| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTPLA |
| Uniprot No | B0YJ81 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-288aa |
| 氨基酸序列 | MGRLTEAAAAGSGSRAAGWAGSPPTLLPLSPTSPRCAATMASSDEDGTNGGASEAGEDREAPGERRRLGVLATAWLTFYDIAMTAGWLVLAIAMVRFYMEKGTHRGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVTGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVAGELLTIYAALPHVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD |
| 预测分子量 | 32,3 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条关于PTPLA重组蛋白的虚构参考文献示例(基于学术研究常见方向，非真实文献)：
1. **文献名称**: *Expression and Purification of Recombinant PTPLA in E. coli for Functional Studies*
**作者**: Zhang, L., et al.
**摘要**: 本研究报道了通过大肠杆菌表达系统高效表达和纯化重组PTPLA蛋白的优化方法，分析了其磷酸酶活性，并验证了其在体外细胞信号通路中的调控作用。
2. **文献名称**: *Structural Characterization of PTPLA Reveals a Novel Catalytic Mechanism*
**作者**: Smith, J.R., & Tanaka, K.
**摘要**: 通过X射线晶体学解析了重组PTPLA的三维结构，发现其催化结构域具有独特的活性位点构象，为开发靶向PTPLA的小分子抑制剂提供了结构基础。
3. **文献名称**: *PTPLA Knockdown Alters Lipid Metabolism in Hepatocytes: Insights from Recombinant Protein Rescue Experiments*
**作者**: Gupta, S., et al.
**摘要**: 利用重组PTPLA蛋白回补实验，证明PTPLA缺失会破坏肝细胞脂质代谢稳态，其功能可能与调控胰岛素信号通路中的酪氨酸去磷酸化相关。
(注：以上文献为示例性内容，实际研究中请参考真实数据库如PubMed、Web of Science的检索结果。)
PTPLA (Protein Tyrosine Phosphatase-Like A), also known as VPREB3 (V-set pre-B cell surrogate light chain 3), is a member of the protein tyrosine phosphatase (PTP) family. Despite its structural resemblance to classical PTPs, PTPLA lacks catalytic phosphatase activity due to the absence of critical residues in its pseudophosphatase domain. This unique feature classifies it as a "pseudophosphatase," suggesting non-enzymatic regulatory roles in cellular processes. Initially identified in pre-B cells, PTPLA is implicated in B-cell development and immune system regulation, though its precise biological mechanisms remain under investigation.
Recombinant PTPLA proteins are engineered using expression systems like *E. coli* or mammalian cells to study its structure-function relationships. These systems enable high-yield production of purified proteins for biochemical assays, structural studies (e.g., X-ray crystallography), and interaction partner screening. Recombinant PTPLA has been instrumental in identifying its binding partners, such as components of the B-cell receptor complex, shedding light on its potential role in signal transduction or protein scaffolding.
Emerging research links PTPLA to diseases, including cancers and metabolic disorders. Its overexpression in certain malignancies suggests diagnostic or therapeutic relevance. However, challenges persist in elucidating its exact physiological targets and regulatory pathways. The development of recombinant PTPLA mutants further aids in mapping functional domains and validating its inactive phosphatase status. As a non-catalytic PTP family member, PTPLA exemplifies how pseudophosphatases may evolve to serve specialized roles in cellular signaling, emphasizing the importance of recombinant protein tools in decoding their enigmatic functions.
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