| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTPLB |
| Uniprot No | Q6Y1H2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-254aa |
| 氨基酸序列 | AAVAATAAAKGNGGGGGRAGAGDASGTRKKKGPGPLATAYLVIYNVVMTAGWLVIAVGLV RAYLAKGSYHSLYYSIEKPLKFFQTGALLEILHCAIGIVPSSVVLTSFQVMSRVFLIWAV THSVKEVQSEDSVLLFVIAWTITEIIRYSFYTFSLLNHLPYLIKWARYTLFIVLYPMGVS GELLTIYAALPFVRQAGLYSISLPNKYNFSFDYYAFLILIMISYIPIFPQLYFHMIHQRR KILSHTEEHKKFE |
| 预测分子量 | 28,3 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. |
以下是关于PTPLB重组蛋白的示例参考文献(内容为虚构示例，实际文献请通过学术数据库查询)：
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1. **标题**: *"Cloning and Expression of Recombinant PTPLB in E. coli for Functional Characterization"*
**作者**: Smith J. et al.
**摘要**: 研究报道了在大肠杆菌系统中成功克隆并高效表达PTPLB重组蛋白，通过亲和层析纯化获得高纯度蛋白，并证实其具有酪氨酸磷酸酶活性，为后续酶学机制研究奠定基础。
2. **标题**: *"Structural Insights into PTPLB’s Role in Signal Transduction via Crystallography"*
**作者**: Lee H. & Zhang R.
**摘要**: 利用重组PTPLB蛋白进行X射线晶体学分析，解析其三维结构，揭示了活性位点关键氨基酸残基，并探讨了其在细胞信号转导通路中的潜在调控机制。
3. **标题**: *"PTPLB Recombinant Protein as a Therapeutic Target in Metabolic Disorders"*
**作者**: Garcia M. et al.
**摘要**: 研究通过昆虫细胞表达系统制备PTPLB重组蛋白，发现其与胰岛素受体相互作用，可能参与代谢调节，提示其作为糖尿病治疗靶点的潜力。
4. **标题**: *"Optimization of PTPLB Expression in Mammalian Cells for Drug Screening"*
**作者**: Wang T. et al.
**摘要**: 开发了哺乳动物细胞表达体系(如HEK293)生产功能性PTPLB重组蛋白，验证其在高通量药物筛选中的应用，筛选出小分子抑制剂并评估其活性。
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**注**：以上文献为示例，实际研究中请通过PubMed、Web of Science等平台检索真实文献。若需具体文献，建议提供PTPLB的全称或相关研究领域以缩小范围。
PTPLB (Protein Tyrosine Phosphatase-Like Protein B) is a recombinant protein engineered to mimic or modulate specific enzymatic activities associated with tyrosine phosphatases, a class of enzymes critical for regulating cellular signaling pathways. These proteins are pivotal in controlling processes like cell growth, differentiation, and apoptosis by dephosphorylating tyrosine residues on target proteins. PTPLB, often designed for research or therapeutic applications, is typically derived from bacterial or eukaryotic expression systems (e.g., E. coli, mammalian cells) to ensure proper folding and post-translational modifications. Its "phosphatase-like" designation suggests structural or functional homology to natural phosphatases but may lack full enzymatic activity, serving instead as a competitive inhibitor, substrate trap, or molecular tool to study phosphatase interactions.
Interest in PTPLB stems from its potential role in diseases linked to dysregulated phosphorylation, such as cancer, diabetes, and autoimmune disorders. For instance, aberrant tyrosine phosphatase activity is implicated in oncogenic signaling, making PTPLB a candidate for drug discovery or mechanistic studies. Recombinant production allows scalable, high-purity yields for biochemical assays, structural studies (e.g., X-ray crystallography), or antibody development.
Recent studies focus on optimizing PTPLB variants for enhanced stability, specificity, or reduced immunogenicity in therapeutic contexts. Challenges include maintaining functional conformation during purification and addressing off-target effects. As phosphorylation networks grow in complexity, PTPLB and similar recombinant proteins remain indispensable tools for dissecting signaling pathways and developing targeted therapies. Research continues to explore its interactions with substrates, regulatory proteins, and small-molecule inhibitors, aiming to unlock its full biomedical potential.
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