| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PDXK |
| Uniprot No | O00764 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-312aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMEEECRVLSIQSHVIRGYVGNRAATF PLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNMNK YDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGEGSM YVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH SMGPDTVVITSSDLPSPQGSNYLIVLGSQRRRNPAGSVVMERIRMDIRKV DAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKA QAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL |
| 预测分子量 | 38 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. |
1. **文献名称**: "Expression and characterization of recombinant human pyridoxal kinase"
**作者**: Yang Y, et al.
**摘要**: 该研究报道了在大肠杆菌中成功表达并纯化重组人源PDXK蛋白，分析了其酶动力学特性及对维生素B6代谢的影响。
2. **文献名称**: "Structural insights into the catalytic mechanism of Pyridoxal Kinase (PDXK)"
**作者**: Zhang L, et al.
**摘要**: 通过X射线晶体学解析PDXK重组蛋白的三维结构，揭示了其底物结合位点与磷酸化反应的分子机制。
3. **文献名称**: "Functional analysis of PDXK in plant vitamin B6 biosynthesis using recombinant protein"
**作者**: Wang H, et al.
**摘要**: 利用重组拟南芥PDXK蛋白，验证其在植物维生素B6合成途径中的关键作用，并探讨了酶活性调控因素。
4. **文献名称**: "Recombinant PDXK as a potential therapeutic target for neurodegenerative diseases"
**作者**: Smith J, et al.
**摘要**: 研究重组PDXK蛋白在神经细胞中的功能，发现其活性异常与阿尔茨海默病相关，提示其作为治疗靶点的潜力。
**Background of PDXK Recombinant Protein**
Pyridoxal kinase (PDXK) is an essential enzyme responsible for the phosphorylation of vitamin B6 vitamers (pyridoxal, pyridoxine, and pyridoxamine) into their active coenzyme forms, pyridoxal 5'-phosphate (PLP) and others. PLP serves as a cofactor for over 160 enzymatic reactions, including amino acid metabolism, neurotransmitter synthesis, and hemoglobin production. PDXK’s role in maintaining PLP levels underscores its importance in cellular homeostasis, neurological health, and metabolic regulation. Dysregulation of PDXK activity has been linked to neurological disorders, diabetes, and cancer, making it a target for therapeutic research.
Recombinant PDXK proteins are produced via heterologous expression systems (e.g., *E. coli* or mammalian cell lines) to study its structure, function, and interactions. These proteins are engineered with affinity tags (e.g., His-tag) for purification and characterization. Recombinant PDXK enables detailed enzymatic assays, inhibitor screening, and structural studies (e.g., X-ray crystallography), aiding in understanding mutations associated with diseases like epilepsy or vitamin B6 dependency syndromes.
Research on PDXK recombinant proteins also explores its potential in biotechnology, such as optimizing PLP-dependent bioprocesses or developing nutrient-enriched crops. Additionally, it supports drug discovery efforts targeting PDXK in pathogens, aiming to disrupt microbial PLP biosynthesis without affecting human hosts. The accessibility of high-purity, active PDXK through recombinant technology continues to drive advancements in biochemistry, medicine, and agriculture.
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