| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPST2 |
| Uniprot No | O60704 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-377aa |
| 氨基酸序列 | ADPQQVLECRAVLAGLRSPRGAMRPEQEELVMVGTNHVEYRYGKAMPLIF VGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWSKSGREKLR LDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLSRL FPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMY AQCMEVGKEKCLPVYYEQLVLHPRRSLKLILDFLGIAWSDAVLHHEDLIG KPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPGDVVRDMAQIAPMLAQ LGYDPYANPPNYGNPDPFVINNTQRVLKGDYKTPANLKGYFQVNQNSTSS HLGSSHHHHHH |
| 预测分子量 | 40 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TPST2重组蛋白的假设性参考文献示例，涵盖其克隆表达、功能分析及结构研究：
---
1. **文献名称**：*Cloning and Functional Characterization of Recombinant Human TPST2 in Escherichia coli*
**作者**：Zhang Y, et al.
**摘要**：本研究成功克隆了人源TPST2基因，并利用大肠杆菌表达系统实现了重组蛋白的高效表达。通过亲和层析纯化获得高纯度TPST2.体外酶活实验证实其对纤维蛋白原样底物具有特异性磺酸化活性，为后续功能研究奠定基础。
---
2. **文献名称**：*TPST2-Mediated Tyrosine Sulfation Regulates Thyroid Hormone Bioavailability*
**作者**：Smith JL, et al.
**摘要**：研究通过重组TPST2蛋白验证了其在甲状腺激素前体磺酸化中的关键作用。体外实验表明，TPST2缺失会导致激素活性显著降低，提示其与甲状腺功能异常的潜在关联。
---
3. **文献名称**：*Crystal Structure of TPST2 Reveals Substrate Recognition Mechanism*
**作者**：Johnson R, et al.
**摘要**：利用重组TPST2蛋白进行X射线晶体学分析，解析了其与底物类似物复合物的三维结构，揭示了催化口袋中关键氨基酸残基的作用，为设计靶向抑制剂提供结构依据。
---
4. **文献名称**：*Optimizing Recombinant TPST2 Production in Mammalian Cells for Therapeutic Screening*
**作者**：Lee H, et al.
**摘要**：通过优化CHO细胞表达条件(如载体构建、培养参数)，显著提升TPST2重组蛋白的产量和稳定性，验证其适用于高通量药物筛选平台。
---
注：以上文献为示例，实际引用需根据真实研究调整。建议通过PubMed或Web of Science以“TPST2 recombinant protein”等关键词检索最新文献。
**Background of TPST2 Recombinant Protein**
Tyrosylprotein sulfotransferase 2 (TPST2) is an enzyme that catalyzes the post-translational sulfation of tyrosine residues in secretory and membrane-bound proteins. This modification, mediated in the Golgi apparatus, is critical for modulating protein-protein interactions, receptor signaling, and extracellular communication. TPST2 is one of two human TPST isoforms (TPST1 and TPST2) and shares structural similarities with other sulfotransferases, featuring conserved catalytic domains essential for transferring sulfate groups from the donor molecule 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to target proteins.
TPST2 plays a vital role in diverse physiological processes. It sulfates substrates such as adhesion molecules (e.g., PSGL-1), coagulation factors (e.g., factor VIII), and chemokine receptors, influencing leukocyte trafficking, hemostasis, and immune responses. Dysregulation of TPST2 activity has been linked to diseases, including congenital hypothyroidism and immunodeficiency syndromes. For instance, TPST2 mutations impair sulfation of thyroid-stimulating hormone receptor (TSHR), disrupting its function and leading to hormonal imbalances.
Recombinant TPST2 protein is engineered for research and therapeutic applications. Produced via heterologous expression systems (e.g., mammalian or insect cells), it retains enzymatic activity and enables studies on sulfation mechanisms, substrate specificity, and disease-related mutations. Its applications span drug discovery, enzyme kinetics analysis, and structural biology, aiding in the development of sulfation-targeted therapies. Additionally, recombinant TPST2 serves as a tool to explore sulfation's role in pathogen-host interactions, cancer metastasis, and inflammatory diseases.
In summary, TPST2 recombinant protein provides a versatile platform to dissect tyrosine sulfation's biological significance and harness its potential in biomedical research and therapeutic innovation.
×
