| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Pkm |
| Uniprot No | P14618 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 185-461aa |
| 氨基酸序列 | VKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTAR |
| 预测分子量 | 57.4 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3篇关于PKM重组蛋白的相关文献摘要概括(内容基于公开研究归纳，非真实文献)：
1. **《Recombinant expression and purification of human PKM2 in E. coli for metabolic studies》**
- 作者：Chen L, et al.
- 摘要：本研究报道了在大肠杆菌中高效表达并纯化人源PKM2重组蛋白的方法，通过优化密码子和诱导条件获得可溶性蛋白，并验证其酶活性，为肿瘤代谢研究提供工具。
2. **《Structural insights into the allosteric regulation of PKM1 by post-translational modifications》**
- 作者：Zhang Y, et al.
- 摘要：通过X射线晶体学解析了重组PKM1蛋白的变构调节机制，揭示了磷酸化等翻译后修饰如何影响其四聚体构象及催化活性，为代谢疾病靶点设计奠定基础。
3. **《Targeting PKM2 dimer-to-tetramer transition for cancer therapy: A high-throughput screening approach》**
- 作者：Wang H, et al.
- 摘要：利用重组PKM2蛋白开发了基于荧光共振能量转移(FRET)的筛选平台，发现小分子化合物可稳定PKM2四聚体形式，抑制肿瘤细胞 Warburg 效应，具有潜在抗癌应用。
注：以上文献名为示例性质，如需真实文献，建议在PubMed或Web of Science中检索关键词“PKM2 recombinant protein expression”或“PKM1/PKM2 metabolic regulation”。
**Background of PKM Recombinant Proteins**
Pyruvate kinase (PK) is a critical enzyme in glycolysis, catalyzing the conversion of phosphoenolpyruvate (PEP) to pyruvate while generating ATP. The PKM gene encodes two alternatively spliced isoforms, PKM1 and PKM2. which differ by a single exon. PKM1 is constitutively active and predominantly expressed in normal tissues, while PKM2. a less active isoform, is frequently upregulated in rapidly proliferating cells, particularly cancer cells. PKM2’s dynamic regulation—switching between active tetrameric and inactive dimeric forms—allows cancer cells to balance glycolytic flux with biosynthetic demands, a hallmark of the Warburg effect. This metabolic reprogramming supports tumor growth by diverting intermediates into pathways for nucleotide, lipid, and amino acid synthesis.
Recombinant PKM proteins are engineered to study isoform-specific functions, metabolic adaptations, and therapeutic targeting. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), these proteins retain structural and functional characteristics, enabling *in vitro* assays, structural studies, and drug screening. PKM2. in particular, has gained attention for its non-metabolic roles in gene regulation, kinase signaling, and interactions with oncogenic pathways (e.g., HIF-1α, STAT3). Its overexpression in tumors and secretion into extracellular vesicles also implicates it as a potential cancer biomarker.
Research on PKM recombinant proteins has advanced understanding of metabolic dysregulation in diseases and spurred development of PKM2 modulators as anticancer agents. Challenges remain in elucidating context-dependent roles and isoform-specific targeting, but ongoing studies continue to highlight PKM’s centrality in cellular metabolism and disease pathology.
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