| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SHPK |
| Uniprot No | Q9UHJ6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-478aa |
| 氨基酸序列 | AARPITLGI DLGTTSVKAA LLRAAPDDPS GFAVLASCAR AARAEAAVES AVAGPQGREQ DVSRILQALH ECLAALPRPQ LRSVVGIGVS GQMHGVVFWK TGQGCEWTEG GITPVFEPRA VSHLVTWQDG RCSSEFLASL PQPKSHLSVA TGFGCATIFW LLKYRPEFLK SYDAAGTIHD YVVAMLCGLP RPLMSDQNAA SWGYFNTQSQ SWNVETLRSS GFPVHLLPDI AEPGSVAGRT SHMWFEIPKG TQVGVALGDL QASVYSCMAQ RTDAVLNIST SVQLAASMPS GFQPAQTPDP TAPVAYFPYF NRTYLGVAAS LNGGNVLATF VHMLVQWMAD LGLEVEESTV YSRMIQAAVQ QRDTHLTITP TVLGERHLPD QLASVTRISS SDLSLGHVTR ALCRGIVQNL HSMLPIQQLQ DWGVERVMGS GSALSRNDVL KQEVQRAFPL PMSFGQDVDA AVGAALVMLR RHLNQKES |
| 预测分子量 | 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SHPK重组蛋白的3篇参考文献示例(注：文献为虚构示例，仅作格式参考)：
1. **《高效表达与纯化重组SHPK蛋白及其酶学特性分析》**
*作者：Smith J, et al.*
摘要：研究报道了利用大肠杆菌系统表达SHPK重组蛋白的优化方法，通过亲和层析纯化获得高纯度蛋白，并证实其具有磷酸转移酶活性，为功能研究提供材料基础。
2. **《SHPK重组蛋白的晶体结构解析及其底物结合机制》**
*作者：Lee H, et al.*
摘要：通过X射线衍射解析了SHPK重组蛋白的三维结构，揭示了其活性中心的构象特征，并阐明了底物特异性结合的分子机制，为靶向药物设计提供结构依据。
3. **《SHPK重组蛋白在细胞凋亡信号通路中的功能研究》**
*作者：Zhang Y, et al.*
摘要：利用重组SHPK蛋白进行体外实验，证明其通过调节关键信号分子的磷酸化水平参与细胞凋亡调控，提示其在疾病治疗中的潜在应用价值。
(若需真实文献，建议在PubMed或Web of Science中检索“SHPK recombinant protein”或相关关键词，并筛选近期研究。)
**Background of SHPK Recombinant Protein**
SHPK (Sedoheptulokinase) is an enzyme encoded by the *SHPK* gene, which plays a critical role in the pentose phosphate pathway (PPP), a metabolic route essential for nucleotide synthesis and redox balance. SHPK catalyzes the phosphorylation of sedoheptulose to sedoheptulose-7-phosphate, a step that links the PPP to other metabolic networks, including glycolysis and amino acid metabolism. Dysregulation of SHPK activity has been implicated in metabolic disorders, immune dysfunction, and cancer, highlighting its biological and therapeutic significance.
Recombinant SHPK protein is produced using biotechnological methods, typically through the expression of the *SHPK* gene in heterologous systems like *E. coli* or mammalian cell cultures. This approach allows large-scale production of the purified enzyme for functional and structural studies. Researchers employ techniques such as codon optimization, affinity tagging, and chromatography-based purification to enhance protein yield and stability. The recombinant form retains the enzymatic activity of native SHPK, enabling in vitro assays to study substrate specificity, kinetic properties, and inhibitor screening.
Interest in SHPK recombinant protein stems from its potential applications in both basic research and drug development. It serves as a tool to investigate metabolic reprogramming in diseases, particularly cancers that rely on altered PPP flux for proliferation and survival. Additionally, SHPK inhibitors or modulators could offer novel therapeutic strategies for metabolic syndromes or malignancies. Challenges remain in optimizing recombinant SHPK for clinical translation, including ensuring proper post-translational modifications and minimizing off-target effects in complex biological systems. Ongoing studies aim to unravel its regulatory mechanisms and explore its interplay with other metabolic enzymes, paving the way for targeted interventions.
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