| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTPRM |
| Uniprot No | P28827 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 764-1452aa |
| 氨基酸序列 | MKKRKLAKKRKETMSSTRQEMTVMVNSMDKSYAEQGTNCDEAFSFMDTHNLNGRSVSSPSSFTMKTNTLSTSVPNSYYPDETHTMASDTSSLVQSHTYKKREPADVPYQTGQLHPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLCGDTSVPASQVRSLYYDMNKLDPQTNSSQIKEEFRTLNMVTPTLRVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNSG |
| 预测分子量 | 163,6 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PTPRM重组蛋白的3篇代表性文献摘要(文献标题为虚构示例，供参考)：
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1. **标题**：Structural insights into the extracellular domain of PTPRM through recombinant protein expression
**作者**：Smith A, et al.
**摘要**：本研究通过重组表达PTPRM的胞外段蛋白，利用X射线晶体学解析其三维结构，揭示了其同源二聚化机制及与细胞粘附相关的分子相互作用。
2. **标题**：Recombinant PTPRM phosphatase domain inhibits cancer cell migration in vitro
**作者**：Zhang L, et al.
**摘要**：通过大肠杆菌系统重组表达PTPRM的磷酸酶活性域，实验证明其可通过调控EGFR信号通路抑制乳腺癌细胞的迁移和侵袭能力。
3. **标题**：Functional characterization of PTPRM in synaptic plasticity using recombinant protein rescue models
**作者**：Lee J, et al.
**摘要**：在PTPRM基因敲除神经元中，回补重组表达的PTPRM蛋白可恢复突触可塑性，提示其在神经信号传导中的关键作用。
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**备注**：以上为示例性内容，实际文献需通过PubMed或Google Scholar等平台检索关键词“PTPRM recombinant protein”获取。如需具体文献，建议补充更详细的研究方向(如结构、疾病关联等)。
The receptor-type protein tyrosine phosphatase mu (PTPRM) is a member of the PTP family, which plays critical roles in regulating cellular signaling by dephosphorylating tyrosine residues on target proteins. PTPRM is a transmembrane protein characterized by an extracellular domain containing immunoglobulin-like (Ig) and fibronectin type III (FNIII) repeats, a single transmembrane region, and an intracellular catalytic domain with phosphatase activity. It mediates homophilic cell-cell adhesion through its extracellular domain, facilitating interactions with PTPRM molecules on adjacent cells. This adhesion property, coupled with its phosphatase activity, enables PTPRM to modulate signaling pathways involved in cell growth, differentiation, and tissue development. Dysregulation of PTPRM has been implicated in cancer, neurological disorders, and immune diseases, underscoring its biological significance.
Recombinant PTPRM proteins are engineered using expression systems (e.g., mammalian cells, bacteria) to produce purified, functional domains for research. These proteins often include tags (e.g., His, GST) for simplified purification and detection. Recombinant PTPRM is widely used to study its structure-function relationships, substrate specificity, and interactions with signaling partners like receptor tyrosine kinases (RTKs) or cadherins. In cancer research, it serves as a tool to explore its dual role as a tumor suppressor (via dephosphorylating oncogenic kinases) or promoter (context-dependent). Additionally, recombinant PTPRM aids in drug discovery, particularly in screening inhibitors targeting its phosphatase domain. Its extracellular domain is also utilized to investigate adhesion-mediated signaling in neural development and synaptic plasticity. By enabling precise biochemical and cellular assays, recombinant PTPRM proteins contribute to unraveling its therapeutic potential in diseases linked to tyrosine phosphorylation dysregulation.
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