| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRPSAP2 |
| Uniprot No | O60256 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-369aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMFCVTPP ELETKMNITK GGLVLFSANS NSSCMELSKK IAERLGVEMG KVQVYQEPNR ETRVQIQESV RGKDVFIIQT VSKDVNTTIM ELLIMVYACK TSCAKSIIGV IPYFPYSKQC KMRKRGSIVS KLLASMMCKA GLTHLITMDL HQKEIQGFFN IPVDNLRASP FLLQYIQEEI PDYRNAVIVA KSPASAKRAQ SFAERLRLGI AVIHGEAQDA ESDLVDGRHS PPMVRSVAAI HPSLEIPMLI PKEKPPITVV GDVGGRIAII VDDIIDDVDS FLAAAETLKE RGAYKIFVMA THGLLSSDAP RRIEESAIDE VVVTNTIPHE VQKLQCPKIK TVDISMILSE AIRRIHNGES MSYLFRNIGL DD |
| 预测分子量 | 43 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PRPSAP2重组蛋白研究的模拟参考文献示例(注：部分内容为假设性概括，实际文献需通过学术数据库核实)：
---
1. **文献名称**: *"Functional characterization of PRPSAP2 in hepatocellular carcinoma through recombinant protein expression"*
**作者**: Li X, Wang Y, Zhang H
**摘要**: 本研究通过在大肠杆菌中表达并纯化重组PRPSAP2蛋白，分析了其在肝癌细胞中的功能。实验表明，PRPSAP2重组蛋白能够增强磷酸核糖焦磷酸(PRPP)合成酶的活性，并促进肝癌细胞的增殖和代谢重编程。
---
2. **文献名称**: *"Structural insights into PRPSAP2 and its interaction with PRPS1"*
**作者**: Smith J, Brown K, Lee S
**摘要**: 作者利用昆虫细胞系统表达重组PRPSAP2蛋白，通过X射线晶体学解析其三维结构，并揭示了PRPSAP2与PRPS1(PRPP合成酶)的相互作用界面，为靶向嘌呤代谢通路的药物设计提供依据。
---
3. **文献名称**: *"PRPSAP2 as a potential therapeutic target in colorectal cancer: Evidence from recombinant protein-based screening"*
**作者**: Chen L, Gupta R, Kim M
**摘要**: 该研究通过重组PRPSAP2蛋白的高通量药物筛选，发现小分子抑制剂可阻断其与PRPP合成酶的结合，从而抑制结直肠癌细胞的嘌呤合成和生长，提示PRPSAP2可能成为癌症治疗新靶点。
---
4. **文献名称**: *"Recombinant PRPSAP2 expression in HEK293 cells and its role in metabolic disorders"*
**作者**: Müller T, Schmidt D
**摘要**: 研究在HEK293细胞中过表达重组PRPSAP2蛋白，发现其异常表达与尿酸代谢紊乱相关，可能通过调控PRPP合成影响嘌呤代谢通路，为代谢疾病机制研究提供新方向。
---
建议通过PubMed、Web of Science等平台以“PRPSAP2 recombinant”“PRPSAP2 expression”为关键词检索最新文献。如需实际文献支持，可提供更具体的研究方向以便进一步筛选。
**Background of PRPSAP2 Recombinant Protein**
PRPSAP2 (phosphoribosyl pyrophosphate synthetase-associated protein 2) is a protein encoded by the *PRPSAP2* gene, which is evolutionarily conserved and primarily associated with nucleotide metabolism. It interacts with phosphoribosyl pyrophosphate synthetase (PRPS), a key enzyme in the de novo biosynthesis of purines and pyrimidines. PRPSAP2 is believed to modulate PRPS activity, potentially influencing cellular nucleotide pools, energy homeostasis, and pathways linked to cell proliferation. Dysregulation of nucleotide metabolism is implicated in various pathologies, including metabolic disorders, neurodevelopmental conditions, and cancers, positioning PRPSAP2 as a molecule of interest in biomedical research.
Recombinant PRPSAP2 protein is engineered through molecular cloning techniques, where the *PRPSAP2* gene is expressed in heterologous systems such as *E. coli*, yeast, or mammalian cells. This allows large-scale production of the protein with high purity, often facilitated by affinity tags (e.g., His-tag) for simplified purification. The recombinant form retains functional properties, enabling in vitro studies to dissect its biochemical interactions, structural features, and regulatory roles in nucleotide metabolism.
Research on PRPSAP2 recombinant protein has provided insights into its potential as a diagnostic or therapeutic target. For instance, altered PRPSAP2 expression has been observed in certain cancers, suggesting a role in tumorigenesis. Additionally, its involvement in metabolic pathways highlights relevance in disorders like Lesch-Nyhan syndrome or mitochondrial diseases. Recombinant PRPSAP2 also serves as a tool for antibody development, enzyme activity assays, and high-throughput drug screening. Despite progress, mechanistic details of its regulatory functions and therapeutic potential remain under investigation, warranting further studies to explore its clinical applications.
×
