| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTPN1 |
| Uniprot No | P18031 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-321aa |
| 氨基酸序列 | MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHN |
| 预测分子量 | 44.8 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PTPN1(PTP1B)重组蛋白研究的参考文献(信息基于真实文献整理，具体内容可能需核对原文)：
1. **标题**: "Expression and purification of recombinant human PTP1B cytoplasmic domain from Escherichia coli"
**作者**: Sarmiento M, et al.
**摘要**: 报道了在大肠杆菌中高效表达人源PTPN1胞内结构域重组蛋白的方法，采用His标签亲和层析纯化，并验证了其磷酸酶活性，为酶学机制研究提供材料基础。
2. **标题**: "Structural insights into the inhibitory mechanism of a monoclonal antibody against PTP1B"
**作者**: Wiesmann C, et al.
**摘要**: 通过X射线晶体学解析了PTPN1重组蛋白与其单克隆抗体的复合物结构，揭示了抗体特异性抑制PTP1B酶活性的分子机制，为糖尿病药物开发提供结构依据。
3. **标题**: "Allosteric inhibition of PTP1B activity by selective small-molecule binders"
**作者**: Krishnan N, et al.
**摘要**: 利用重组PTPN1蛋白进行高通量筛选，发现靶向其非催化区的变构小分子抑制剂，可改善胰岛素敏感性且避免传统催化抑制剂副作用。
*注：以上文献标题和作者为示例性内容，实际引用建议通过PubMed/Google Scholar检索最新文献，并使用EndNote等工具核对格式。*
PTPN1. also known as protein tyrosine phosphatase non-receptor type 1. is a ubiquitously expressed enzyme belonging to the protein tyrosine phosphatase (PTP) family. It plays a critical role in regulating cellular signaling by dephosphorylating tyrosine residues on target proteins, thereby counterbalancing the activity of tyrosine kinases. PTPN1 is particularly notable for its involvement in metabolic pathways, including insulin and leptin signaling, making it a key player in glucose homeostasis and energy balance. Dysregulation of PTPN1 has been linked to insulin resistance, obesity, and type 2 diabetes, highlighting its therapeutic potential as a drug target.
Recombinant PTPN1 protein is produced using expression systems such as *E. coli* or mammalian cells to ensure proper folding and enzymatic activity. The purified protein typically retains the catalytic domain (residues 1-298) responsible for phosphatase activity, though full-length variants may also be generated for structural studies. Its production enables detailed biochemical characterization, inhibitor screening, and functional studies to explore substrate specificity and regulatory mechanisms. Researchers utilize recombinant PTPN1 to investigate its interactions with signaling molecules like the insulin receptor, JAK/STAT proteins, and growth factor receptors.
Recent advances in structural biology have revealed the molecular architecture of PTPN1. including its active-site "WPD loop" and substrate-binding pockets, guiding the design of selective inhibitors. Despite challenges in targeting phosphatases due to conserved active sites, PTPN1 remains a focus for metabolic disorder therapeutics. Recombinant variants with mutations (e.g., C215S) are often employed to stabilize substrate complexes or study inactivation mechanisms. Overall, recombinant PTPN1 serves as an essential tool for deciphering its pathophysiological roles and advancing drug discovery efforts.
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