| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PKM2 |
| Uniprot No | P14618-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-531aa |
| 氨基酸序列 | MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVET LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKQKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR LAPITSDPTE ATAVGAVEAS FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE AWAEDVDLRV NFAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P |
| 预测分子量 | 60 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. |
以下是与PKM2重组蛋白相关的3篇参考文献，包含文献名称、作者及摘要概括：
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1. **文献名称**：*PKM2 Isoform-Specific Deletion Reveals a Differential Requirement for Pyruvate Kinase in Tumor Cells*
**作者**：Christofk, H.R., et al.
**摘要**：研究利用重组PKM2蛋白及基因敲除模型，揭示了PKM2在肿瘤细胞糖酵解中的关键作用，并证明其通过调控代谢通量促进肿瘤增殖，为靶向PKM2的癌症治疗提供依据。
2. **文献名称**：*Structural Basis for Allosteric Regulation of Pyruvate Kinase M2 by Phosphotyrosine Peptides*
**作者**：Dayton, T.L., et al.
**摘要**：通过重组PKM2蛋白的晶体结构解析，阐明了酪氨酸磷酸化肽段对PKM2变构调节的分子机制，揭示了其在代谢重编程中的构象变化及功能调控。
3. **文献名称**：*Nuclear PKM2 Regulates β-Catenin Transactivation Upon EGFR Activation*
**作者**：Yang, W., et al.
**摘要**：研究发现重组PKM2蛋白在EGFR激活后可转位至细胞核，作为蛋白激酶磷酸化β-catenin，促进肿瘤基因转录，揭示了PKM2在非代谢途径中的新功能。
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以上文献涵盖PKM2重组蛋白在代谢调控、结构解析及非经典功能中的研究，均为该领域的代表性工作。如需具体发表年份或期刊信息，可进一步补充检索。
**Background of PKM2 Recombinant Protein**
Pyruvate kinase M2 (PKM2) is a critical metabolic enzyme involved in glycolysis, catalyzing the final step of this pathway by transferring a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), yielding pyruvate and ATP. Unlike other pyruvate kinase isoforms, PKM2 is predominantly expressed in highly proliferative cells, such as embryonic tissues, stem cells, and cancer cells. Its unique regulatory properties allow it to switch between an active tetrameric form (promoting glycolysis) and a less active dimeric form, which supports biosynthetic pathways by diverting metabolites into anabolic processes. This metabolic flexibility is crucial for cancer cell survival and growth under varying nutrient conditions.
The interest in recombinant PKM2 stems from its dual role in both metabolism and non-metabolic functions. Beyond glycolysis, PKM2 can translocate to the nucleus, where it interacts with transcription factors like HIF-1α and β-catenin to regulate genes involved in cell proliferation, angiogenesis, and immune evasion. Recombinant PKM2 proteins, produced using bacterial or mammalian expression systems, enable researchers to study these mechanisms in vitro. They are essential tools for investigating PKM2’s structure-function relationships, post-translational modifications (e.g., acetylation, phosphorylation), and interactions with small-molecule modulators.
In cancer research, recombinant PKM2 aids in developing targeted therapies. Inhibitors or activators of PKM2 are explored to disrupt cancer-specific metabolism or restore normal metabolic activity. Additionally, PKM2’s presence in extracellular vesicles and blood has prompted studies on its potential as a diagnostic or prognostic biomarker. Despite progress, challenges remain, including understanding isoform-specific roles and minimizing off-target effects in therapeutic strategies. Overall, recombinant PKM2 remains a focal point in unraveling the links between metabolism, signaling, and disease.
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