| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PDXP |
| Uniprot No | Q96GD0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-296aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMARCERLRGAALRDVLGRAQGVLFDCDGVL WNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGL RAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRAELRAAGLRLA GDPSAGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDP WHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDP ARTLMVGDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVP HYYVESIADLTEGLED |
| 预测分子量 | 34 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PDXP(Pyridoxal phosphatase)重组蛋白的示例性参考文献(文献信息为示例性概括，建议通过学术数据库查证具体文献)：
1. **"Functional characterization of human pyridoxal phosphatase (PDXP) in vitamin B6 metabolism"**
- **作者**: Smith A, et al.
- **摘要**: 研究通过重组表达PDXP蛋白，分析其催化维生素B6代谢中间产物(如吡哆醛磷酸盐)的磷酸酶活性，揭示其酶动力学参数及对细胞内维生素B6稳态的调控作用。
2. **"Structural insights into the catalytic mechanism of PDXP through X-ray crystallography"**
- **作者**: Johnson R, et al.
- **摘要**: 利用重组PDXP蛋白进行晶体结构解析，阐明其活性位点关键氨基酸残基的作用，提出PDXP催化底物去磷酸化的分子机制。
3. **"PDXP knockdown exacerbates neuronal excitability via impaired GABA synthesis"**
- **作者**: Chen L, et al.
- **摘要**: 通过体外重组PDXP蛋白实验结合细胞模型，证明PDXP活性降低会导致γ-氨基丁酸(GABA)合成障碍，进而影响神经信号传导，提示其与神经系统疾病的潜在关联。
4. **"Optimization of recombinant PDXP expression in E. coli for high-throughput screening"**
- **作者**: Wang Y, et al.
- **摘要**: 报道一种高效重组PDXP蛋白的大肠杆菌表达系统，优化纯化流程并获得高活性蛋白，用于药物筛选平台开发以靶向PDXP相关代谢疾病。
**提示**：以上文献为模拟概括，实际文献需通过PubMed、Google Scholar等平台检索关键词(如"PDXP recombinant protein"或"pyridoxal phosphatase")获取。
**Background of PDXP Recombinant Protein**
Pyridoxal phosphatase (PDXP), also known as chronophin, is a key enzyme involved in vitamin B6 metabolism. It catalyzes the dephosphorylation of pyridoxal 5'-phosphate (PLP), the bioactive form of vitamin B6. to generate pyridoxal (PL), thereby regulating intracellular PLP homeostasis. PLP serves as a cofactor for over 160 enzymatic reactions, including neurotransmitter synthesis (e.g., serotonin, dopamine), amino acid metabolism, and glycogenolysis. PDXP’s activity ensures a balance between PLP storage and utilization, critical for cellular processes in the brain, liver, and other tissues.
The recombinant PDXP protein is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, to achieve high purity and functional activity. This engineered protein retains the enzymatic properties of native PDXP, enabling researchers to study its structure, substrate specificity, and regulatory mechanisms. Its recombinant form is particularly valuable for *in vitro* assays, structural studies (e.g., X-ray crystallography), and screening inhibitors or modulators.
PDXP has garnered attention in neurodegenerative and metabolic disease research. Dysregulation of PLP levels is linked to neurological disorders (e.g., epilepsy, Alzheimer’s disease) and metabolic imbalances. For instance, reduced PLP availability impairs neurotransmitter synthesis, potentially contributing to cognitive deficits. Recombinant PDXP facilitates investigations into these pathways and the development of therapeutic strategies targeting vitamin B6 metabolism.
Additionally, PDXP interacts with other signaling molecules, such as the actin-regulating protein cofilin, suggesting roles beyond vitamin B6 metabolism, including cytoskeletal dynamics and cell motility. This multifunctionality highlights PDXP’s broader biological significance.
In summary, recombinant PDXP protein serves as a vital tool for deciphering its physiological roles, disease associations, and potential as a drug target, bridging molecular biology and clinical research.
×
