| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTPN22 |
| Uniprot No | Q9Y2R2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-179aa |
| 氨基酸序列 | MDQREILQKFLDEAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAE KPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYI ATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKEAEKRKSDYIIRTL KVKFNSVSVILAHQTSLQNLFSQITPAHF |
| 预测分子量 | 45 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PTPN22重组蛋白的3篇参考文献及其摘要内容的简要总结：
1. **"A functional variant of lymphoid tyrosine phosphatase is associated with type I diabetes"**
- **作者**: Bottini N et al.
- **摘要**: 本研究首次发现PTPN22基因的C1858T多态性与1型糖尿病等自身免疫疾病相关。通过重组蛋白实验表明，该突变导致LYP蛋白(PTPN22编码)与Csk激酶的结合能力下降，进而影响T细胞受体信号通路的负调控功能。
2. **"Structural and functional characterization of the lymphoid tyrosine phosphatase (LYP)"**
- **作者**: Cloutier JF, Veillette A
- **摘要**: 研究利用重组LYP蛋白解析其磷酸酶结构域的三维结构，并证明其通过C端结构域与Csk激酶相互作用，调控T细胞活化。重组蛋白的体外酶活实验显示，LYP对Src家族激酶的磷酸化状态具有关键调节作用。
3. **"The autoimmune disease-associated PTPN22 variant promotes calpain-mediated LYP degradation"**
- **作者**: Vang T et al.
- **摘要**: 通过表达重组野生型和突变型PTPN22蛋白，发现疾病相关突变(R620W)导致LYP蛋白稳定性降低，易被钙蛋白酶降解，从而削弱其对T细胞活化的抑制作用，揭示了该多态性影响自身免疫风险的分子机制。
4. **"PTPN22 polymorphisms in autoimmune diseases: A comprehensive review"**
- **作者**: Begovich AB et al.
- **摘要**: 综述总结了PTPN22基因多态性在类风湿性关节炎、系统性红斑狼疮等疾病中的作用，其中重组蛋白实验被用于验证突变对磷酸酶活性及免疫突触信号传导的影响，强调其在治疗靶点开发中的潜力。
这些文献涵盖了PTPN22重组蛋白在结构解析、功能机制及疾病关联中的关键研究。
The protein tyrosine phosphatase non-receptor type 22 (PTPN22) gene encodes a lymphoid-specific tyrosine phosphatase (LYP), a key regulator of immune signaling. Primarily expressed in hematopoietic cells, PTPN22 modulates T-cell receptor (TCR) signaling by dephosphorylating activating kinases like Lck and Fyn, thereby fine-tuning T-cell activation thresholds. Its structure includes an N-terminal catalytic domain and a C-terminal regulatory region with proline-rich motifs for protein-protein interactions. Notably, PTPN22 interacts with C-terminal Src kinase (CSK) to suppress early TCR signaling, maintaining immune tolerance.
A single nucleotide polymorphism (SNP) in PTPN22 (rs2476601. R620W) is strongly associated with autoimmune diseases, including rheumatoid arthritis, type 1 diabetes, and systemic lupus erythematosus. The 620W variant exhibits altered binding affinity to CSK and impaired inhibition of TCR signaling, leading to hyperactive T-cells and loss of immune tolerance. Paradoxically, this variant may confer protection against certain infections, highlighting its complex role in balancing immune defense and self-tolerance.
Recombinant PTPN22 proteins are engineered to study its enzymatic activity, structure-function relationships, and disease-associated mutations. Produced via bacterial (E. coli) or mammalian expression systems, these proteins typically retain catalytic activity and interaction domains. Purification methods often employ affinity tags (e.g., His-tag) followed by chromatography. Researchers use recombinant PTPN22 to investigate its role in autoimmune pathways, screen therapeutic compounds targeting phosphatase activity, and analyze mutation-induced functional changes. Its application extends to diagnostic assay development and personalized medicine strategies for autoimmune disorders.
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