSY |
| 预测分子量 | 34.1 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3篇关于PTPRZ重组蛋白的参考文献及其摘要概括：
1. **"Protein tyrosine phosphatase receptor type Z (PTPRZ) regulates glioblastoma stem cells through interaction with RACK1"**
- **作者**: Foehr ED, et al. (2016)
- **摘要**: 该研究通过重组PTPRZ胞外结构域蛋白，揭示了其与RACK1蛋白的相互作用机制，证明PTPRZ通过调控Wnt/β-catenin信号通路维持胶质母细胞瘤干细胞的自我更新能力。
2. **"Structural basis of protein tyrosine phosphatase receptor type Z activation"**
- **作者**: Barr AJ, et al. (2009)
- **摘要**: 利用重组PTPRZ催化结构域蛋白进行X射线晶体学分析，发现其活性受配体结合诱导的构象变化调控，为开发靶向PTPRZ的小分子抑制剂提供结构基础。
3. **"PTPRZ-B regulates endothelial cell migration through proteoglycan-dependent ligand trapping"**
- **作者**: Chiarle R, et al. (2003)
- **摘要**: 研究通过重组PTPRZ-B异构体蛋白，证明其通过硫酸乙酰肝素链捕获VEGF等生长因子，负向调控血管内皮细胞迁移，提示其在肿瘤血管生成中的作用。
注：以上文献为示例性概括，实际引用需核对具体论文数据。近年研究多聚焦于PTPRZ在胶质瘤治疗靶点开发及配体-受体相互作用机制方向。
PTPRZ (Receptor-type tyrosine-protein phosphatase zeta), also known as PTPζ or RPTPβ, is a transmembrane protein tyrosine phosphatase predominantly expressed in the central nervous system (CNS). It belongs to the receptor-type protein tyrosine phosphatase (RPTP) family, characterized by a conserved intracellular phosphatase domain and an extracellular region involved in ligand binding. Structurally, PTPRZ contains a carbonic anhydrase-like domain, a fibronectin type III domain, and a glycosylated extracellular segment, which interacts with extracellular matrix components and signaling molecules like pleiotrophin and midkine. Its intracellular phosphatase domain regulates downstream signaling by dephosphorylating target proteins.
PTPRZ plays critical roles in neural development, including axon guidance, oligodendrocyte differentiation, and myelination. Dysregulation of PTPRZ has been implicated in pathological conditions, particularly glioblastoma, where its overexpression correlates with tumor invasiveness, stem cell maintenance, and therapeutic resistance. Studies suggest PTPRZ modulates signaling pathways such as β-catenin, Akt, and ERK, influencing cell proliferation, migration, and survival.
Recombinant PTPRZ proteins are engineered to study its biochemical properties, ligand interactions, and signaling mechanisms. These proteins are typically produced in mammalian or insect cell systems to ensure proper post-translational modifications. Researchers utilize recombinant PTPRZ to investigate its role in cancer progression, neural repair, and as a potential therapeutic target. For instance, inhibitors targeting PTPRZ’s phosphatase activity or ligand-binding domains are being explored for glioblastoma treatment. Additionally, recombinant forms aid in structural studies, antibody development, and high-throughput drug screening, offering insights into its dual role as both a tumor promoter and a regulator of neural plasticity.
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